Q9NQ31 Q8NBS2 Q8TAC6 Q8TAD3 Q8TAE0 BCA3_HUMAN Proline-rich protein BCA3 Breast cancer-associated gene 3 protein PKA-interacting protein AKIP1 BCA3 C11orf17 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Characterization of a novel human breast cancer associated gene (BCA3) encoding an alternatively spliced proline-rich protein. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3) TISSUE SPECIFICITY Lymph node Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene ST5) and mouse chromosome 7. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT LYS-23 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT LYS-23 Kidney A-kinase-interacting protein localizes protein kinase A in the nucleus. TISSUE SPECIFICITY SUBCELLULAR LOCATION INTERACTION WITH PRKACA Interacts with PRKACA. P17612 false 2 Nucleus. Note=Locates to punctate spots. Q9NQ31-1 1 1a Q9NQ31-2 2 Q9NQ31-3 3 1b Expressed at high levels in adult heart and at lower levels in brain, testis, ovary and skeletal muscle. Up-regulated in some breast cancer cell lines. Isoform 1 and isoform 3 are expressed in fetal brain. Alternative splicing Nucleus Polymorphism Proto-oncogene R K A T F S MDNCLAAAALNGVDRRSLQRSARLALEVLERAKRRAVDWHALERPKGCMGVLAREAPHLEKQPAAGPQRVLPGEREERPPTLSASFRTMAEFMDYTSSQCGKYYSSVPEEGGATHVYRYHRGESKLHMCLDIGNGQRKDRKKTSLGPGGSYQISEHAPEASQPAENISKDLYIEVYPGTYSVTVGSNDLTKKTHVVAVDSGQSVDLVFPV Q16821 A0AVQ2 O43476 Q75LN8 Q7KYM8 Q86UI6 PPR3A_HUMAN Protein phosphatase 1 regulatory subunit 3A Protein phosphatase 1 glycogen-associated regulatory subunit Protein phosphatase type-1 glycogen targeting subunit PPP1R3A PP1G Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A common variant in PPP1R3 associated with insulin resistance and type 2 diabetes. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2) TISSUE SPECIFICITY VARIANT INSULIN RESISTANCE TYR-905 VARIANT SER-883 Skeletal muscle The DNA sequence of human chromosome 7. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANTS VAL-451; ASN-476 AND LEU-882 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Sequence of the human glycogen-associated regulatory subunit of type I protein phosphatase and analysis of its coding region and mRNA level in muscle from patients with non-insulin-dependent diabetes. NUCLEOTIDE SEQUENCE [MRNA] OF 2-1122 (ISOFORM 1) VARIANT NIDDM GLU-931 Skeletal muscle Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-759 MASS SPECTROMETRY Epithelium A widespread amino acid polymorphism at codon 905 of the glycogen-associated regulatory subunit of protein phosphatase-1 is associated with insulin resistance and hypersecretion of insulin. VARIANT INSULIN RESISTANCE TYR-905 The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] ALA-554 Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. Interacts with PPP1CC catalytic subunit of PP1, and associates with glycogen. Membrane; Single-pass membrane protein. Q16821-1 1 Q16821-2 2 No experimental confirmation available Skeletal muscle and heart. The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes. Phosphorylation at Ser-46 by ISPK stimulates the dephosphorylation of glycogen synthase and phosphorylase kinase. Defects in PPP1R3A are a cause of susceptibility to noninsulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type II. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance. Defects in PPP1R3A are a cause of insulin resistance (Ins resistance). Contains 1 CBM21 (carbohydrate binding type-21) domain. Alternative splicing Carbohydrate metabolism Diabetes mellitus Disease mutation Glycogen metabolism Membrane Phosphoprotein Polymorphism Transmembrane GTRRVSFADSFGFNL ERTRAGACKTMERSS G S C Y M V K N G A E K H L R S D Y A E MEPSEVPSQISKDNFLEVPNLSDSLCEDEEVTFQPGFSPQPSRRGSDSSEDIYLDTPSSGTRRVSFADSFGFNLVSVKEFDCWELPSASTTFDLGTDIFHTEEYVLAPLFDLPSSKEDLMQQLQIQKAILESTESLLGSTSIKGIIRVLNVSFEKLVYVRMSLDDWQTHYDILAEYVPNSCDGETDQFSFKIVLVPPYQKDGSKVEFCIRYETSVGTFWSNNNGTNYTFICQKKEQEPEPVKPWKEVPNRQIKGCLKVKSSKEESSVTSEENNFENPKNTDTYIPTIICSHEDKEDLEASNRNVKDVNREHDEHNEKELELMINQHLIRTRSTASRDERNTFSTDPVNFPNKAEGLEKKQIHGEICTDLFQRSLSPSSSAESSVKGDFYCNEKYSSGDDCTHQPSEETTSNMGEIKPSLGDTSSDELVQLHTGSKEVLDDNANPAHGNGTMQIPCPSSDQLMAGNLNKKHEGGAKKIEVKDLGCLRRDFHSDTSACLKESTEEGSSKEDYYGNGKDDEEQRIYLGVNEKQRKNFQTILHDQERKMGNPKISVAGIGASNRDLATLLSEHTAIPTRAITADVSHSPRTNLSWEEAVLTPEHHHLTSEGSALGGITGQVCSSRTGNVLRNDYLFQVEEKSGGINSEDQDNSPQHKQSWNVLESQGKSRENKTNITEHIKGQTDCEDVWGKRDNTRSLKATTEELFTCQETVCCELSSLADHGITEKAEAGTAYIIKTTSESTPESMSAREKAIIAKLPQETARSDRPIEVKETAFDPHEGRNDDSHYTLCQRDTVGVIYDNDFEKESRLGICNVRVDEMEKEETMSMYNPRKTHDREKCGTGNITSVEESSWVITEYQKATSKLDLQLGMLPTDKTVFSENRDHRQVQELSKKTDSDAIVHSAFNSDTNRAPQNSSPFSKHHTEISVSTNEQAIAVENAVTTMASQPISTKSENICNSTREIQGIEKHPYPESKPEEVSRSSGIVTSGSRKERCIGQIFQTEEYSVEKSLGPMILINKPLENMEEARHENEGLVSSGQSLYTSGEKESDSSASTSLPVEESQAQGNESLFSKYTNSKIPYFLLFLIFLITVYHYDLMIGLTFYVLSLSWLSWEEGRQKESVKKK P38936 Q14010 Q9BUT4 CDN1A_HUMAN Cyclin-dependent kinase inhibitor 1 p21 CDK-interacting protein 1 Melanoma differentiation-associated protein 6 MDA-6 CDKN1A CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. NUCLEOTIDE SEQUENCE [MRNA] WAF1, a potential mediator of p53 tumor suppression. NUCLEOTIDE SEQUENCE [MRNA] p21 is a universal inhibitor of cyclin kinases. NUCLEOTIDE SEQUENCE [MRNA] Use of a sensitive and efficient subtraction hybridization protocol for the identification of genes differentially regulated during the induction of differentiation in human melanoma cells. NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. NUCLEOTIDE SEQUENCE [MRNA] Two variants of the CIP1/WAF1 gene occur together and are associated with human cancer. NUCLEOTIDE SEQUENCE [MRNA] VARIANT ARG-31 NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu). NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT ARG-31 The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ARG-31 Eye Lung N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1). PROTEIN SEQUENCE OF 2-16 ACETYLATION AT SER-2 Reversible phosphorylation at the C-terminal regulatory domain of p21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding. PROTEIN SEQUENCE OF 136-148 PHOSPHORYLATION AT THR-145; SER-146 AND SER-160 MASS SPECTROMETRY Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. PHOSPHORYLATION AT THR-145 MUTAGENESIS OF THR-145 AND SER-146 SUBCELLULAR LOCATION A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 MASS SPECTROMETRY Epithelium Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 139-160 May be the important intermediate by which p53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. P78396 false 1 P20248 false 1 O95067 false 1 P24385 false 2 P30281 false 1 P24864 false 3 O96020 false 1 O75419 false 1 Q99459 false 1 Q99741 false 1 O00311 false 1 P24941 false 5 P11802 false 2 Q00535 false 1 Q00534 false 1 O75496 false 1 Q7L590 false 1 O94921 false 4 Cytoplasm. Nucleus. Expressed in all adult human tissues, with 5-fold lower levels observed in the brain. By p53, mezerein (antileukemic compound) and interferon beta. Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Belongs to the CDI family. 3D-structure Acetylation Cell cycle Cytoplasm Direct protein sequencing Metal-binding Nucleus Phosphoprotein Polymorphism Protein kinase inhibitor Zinc Zinc-finger S R D G T A T D S A S D MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Q9JJR5 Q3TR76 BCA3_MOUSE Proline-rich protein BCA3 Breast cancer-associated gene 3 protein PKA-interacting protein AKIP1 Bca3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Sciurognathi Muroidea Muridae Murinae Mus Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene ST5) and mouse chromosome 7. NUCLEOTIDE SEQUENCE The transcriptional landscape of the mammalian genome. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head Thymus Interacts with PRKACA. Nucleus (By similarity). Note=Locates to punctate spots. Nucleus MEYCLAAAALNGVDRRSLQRSARLGREVLERAKRRAVDWHSPERSRGNVGVLYRQGPYQERWSVPGSQRLLGEREERCPTLSSSFGAMAEFMDYTSSQCGKYYLSMPEEGGATHVYRYHRRKPPEMHMYSDTGHSQEQRNCRGETSVGQESIYQTSEHSQESSWPTENISKDLYIEVYPGTYSVTVGSSALSKKTHVVAVDPGQSVDLVFPV Q96IZ0 O75796 Q6FHY9 Q8N700 PAWR_HUMAN PRKC apoptosis WT1 regulator protein Prostate apoptosis response 4 protein Par-4 PAWR PAR4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A novel repressor, par-4, modulates transcription and growth suppression functions of the Wilms' tumor suppressor WT1. NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH WT1 NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANTS LEU-42; ARG-78; ALA-137 AND ALA-202 Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ARG-78 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Kidney Structural and functional characterization of the upstream regulatory region of the human gene encoding prostate apoptosis response factor-4. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64 Blood Par-4 drives trafficking and activation of Fas and Fasl to induce prostate cancer cell apoptosis and tumor regression. FUNCTION IN APOPTOSIS AND TUMOR REGRESSION p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition. INTERACTION WITH SQSTM1 AND PRKCZ THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. SUBCELLULAR LOCATION INTERACTION WITH THAP1 AATF inhibits aberrant production of amyloid beta peptide 1-42 by interacting directly with Par-4. INTERACTION WITH AATF PAR-4 is involved in regulation of beta-secretase cleavage of the Alzheimer amyloid precursor protein. INTERACTION WITH BACE1 Apoptosis by Par-4 in cancer and neurodegenerative diseases. REVIEW ON FUNCTION IN APOPTOSIS AND NEURODEGENERATIVE DISEASES Par-4 inducible apoptosis in prostate cancer cells. REVIEW Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-226; SER-228; THR-229 AND SER-231 MASS SPECTROMETRY Pro-apoptopic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappaB transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1. Interacts with WT1, via the C-terminal region. Homooligomer. Interacts also with a wide variety of proteins, such as atypical PKCs, p62, DAPK3 kinase and THAP1. Interacts with actin, AATF, BACE1, SPSB1, SPSB2 AND SPSB4. Component of a ternary complex composed of SQSTM1 and PRKCZ. O43293 false 1 Cytoplasm. Nucleus. Note=Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis (By similarity). Nuclear localization includes nucleoplasm and PML nuclear bodies. Widely expressed. Expression is elevated in various neurodegenerative diseases such as amyotrophic lateral sclerosis, Alzheimer, Parkinson and Huntington diseases and stroke. Down-regulated in several cancers. By apoptosis. The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners. The SAC domain is a death-inducing domain selective for apoptosis induction in cancer cells. This domain is essential for nuclear entry, Fas activation, inhibition of NF-kappaB activity and induction of apoptosis in cancer cells. Preferentially phosphorylated at the Thr-163 by PKC in cancer cells. Apoptosis Coiled coil Cytoplasm Nucleus Phosphoprotein Polymorphism Transcription Transcription regulation P L P R G A E A AP PPAR I M R T MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANELNNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR Q9HAT0 Q9UF38 ROP1A_HUMAN Ropporin-1A Rhophilin-associated protein 1A Cancer/testis antigen 91 CT91 ROPN1 ROPN1A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning of a human sperm-specific binding protein of rhophilin and function in spermatogenesis. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) A yeast two-hybrid system using Sp17 identified ropporin as a novel cancer-testis antigen in hematologic malignancies. TISSUE SPECIFICITY POSSIBLE INTERACTION WITH SPA17 DEVELOPMENTAL STAGE IDENTIFICATION AS A CANCER/TESTIS ANTIGEN Homodimer. Interacts with AKAP3 and RHPN1 (By similarity). May interact with SPA17. Note=In the sperm tail, found in the principal piece and in the cytoplasmic droplet located at the distal end of the midpiece. Inner surface of the fibrous sheath. Q9HAT0-1 1 Q9HAT0-2 2 No experimental confirmation available Testis specific in adult. Overexpressed in hematologic tumor cells. Expressed in fetal liver. The RIIa domain mediates interaction with AKAP3. The name 'ropporin' comes from the Japanese word 'oppo' which means 'tail'. Belongs to the ropporin family. Contains 1 RIIa domain. Alternative splicing DYFEALSRGETPPVRERSER EYVLLSRLHPLEDGRRQ RVL MAQTDKPTCIPPELPKMLKEFAKAAIRVQPQDLIQWAADYFEALSRGETPPVRERSERVALCNRAELTPELLKILHSQVAGRLIIRAEELAQMWKVVNLPTDLFNSVMNVGRFTEEIEWLKFLALACSALGVTITKTLKIVCEVLSCDHNGGSPRIPFSTFQFLYTYIAKVDGEISASHVSRMLNYMEQEVIGPDGIITVNDFTQNPRVQLE Q12802 Q14572 Q59FP6 Q86W90 Q8WXQ6 Q96JP6 Q96P79 Q9Y5T0 Q9Y5T6 AKP13_HUMAN A-kinase anchor protein 13 AKAP 13 Protein kinase A-anchoring protein 13 Breast cancer nuclear receptor-binding auxiliary protein Human thyroid-anchoring protein 31 Guanine nucleotide exchange factor Lbc AKAP-Lbc LBC oncogene P47 Lymphoid blast crisis oncogene Non-oncogenic Rho GTPase-specific GTP exchange factor AKAP13 BRX HT31 LBC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6) Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3) FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH ESR1; THRA AND PPARA VARIANT SER-2457 Testis Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7) ALTERNATIVE SPLICING (ISOFORM 6) FUNCTION SUBCELLULAR LOCATION DOMAIN TISSUE SPECIFICITY Skeletal muscle ERRATUM Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) INTERACTION WITH RHOA VARIANTS CYS-574 AND SER-2457 AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH RHOA; RHOB AND RHOC MUTAGENESIS OF ALA-1251; ILE-1260 AND TYR-2153 VARIANTS VAL-624; MET-897 AND SER-2457 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS THR-452; ARG-494; CYS-574; LYS-689; ALA-845; MET-897; ALA-1062; ASN-1086 AND THR-1216 Lung The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5) Brain Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. NUCLEOTIDE SEQUENCE [MRNA] OF 754-1768 PKA AND RII BINDING MUTAGENESIS OF ALA-1265 Thyroid NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1486-2813 (ISOFORM 4) VARIANT SER-2457 Brain The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway. FUNCTION INTERACTION WITH ESR2 Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. INTERACTION WITH NME2 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1929 AND SER-1932 MASS SPECTROMETRY Epithelium A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2728 MASS SPECTROMETRY Epithelium A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. STRUCTURE BY NMR OF 493-516 Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Isoform 6 stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions. Binds cAMP-dependent protein kinase (PKA) and to the RII-alpha regulatory subunit of PKA. Interacts with ESR1, ESR2, THRA, PPARA, RHOA and NME2. Q16611 false 1 P21980 false 3 P31946 false 1 Isoform 3: Cytoplasm. Nucleus. Isoform 2: Cytoplasm. Isoform 6: Cytoplasm. Isoform 7: Membrane. Q12802-1 1 Q12802-2 2 Q12802-3 3 Q12802-4 4 Q12802-5 5 Q12802-6 6 LBC Q12802-7 7 Isoform 3 and isoform 6 are found in hematopoietic cells, skeletal muscle, lung, heart, estrogen-responsive reproductive tissues, including breast ductal epithelium. Also found in testis and breast cancer cell lines. Isoform 6 is not found in brain, placenta, liver, pancreas or kidney. Isoform 7 is expressed in myeloid and lymphoid lineages, a variety of epithelial tissues and skeletal muscle. Isoform 2 is predominantly found in the heart and at lower levels in the lung, placenta, kidney, pancreas, skeletal muscle and liver. Both the DH and PH domains are required for transforming activity. Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. 3D-structure Alternative splicing Coiled coil Cytoplasm Guanine-nucleotide releasing factor Membrane Metal-binding Nucleus Phorbol-ester binding Phosphoprotein Polymorphism Proto-oncogene Zinc Zinc-finger DAGPRETLMHFAVRLGLLRL GENLYDLQTHFKFVIFL LFF TQA MLY SMRVLGDVVRRPPIHR MSWCPSGVQYSAGLSADFNY NRDEDEGIP SGNGWRCFN M T W R R C G V E K V A V M P A D N M T G S A T A P I P A P Y F G R C R A V A T S P D A M S N H V D D G QL HV MKLNPQQAPLYGDCVVTVLLAEEDKAEDDVVFYLVFLGSTLRHCTSTRKVSSDTLETIAPGHDCCETVKVQLCASKEGLPVFVVAEEDFHFVQDEAYDAAQFLATSAGNQQALNFTRFLDQSGPPSGDVNSLDKKLVLAFRHLKLPTEWNVLGTDQSLHDAGPRETLMHFAVRLGLLRLTWFLLQKPGGRGALSIHNQEGATPVSLALERGYHKLHQLLTEENAGEPDSWSSLSYEIPYGDCSVRHHRELDIYTLTSESDSHHEHPFPGDGCTGPIFKLMNIQQQLMKTNLKQMDSLMPLMMTAQDPSSAPETDGQFLPCAPEPTDPQRLSSSEETESTQCCPGSPVAQTESPCDLSSIVEEENTDRSCRKKNKGVERKGEEVEPAPIVDSGTVSDQDSCLQSLPDCGVKGTEGLSSCGNRNEETGTKSSGMPTDQESLSSGDAVLQRDLVMEPGTAQYSSGGELGGISTTNVSTPDTAGEMEHGLMNPDATVWKNVLQGGESTKERFENSNIGTAGASDVHVTSKPVDKISVPNCAPAASSLDGNKPAESSLAFSNEETSTEKTAETETSRSREESADAPVDQNSVVIPAAAKDKISDGLEPYTLLAAGIGEAMSPSDLALLGLEEDVMPHQNSETNSSHAQSQKGKSSPICSTTGDDKLCADSACQQNTVTSSGDLVAKLCDNIVSESESTTARQPSSQDPPDASHCEDPQAHTVTSDPVRDTQERADFCPFKVVDNKGQRKDVKLDKPLTNMLEVVSHPHPVVPKMEKELVPDQAVISDSTFSLANSPGSESVTKDDALSFVPSQKEKGTATPELHTATDYRDGPDGNSNEPDTRPLEDRAVGLSTSSTAAELQHGMGNTSLTGLGGEHEGPAPPAIPEALNIKGNTDSSLQSVGKATLALDSVLTEEGKLLVVSESSAAQEQDKDKAVTCSSIKENALSSGTLQEEQRTPPPGQDTQQFHEKSISADCAKDKALQLSNSPGASSAFLKAETEHNKEVAPQVSLLTQGGAAQSLVPPGASLATESRQEALGAEHNSSALLPCLLPDGSDGSDALNCSQPSPLDVGVKNTQSQGKTSACEVSGDVTVDVTGVNALQGMAEPRRENISHNTQDILIPNVLLSQEKNAVLGLPVALQDKAVTDPQGVGTPEMIPLDWEKGKLEGADHSCTMGDAEEAQIDDEAHPVLLQPVAKELPTDMELSAHDDGAPAGVREVMRAPPSGRERSTPSLPCMVSAQDAPLPKGADLIEEAASRIVDAVIEQVKAAGALLTEGEACHMSLSSPELGPLTKGLESAFTEKVSTFPPGESLPMGSTPEEATGSLAGCFAGREEPEKIILPVQGPEPAAEMPDVKAEDEVDFRASSISEEVAVGSIAATLKMKQGPMTQAINRENWCTIEPCPDAASLLASKQSPECENFLDVGLGRECTSKQGVLKRESGSDSDLFHSPSDDMDSIIFPKPEEEHLACDITGSSSSTDDTASLDRHSSHGSDVSLSQILKPNRSRDRQSLDGFYSHGMGAEGRESESEPADPGDVEEEEMDSITEVPANCSVLRSSMRSLSPFRRHSWGPGKNAASDAEMNHRSSMRVLGDVVRRPPIHRRSFSLEGLTGGAGVGNKPSSSLEVSSANAEELRHPFSGEERVDSLVSLSEEDLESDQREHRMFDQQICHRSKQQGFNYCTSAISSPLTKSISLMTISHPGLDNSRPFHSTFHNTSANLTESITEENYNFLPHSPSKKDSEWKSGTKVSRTFSYIKNKMSSSKKSKEKEKEKDKIKEKEKDSKDKEKDKKTVNGHTFSSIPVVGPISCSQCMKPFTNKDAYTCANCSAFVHKGCRESLASCAKVKMKQPKGSLQAHDTSSLPTVIMRNKPSQPKERPRSAVLLVDETATTPIFANRRSQQSVSLSKSVSIQNITGVGNDENMSNTWKFLSHSTDSLNKISKVNESTESLTDEGVGTDMNEGQLLGDFEIESKQLEAESWSRIIDSKFLKQQKKDVVKRQEVIYELMQTEFHHVRTLKIMSGVYSQGMMADLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSEKNFLIKRIGDVLVNQFSGENAERLKKTYGKFCGQHNQSVNYFKDLYAKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLAQSLSLVKDVIGAVDSKVASYEKKVRLNEIYTKTDSKSIMRMKSGQMFAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTINTLNRDEDEGIPSENEEEKKMLDTRARELKEQLHQKDQKILLLLEEKEMIFRDMAECSTPLPEDCSPTHSPRVLFRSNTEEALKGGPLMKSAINEVEILQGLVSGNLGGTLGPTVSSPIEQDVVGPVSLPRRAETFGGFDSHQMNASKGGEKEEGDDGQDLRRTESDSGLKKGGNANLVFMLKRNSEQVVQSVVHLYELLSALQGVVLQQDSYIEDQKLVLSERALTRSLSRPSSLIEQEKQRSLEKQRQDLANLQKQQAQYLEEKRRREREWEARERELREREALLAQREEEVQQGQQDLEKEREELQQKKGTYQYDLERLRAAQKQLEREQEQLRREAERLSQRQTERDLCQVSHPHTKLMRIPSFFPSPEEPPSPSAPSIAKSGSLDSELSVSPKRNSISRTHKDKGPFHILSSTSQTNKGPEGQSQAPASTSASTRLFGLTKPKEKKEKKKKNKTSRSQPGDGPASEVSAEGEEIFC O75952 Q8WXW5 Q9HAY3 Q9HAY4 Q9HAY5 Q9HCY9 CABYR_HUMAN Calcium-binding tyrosine phosphorylation-regulated protein Calcium-binding protein 86 Testis-specific calcium-binding protein CBP86 Fibrousheathin-2 FSP-2 Fibrousheathin II Cancer/testis antigen 88 CT88 CABYR CBP86 FSP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous sheath protein involved in capacitation. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6) PROTEIN SEQUENCE OF 8-23; 28-48; 379-388 AND 394-410 VARIANTS ARG-448 AND ALA-490 CALCIUM-BINDING PHOSPHORYLATION SUBCELLULAR LOCATION TISSUE SPECIFICITY Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Ovary Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-359; SER-362; SER-413; SER-461 AND SER-469 MASS SPECTROMETRY Sperm Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain. ALTERNATIVE SPLICING (ISOFORMS 3 AND 5) SUBUNIT INTERACTION WITH GSK3B PHOSPHORYLATION AT THR-151 AND SER-155 MUTAGENESIS OF THR-146; THR-151; SER-154; SER-155 AND THR-159 SUBCELLULAR LOCATION TISSUE SPECIFICITY Translation and assembly of CABYR coding region B in fibrous sheath and restriction of calcium binding to coding region A. CALCIUM-BINDING SUBCELLULAR LOCATION TISSUE SPECIFICITY May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Isoform 1 binds calcium in vitro. Isoform 2 and isoform 6 probably bind calcium. Isoform 3 and isoform 5 do not bind calcium in vitro. Isoform 4 probably does not bind calcium. Isoform 3 self-associates. Isoform 3 and isoform 5 interact with GSK3B. Isoform 1 does not interact with GSK3B. Cytoplasm. Note=Localized to fibrous sheath including the surface of the longitudinal columns and ribs of the principal piece of sperm flagella. According to Ref.4, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic. Isoform 1: Nucleus. Cytoplasm. Note=According to Ref.4, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic. Isoform 3: Nucleus. Cytoplasm. Note=According to Ref.4, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic. Isoform 5: Nucleus. Cytoplasm. Note=According to Ref.4, isoform 1, isoform 3 and isoform 5 are both nuclear and cytoplasmic. O75952-1 1 O75952-2 2 CBP86-VII O75952-3 3 CBP86-II O75952-4 4 CBP86-IV O75952-5 5 CBP86-III O75952-6 6 CBP86-VI Expressed in elongating spermatids and spermatozoa (at protein level). Isoform 1 is expressed in testis. Isoform 3 and isoform 5 are also expressed in brain, pancreas and numerous brain tumors. Isoform 1 is phosphorylated on tyrosine residues during in vitro capacitation. Isoform 3 and isoform 5 are phosphorylated by GSK3B in vitro. Dephosphorylation affects its ability to bind calcium. Contains 1 RIIa domain. Alternative splicing Calcium Cytoplasm Cytoskeleton Direct protein sequencing Metal-binding Nucleus Phosphoprotein Polymorphism Structural protein GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYM AM ATSERGQPPPCSNMWTLYCLTDKNQQGHPSPPPAPGPFPQA TLYLPNPKDPQFQQHPPKVTFPTYVMGDTKKTSAPPFILVG SNVQEAQGWKPLPGHAVVSQSDVLRYVAMQVPIAVPADEKY QKHTLSPQNANPPSGQDVPRPKSPVFLSVAFPVEDVAKKSS GSGDKCAPFGSYGIAGEVTVTTAHKRRKAETEN GKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVA EDVAKKSSGSGDKCAPFGSYGIAGEVTVTTAHKRRKAE TEN T M K R S A T A T A S A S A T A I V MISSKPRLVVPYGLKTLLEGISRAVLKTNPSNINQFAAAYFQELTMYRGNTTMDIKDLVKQFHQIKVEKWSEGTTPQKKLECLKEPGKTSVESKVPTQMEKSTDTDEDNVTRTEYSDKTTQFPSVYAVPGTEQTEAVGGLSSKPATPKTTTPPSSPPPTAVSPEFAYVPADPAQLAAQMLGKVSSIHSDQSDVLMVDVATSMPVVIKEVPSSEAAEDVMVAAPLVCSGKVLEVQVVNQTSVHVDLGSQPKENEAEPSTASSVPLQDEQEPPAYDQAPEVTLQADIEVMSTVHISSVYNDVPVTEGVVYIEQLPEQIVIPFTDQVACLKENEQSKENEQSPRVSPKSVVEKTTSGMSKKSVESVKLAQLEENAKYSSVYMEAEATALLSDTSLKGQPEVPAQLLDAEGAIKIGSEKSLHLEVEITSIVSDNTGQEESGENSVPQEMEGKPVLSGEAAEAVHSGTSVKSSSGPFPPAPEGLTAPEIEPEGESTAE Q15831 STK11_HUMAN Serine/threonine-protein kinase 11 Serine/threonine-protein kinase LKB1 Renal carcinoma antigen NY-REN-19 STK11 LKB1 PJS Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [MRNA] Liver Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. NUCLEOTIDE SEQUENCE [MRNA] Liver Low frequency of somatic mutations in the LKB1/Peutz-Jeghers syndrome gene in sporadic breast cancer. NUCLEOTIDE SEQUENCE [GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung Uterus Antigens recognized by autologous antibody in patients with renal-cell carcinoma. IDENTIFICATION AS A RENAL CANCER ANTIGEN Renal cell carcinoma Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD. FUNCTION SUBCELLULAR LOCATION INTERACTION WITH STRAD AUTOPHOSPHORYLATION AT THR-336 AND THR-363 MUTAGENESIS OF ASP-176 MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. FUNCTION SUBCELLULAR LOCATION MUTAGENESIS OF ASP-194 INTERACTION WITH STRAD AND CAB39 Somatic mutations in LKB1 are rare in sporadic colorectal and testicular tumors. VARIANT TESTICULAR TUMORS ASP-163 Nine novel germline mutations of STK11 in ten families with Peutz-Jeghers syndrome. VARIANT PJS ASN-247 DEL A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. VARIANTS PJS PRO-67 AND 303-ILE--GLN-306 DELINS ASN Novel mutations in the LKB1/STK11 gene in Dutch Peutz-Jeghers families. VARIANTS PJS 162-ASN--MET-164; ASN-194 AND LYS-297 Mutations and impaired function of LKB1 in familial and non-familial Peutz-Jeghers syndrome and a sporadic testicular cancer. CHARACTERIZATION OF VARIANT TESTICULAR TUMORS ASP-163 Somatic mutations in the Peutz-Jeghers (LKB1/STKII) gene in sporadic malignant melanomas. VARIANTS MELANOMA ASP-49 AND ARG-135 Somatic mutation of the Peutz-Jeghers syndrome gene, LKB1/STK11, in malignant melanoma. VARIANT MELANOMA TYR-194 Mutation analysis of the STK11/LKB1 gene and clinical characteristics of an Australian series of Peutz-Jeghers syndrome patients. VARIANTS PJS CYS-239 AND SER-315 Essential role in G1 cell cycle arrest. Phosphorylates and activates members of the AMPK-related subfamily of protein kinases. Tumor suppressor. ATP + a protein = ADP + a phosphoprotein. Magnesium or Manganese. Activated by binding of a complex consisting of CAB39 and STRAD or CAB39 and ALS2CR2. Q9C0K7 false 1 Q9Y376 false 1 Q96L34 false 1 Q7RTN6 false 3 Nucleus. Cytoplasm. Note=Relocates to the cytoplasm when bound to CAB39 and STRAD or CAB39 and ALS2CR2. Ubiquitously expressed. Strongest expression in testis and fetal liver. Phosphorylated by a cAMP-dependent protein kinase. Defects in STK11 are a cause of Peutz-Jeghers syndrome (PJS) [MIM:175200]. PJS is a rare hereditary disease in which there is predisposition to benign and malignant tumors of many organ systems. PJS is an autosomal dominant disorder characterized by melanocytic macules of the lips, multiple gastrointestinal hamartomatous polyps and an increased risk for various neoplasms, including gastrointestinal cancer. Defects in STK11 have been associated with testicular tumors [MIM:273300]. It includes germ cell tumor (GCT) or testicular germ cell tumor (TGCT). Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain. PJS entry ATP-binding Cell cycle Cytoplasm Disease mutation Kinase Magnesium Manganese Metal-binding Nucleotide-binding Nucleus Phosphoprotein Serine/threonine-protein kinase Transferase Y D L P G R DGL NDM G D D N D Y W C R K IRQH N P S D Y D A MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPGNLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSIRQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDIIYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSASSKIRRLSACKQQ O43823 AKAP8_HUMAN A-kinase anchor protein 8 A-kinase anchor protein 95 kDa AKAP 95 AKAP8 AKAP95 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95. NUCLEOTIDE SEQUENCE [MRNA] Cerebellum Testis The DNA sequence and biology of human chromosome 19. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Large-scale characterization of HeLa cell nuclear phosphoproteins. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 MASS SPECTROMETRY Epithelium Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339 MASS SPECTROMETRY Epithelium A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 MASS SPECTROMETRY Epithelium The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] HIS-664 Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II). Binds to dimeric RII-alpha regulatory subunit of PKA during mitosis. Nucleus matrix. Note=Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis. Highly expressed in heart, liver, skeletal muscle, kidney and pancreas. Belongs to the AKAP95 family. DNA-binding Metal-binding Nucleus Phosphoprotein Polymorphism Repeat Zinc Zinc-finger Q H MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEAAKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQDRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARERGSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSPSRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDGTGRKRKQFQLYEEPDTKLARVDSEGDFSENDDAAGDFRSGDEEFKGEDELCDSGRQRGEKEDEDEDVKKRREKQRRRDRTRDRAADRIQFACSVCKFRSFDDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIVNRNKKIEKRRQELMEKETAKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQPQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNRHIVKMLEKYLKGEDPFTSETVDPEMEGDDNLGGEDKKETPEEVAADVLAEVITAAVRAVDGEGAPAPESSGEPAEDEGPTDTAEAGSDPQAEQLLEEQVPCGTAHEKGVPKARSEAAEAGNGAETMAAEAESAQTRVAPAPAAADAEVEQTDAESKDAVPTE P61224 P09526 Q6DCA1 Q6LES0 RAP1B_HUMAN Ras-related protein Rap-1b precursor GTP-binding protein smg p21B RAP1B OK/SW-cl.11 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Nucleotide sequence of a human cDNA encoding a ras-related protein (rap1B). NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Uterus Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Colon adenocarcinoma cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta Testis Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K. PROTEIN SEQUENCE OF 1-35 SUBCELLULAR LOCATION ADP-RIBOSYLATION AT SER-39 Rap1-B is phosphorylated by protein kinase A in intact human platelets. PROTEIN SEQUENCE OF 146-180 PHOSPHORYLATION Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 168-176 Platelet Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine. ISOPRENYLATION AT CYS-181 Platelet Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway. INTERACTION WITH SGSM1; SGSM2 AND SGSM3 Activated by guanine nucleotide-exchange factor (GEF) EPAC2 in a cAMP-dependent manner. Interacts with SGSM1, SGSM2 and SGSM3. Cell membrane. Cytoplasm, cytosol. Note=May shuttle between plasma membrane and cytosol. Belongs to the small GTPase superfamily. Ras family. ADP-ribosylation Cytoplasm Direct protein sequencing GTP-binding Lipoprotein Membrane Methylation Nucleotide-binding Phosphoprotein Prenylation K N MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL Q99996 O14869 O43355 O94895 Q75N20 Q9UQH3 Q9UQQ4 Q9Y6B8 Q9Y6Y2 AKAP9_HUMAN A-kinase anchor protein 9 Protein kinase A-anchoring protein 9 PRKA9 A-kinase anchor protein 450 kDa AKAP 450 A-kinase anchor protein 350 kDa AKAP 350 hgAKAP 350 AKAP 120-like protein Protein hyperion Protein yotiao Centrosome- and Golgi-localized PKN-associated protein CG-NAP AKAP9 AKAP350 AKAP450 KIAA0803 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4) Brain Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) VARIANT GLN-1347 INS Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3) VARIANTS ILE-475 AND SER-2983 Brain Cloning of Hyperion. NUCLEOTIDE SEQUENCE [GENOMIC DNA] The DNA sequence of human chromosome 7. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] AKAP350, a multiply spliced protein kinase A-anchoring protein associated with centrosomes. NUCLEOTIDE SEQUENCE [MRNA] OF 323-3911 (ISOFORM 2) NUCLEOTIDE SEQUENCE [MRNA] OF 2157-3911 (ISOFORM 6) VARIANT SER-2983 Gastric parietal cell Lung Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2212-3911 (ISOFORMS 2/3) VARIANT SER-2983 Brain AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. FUNCTION INTERACTION WITH CIP4 AND FNBP1 SUBCELLULAR LOCATION ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3869 MASS SPECTROMETRY The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] ILE-2421 AND GLN-3301 Binds to type II regulatory subunits of protein kinase A. Scaffolding protein that assembles several protein kinases and phosphatases on the centrosome and Golgi apparatus. May be required to maintain the integrity of the Golgi apparatus. Isoform 4/Yotiao is associated with the N-methyl-D-aspartate receptor and is specifically found in the neuromuscular junction (NMJ) as well as in neuronal synapses, suggesting a role in the organization of postsynaptic specializations. Interacts with the regulatory region of protein kinase N (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1) and the immature non-phosphorylated form of PKC epsilon. Interacts with CIP4 and FNBP1. Cytoplasm. Centrosome. Golgi apparatus. Note=Cytoplasmic in parietal cells. Q99996-1 1 Q99996-2 2 Q99996-3 3 CG-NAP Q99996-4 4 Yotiao Q99996-5 5 Q99996-6 6 AKAP350 Widely expressed. Isoform 4/Yotiao is highly expressed in skeletal muscle and in pancreas. RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Phosphorylated upon DNA damage, probably by ATM or ATR. Alternative splicing Coiled coil Cytoplasm Golgi apparatus Phosphoprotein Polymorphism QLQEEIK LAQVRVL SADTFQKVE Q VFGFYNMCFSTLC GSSIPELAHSDAYQTREICSS STTQFHAGMRR ALSLTTSWQHHSARPTAPLFFEILSH SLG M I K KQ M I N S P S E Q E Q E G R S N S H N K N QKH PKP Q P Q P N D V E R P N T V G A P I V V D EI HE E V L R I N E D Q H Q H ESE QSQ P A T S MEDEERQKKLEAGKAKIEELSLAFLVRQLAQFRQRKAQSDGQSPSKKQKKKRKTSSSKHDVSAHHDLNIDQSQCNEMYINSSQRVESTVIPESTIMRTLHSGEITSHEQGFSVELESEISTTADDCSSEVNGCSFVMRTGKPTNLLREEEFGVDDSYSEQGAQDSPTHLEMMESELAGKQHEIEELNRELEEMRVTYGTEGLQQLQEFEAAIKQRDGIITQLTANLQQARREKDETMREFLELTEQSQKLQIQFQQLQASETLRNSTHSSTAADLLQAKQQILTHQQQLEEQDHLLEDYQKKKEDFTMQISFLQEKIKVYEMEQDKKVENSNKEEIQEKETIIEELNTKIIEEEKKTLELKDKLTTADKLLGELQEQIVQKNQEIKNMKLELTNSKQKERQSSEEIKQLMGTVEELQKRNHKDSQFETDIVQRMEQETQRKLEQLRAELDEMYGQQIVQMKQELIRQHMAQMEEMKTRHKGEMENALRSYSNITVNEDQIKLMNVAINELNIKLQDTNSQKEKLKEELGLILEEKCALQRQLEDLVEELSFSREQIQRARQTIAEQESKLNEAHKSLSTVEDLKAEIVSASESRKELELKHEAEVTNYKIKLEMLEKEKNAVLDRMAESQEAELERLRTQLLFSHEEELSKLKEDLEIEHRINIEKLKDNLGIHYKQQIDGLQNEMSQKIETMQFEKDNLITKQNQLILEISKLKDLQQSLVNSKSEEMTLQINELQKEIEILRQEEKEKGTLEQEVQELQLKTELLEKQMKEKENDLQEKFAQLEAENSILKDEKKTLEDMLKIHTPVSQEERLIFLDSIKSKSKDSVWEKEIEILIEENEDLKQQCIQLNEEIEKQRNTFSFAEKNFEVNYQELQEEYACLLKVKDDLEDSKNKQELEYKSKLKALNEELHLQRINPTTVKMKSSVFDEDKTFVAETLEMGEVVEKDTTELMEKLEVTKREKLELSQRLSDLSEQLKQKHGEISFLNEEVKSLKQEKEQVSLRCRELEIIINHNRAENVQSCDTQVSSLLDGVVTMTSRGAEGSVSKVNKSFGEESKIMVEDKVSFENMTVGEESKQEQLILDHLPSVTKESSLRATQPSENDKLQKELNVLKSEQNDLRLQMEAQRICLSLVYSTHVDQVREYMENEKDKALCSLKEELIFAQEEKIKELQKIHQLELQTMKTQETGDEGKPLHLLIGKLQKAVSEECSYFLQTLCSVLGEYYTPALKCEVNAEDKENSGDYISENEDPELQDYRYEVQDFQENMHTLLNKVTEEYNKLLVLQTRLSKIWGQQTDGMKLEFGEENLPKEETEFLSIHSQMTNLEDIDVNHKSKLSSLQDLEKTKLEEQVQELESLISSLQQQLKETEQNYEAEIHCLQKRLQAVSESTVPPSLPVDSVVITESDAQRTMYPGSCVKKNIDGTIEFSGEFGVKEETNIVKLLEKQYQEQLEEEVAKVIVSMSIAFAQQTELSRISGGKENTASSKQAHAVCQQEQHYFNEMKLSQDQIGFQTFETVDVKFKEEFKPLSKELGEHGKEILLSNSDPHDIPESKDCVLTISEEMFSKDKTFIVRQSIHDEISVSSMDASRQLMLNEEQLEDMRQELVRQYQEHQQATELLRQAHMRQMERQREDQEQLQEEIKRLNRQLAQRSSIDNENLVSERERVLLEELEALKQLSLAGREKLCCELRNSSTQTQNGNENQGEVEEQTFKEKELDRKPEDVPPEILSNERYALQKANNRLLKILLEVVKTTAAVEETIGRHVLGILDRSSKSQSSASLIWRSEAEASVKSCVHEEHTRVTDESIPSYSGSDMPRNDINMWSKVTEEGTELSQRLVRSGFAGTEIDPENEELMLNISSRLQAAVEKLLEAISETSSQLEHAKVTQTELMRESFRQKQEATESLKCQEELRERLHEESRAREQLAVELSKAEGVIDGYADEKTLFERQIQEKTDIIDRLEQELLCASNRLQELEAEQQQIQEERELLSRQKEAMKAEAGPVEQQLLQETEKLMKEKLEVQCQAEKVRDDLQKQVKALEIDVEEQVSRFIELEQEKNTELMDLRQQNQALEKQLEKMRKFLDEQAIDREHERDVFQQEIQKLEQQLKVVPRFQPISEHQTREVEQLANHLKEKTDKCSELLLSKEQLQRDIQERNEEIEKLEFRVRELEQALLVSADTFQKVEDRKHFGAVEAKPELSLEVQLQAERDAIDRKEKEITNLEEQLEQFREELENKNEEVQQLHMQLEIQKKESTTRLQELEQENKLFKDDMEKLGLAIKESDAMSTQDQHVLFGKFAQIIQEKEVEIDQLNEQVTKLQQQLKITTDNKVIEEKNELIRDLETQIECLMSDQECVKRNREEEIEQLNEVIEKLQQELANIGQKTSMNAHSLSEEADSLKHQLDVVIAEKLALEQQVETANEEMTFMKNVLKETNFKMNQLTQELFSLKRERESVEKIQSIPENSVNVAIDHLSKDKPELEVVLTEDALKSLENQTYFKSFEENGKGSIINLETRLLQLESTVSAKDLELTQCYKQIKDMQEQGQFETEMLQKKIVNLQKIVEEKVAAALVSQIQLEAVQEYAKFCQDNQTISSEPERTNIQNLNQLREDELGSDISALTLRISELESQVVEMHTSLILEKEQVEIAEKNVLEKEKKLLELQKLLEGNEKKQREKEKKRSPQDVEVLKTTTELFHSNEESGFFNELEALRAESVATKAELASYKEKAEKLQEELLVKETNMTSLQKDLSQVRDHLAEAKEKLSILEKEDETEVQESKKACMFEPLPIKLSKSIASQTDGTLKISSSNQTPQILVKNAGIQINLQSECSSEEVTEIISQFTEKIEKMQELHAAEILDMESRHISETETLKREHYVAVQLLKEECGTLKAVIQCLRSKEVFGFYNMCFSTLCDSGSDWGQGIYLTHSQGFDIASEGRGEESESATDSFPKKIKGLLRAVHNEGMQVLSLTESPYSDGEDHSIQQVSEPWLEERKAYINTISSLKDLITKMQLQREAEVYDSSQSHESFSDWRGELLLALQQVFLEERSVLLAAFRTELTALGTTDAVGLLNCLEQRIQEQGVEYQAAMECLQKADRRSLLSEIQALHAQMNGRKITLKREQESEKPSQELLEYNIQQKQSQMLEMQVELSSMKDRATELQEQLSSEKMVVAELKSELAQTKLELETTLKAQHKHLKELEAFRLEVKDKTDEVHLLNDTLASEQKKSRELQWALEKEKAKLGRSEERDKEELEDLKFSLESQKQRNLQLNLLLEQQKQLLNESQQKIESQRMLYDAQLSEEQGRNLELQVLLESEKVRIREMSSTLDRERELHAQLQSSDGTGQSRPPLPSEDLLKELQKQLEEKHSRIVELLNETEKYKLDSLQTRQQMEKDRQVHRKTLQTEQEANTEGQKKMHELQSKVEDLQRQLEEKRQQVYKLDLEGQRLQGIMQEFQKQELEREEKRESRRILYQNLNEPTTWSLTSDRTRNWVLQQKIEGETKESNYAKLIEMNGGGTGCNHELEMIRQKLQCVASKLQVLPQKASERLQFETADDEDFIWVQENIDEIILQLQKLTGQQGEEPSLVSPSTSCGSLTERLLRQNAELTGHISQLTEEKNDLRNMVMKLEEQIRWYRQTGAGRDNSSRFSLNGGANIEAIIASEKEVWNREKLTLQKSLKRAEAEVYKLKAELRNDSLLQTLSPDSEHVTLKRIYGKYLRAESFRKALIYQKKYLLLLLGGFQECEDATLALLARMGGQPAFTDLEVITNRPKGFTRFRSAVRVSIAISRMKFLVRRWHRVTGSVSININRDGFGLNQGAEKTDSFYHSSGGLELYGEPRHTTYRSRSDLDYIRSPLPFQNRYPGTPADFNPGSLACSQLQNYDPDRALTDYITRLEALQRRLGTIQSGSTTQFHAGMRR Q16875 O43622 O75902 F263_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 6PF-2-K/Fru-2,6-P2ASE brain/placenta-type isozyme iPFK-2 Renal carcinoma antigen NY-REN-56 6-phosphofructo-2-kinase Fructose-2,6-bisphosphatase PFKFB3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Placenta Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2, 6-bisphosphatase gene (PFKFB3). NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Brain Human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) Brain An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Skeletal muscle The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis Antigens recognized by autologous antibody in patients with renal-cell carcinoma. IDENTIFICATION AS A RENAL CANCER ANTIGEN Renal cell carcinoma Synthesis and degradation of fructose 2,6-bisphosphate. Beta-D-fructose 2,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate. ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate. false 1 Q13617 false 1 Q16875-1 1 Q16875-2 2 Ubiquitous. In the C-terminal section; belongs to the phosphoglycerate mutase family. 3D-structure Alternative splicing ATP-binding Hydrolase Kinase Multifunctional enzyme Nucleotide-binding Phosphoprotein Transferase NMKGSRSSADSSRKH PLLGQACLT M V A G MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH P35348 O60451 Q13675 Q13729 Q6RUJ4 Q6RUJ5 Q6RUJ7 Q6RUJ8 Q6RUJ9 Q9UD63 ADA1A_HUMAN Alpha-1A adrenergic receptor Alpha 1A-adrenoceptor Alpha 1A-adrenoreceptor Alpha-1C adrenergic receptor Alpha-adrenergic receptor 1c ADRA1A ADRA1C Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning, functional expression and tissue distribution of human cDNA for the alpha 1C-adrenergic receptor. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1) VARIANT ARG-347 Prostate Cloning, expression and characterization of human alpha adrenergic receptors alpha 1a, alpha 1b and alpha 1c. NUCLEOTIDE SEQUENCE (ISOFORM 1) VARIANT ARG-347 Heart The alpha 1-adrenergic receptor that mediates smooth muscle contraction in human prostate has the pharmacological properties of the cloned human alpha 1c subtype. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) Hippocampus Lymphocyte The alpha 1C-adrenoceptor in human prostate: cloning, functional expression, and localization to specific prostatic cell types. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT ARG-347 Cloning and pharmacological characterization of human alpha-1 adrenergic receptors: sequence corrections and direct comparison with other species homologues. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT ARG-347 Cloning, functional expression and tissue distribution of human alpha 1c-adrenoceptor splice variants. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3) VARIANT ARG-347 TISSUE SPECIFICITY Prostate Molecular cloning, genomic characterization and expression of novel human alpha1A-adrenoceptor isoforms. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4) TISSUE SPECIFICITY Prostate Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking of native human alpha1A-adrenoceptors. NUCLEOTIDE SEQUENCE (ISOFORMS 2B/3B; 2C; 3C; 5 AND 6) Liver Genome-wide discovery and analysis of human seven transmembrane helix receptor genes. NUCLEOTIDE SEQUENCE (ISOFORM 1) cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Alpha 1a-adrenoceptor polymorphism: pharmacological characterization and association with benign prostatic hypertrophy. VARIANT ARG-347 Alpha 1A-adrenergic receptor polymorphism and vascular response. VARIANT ARG-347 The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] TRP-40 This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Cell membrane; Multi-pass membrane protein. P35348-1 1 Alpha 1c-1,Alpha(1A-1) P35348-2 2 Alpha 1c-2,Alpha(1A-2) P35348-3 3 Alpha 1c-3,Alpha(1A-3) P35348-4 4 Alpha(1A-4) P35348-5 5 P35348-6 6 P35348-7 2b/3b P35348-8 2c P35348-9 3c Heart, brain, liver and prostate, but not in kidney, lung, adrenal, aorta and pituitary. Isoform 4 is the most abundant isoform expressed in the prostate with high levels also detected in liver and heart. Carboxyl-terminal Ser or Thr residues may be phosphorylated. Belongs to the G-protein coupled receptor 1 family. Alternative splicing G-protein coupled receptor Glycoprotein Lipoprotein Membrane Palmitate Phosphoprotein Polymorphism Receptor Transducer Transmembrane GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV DEVSLCHQAGVQWHDLGSLQPPPPGFKRF SCLSLPSSWDYRDVPPGRRHQAQLIFVFLVETGFHHVGQDD LDLLTS GSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLR DEETEAQQGKNDSPSFKQPVHHAAVLGLEV MEKENLEGVSRKDTCGVW SFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV THTHDMKPASRPRLLSLLPKEGEHETHHWS CDPLSLESTPGAQEPCLTLGFTSLSSIHLTKAQIQHVTVTD TGKTVT SFFPDFKPSETVFKIVFWLGYLNSCINPI TYILKYDV LFWRKGLSVCTRLRERKEIKN SF KS VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV TKSRSVTRLECSGMILAHCNLRLPGSRDSPASASQ AAGTTGDVPPGRRHQAQLIFVFLVETGFHHVGQDDLDLLTS VRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV RGMDCRYFTKNCREHIKHVNFMMPPWRKGLEC VRSKSF GHTPMT G W C R G C S T Q C T P Q E S C MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV Q8N8S7 Q502W5 Q5T5M7 Q5VTQ9 Q5VTR0 Q9NVF3 Q9UFB8 ENAH_HUMAN Protein enabled homolog ENAH MENA Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human Mena: cDNA cloning, expression and promoter characterization. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Human Mena protein, a serex-defined antigen overexpressed in breast cancer eliciting both humoral and CD8+ T-cell immune response. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY Mammary tumor The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-591 (ISOFORM 2) Placenta Skin Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-591 (ISOFORM 2) Teratocarcinoma NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-591 (ISOFORM 2) Testis Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. PROTEIN SEQUENCE OF 23-47; 70-81; 123-145; 403-427; 484-499 AND 573-587 FUNCTION INTERACTION WITH BAIAP2 A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. INTERACTION WITH VCL; ZYX AND L.MONOCYTOGENES ACTA Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. INTERACTION WITH ZYX Robo4 is a vascular-specific receptor that inhibits endothelial migration. INTERACTION WITH ROBO4 RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. INTERACTION WITH APBB1IP T-cell Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. SUBCELLULAR LOCATION Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 MASS SPECTROMETRY Epithelium A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-489 MASS SPECTROMETRY Epithelium Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-405; THR-410; THR-502 AND SER-508 MASS SPECTROMETRY ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 MASS SPECTROMETRY Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts syngeristically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. Required for the actin-based mobility of Listeria monocytogenes. Homotetramer (By similarity). Interacts with APBB1IP, PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only after the autoinhibitory region of BAIAP2-alpha has been blocked by interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA. Interaction with ZYX is important for targeting ENAH to focal adhesions and enhances production of actin-rich structures at the apical surface of cells. Interacts, through the Pro-rich region, with the C-terminal SH3 domain of DNMPB. Binds GPHN. Cytoplasm. Cytoplasm, cytoskeleton (By similarity). Cell projection, lamellipodium (By similarity). Cell projection, filopodium (By similarity). Cell junction, synapse (By similarity). Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses. Q8N8S7-1 1 Q8N8S7-2 2 Expressed in myoepithelia of parotid, breast, bronchial glands and sweat glands. Expressed in colon-rectum muscolaris mucosae epithelium, pancreas acinar ductal epithelium, endometrium epithelium, prostate fibromuscolar stroma and placenta vascular media. Overexpressed in a majority of breast cancer cell lines and primary breast tumor lesions. The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. NTN1-induced PKA phosphorylation on Ser-265 directly parallels the formation of filopodial protrusions. Phosphorylated upon DNA damage, probably by ATM or ATR. Belongs to the Ena/VASP family. Contains 1 WH1 domain. Actin-binding Alternative splicing Cell junction Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Phosphoprotein Repeat SH3-binding Synapse T I MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERERLERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAPASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPLSQPSANGVQTEGLDYDRLKQDILDEMRKELTKLKEELIDAIRQELSKSNTA Q15506 Q9BXF7 SP17_HUMAN Sperm surface protein Sp17 Sperm autoantigenic protein 17 Sperm protein 17 Sp17-1 Cancer/testis antigen 22 CT22 SPA17 SP17 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and sequencing of cDNAs encoding the human sperm protein, Sp17. NUCLEOTIDE SEQUENCE [MRNA] Testis Genomic organization of an intron-containing sperm protein 17 gene (Sp17-1) and an intronless pseudogene (Sp17-2) in humans: a new model. NUCLEOTIDE SEQUENCE [MRNA] Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain A yeast two-hybrid system using Sp17 identified ropporin as a novel cancer-testis antigen in hematologic malignancies. POSSIBLE INTERACTION WITH ROPN1 Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates. Homodimer (By similarity). May interact with ROPN1. Membrane; Peripheral membrane protein . Testis and sperm specific. Contains 1 IQ domain. Membrane MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFESLLEKREKTNFDPAEWGSKVEDRFYNNHAFEEQEPPEKSDPKQEESQISGKEEETSVTILDSSEEDKEKEEVAAVKIQAAFRGHIAREEAKKMKTNSLQNEEKEENK P35228 O60757 O94994 Q16263 Q16692 Q4TTS5 NOS2A_HUMAN Nitric oxide synthase, inducible NOS type II Inducible NO synthase Inducible NOS iNOS Hepatocyte NOS HEP-NOS NOS2A NOS2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. NUCLEOTIDE SEQUENCE [MRNA] Liver Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. NUCLEOTIDE SEQUENCE [MRNA] Colon adenocarcinoma Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. NUCLEOTIDE SEQUENCE [MRNA] Chondrocyte Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. NUCLEOTIDE SEQUENCE [MRNA] Articular chondrocyte Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. NUCLEOTIDE SEQUENCE [MRNA] VARIANT LEU-608 Retina Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. NUCLEOTIDE SEQUENCE [MRNA] VARIANT LEU-608 Glioblastoma Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. NUCLEOTIDE SEQUENCE [MRNA] Airway epithelium Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. NUCLEOTIDE SEQUENCE [MRNA] Cardiac myocyte Cloning and characterization of a novel splice valiant of human inducible nitric oxide synthase. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu). NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS TRP-221; LEU-608; ALA-747 AND CYS-1009 Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? NUCLEOTIDE SEQUENCE [MRNA] OF 380-473 Kidney Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. CHARACTERIZATION Inducible nitric oxide synthase in the liver: regulation and function. CHARACTERIZATION Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. INTERACTION WITH SLC9A3R1 Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 74-504 Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 82-528 The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] SER-679 Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. L-arginine + n NADPH + m O(2) = citrulline + nitric oxide + n NADP(+). Heme group. Binds 1 FAD. Binds 1 FMN. Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme. Regulated by calcium/calmodulin. Aspirin inhibits expression and function of this enzyme and effects may be exerted at the level of translational/post-translational modification and directly on the catalytic activity. Homodimer. Binds SLC9A3R1. P35228-1 1 P35228-2 2 Expressed in the liver, retina, bone cells and airway epithelial cells of the lung. Not expressed in the platelets. By endotoxins and cytokines. Belongs to the NOS family. Contains 1 flavodoxin-like domain. Nitric oxide synthase entry 3D-structure Alternative splicing Calcium Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Oxidoreductase Phosphoprotein Polymorphism Zinc R W S L A S T A R C D G F L G V R H L I A T T I T A A D FL SP S P R G G A A V MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPLVETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVTILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDLSKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDRVAVQPSSLEMSAL Q13023 O15028 AKAP6_HUMAN A-kinase anchor protein 6 Protein kinase A-anchoring protein 6 PRKA6 A-kinase anchor protein 100 kDa AKAP 100 mAKAP AKAP6 AKAP100 KIAA0311 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes. NUCLEOTIDE SEQUENCE [MRNA] VARIANT VAL-1492 Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. SEQUENCE REVISION Cloning and characterization of A-kinase anchor protein 100 (AKAP100). A protein that targets A-kinase to the sarcoplasmic reticulum. NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2319 Hippocampus The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] MET-910; ILE-1192; GLN-1702 AND THR-1839 Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the nuclear membrane or sarcoplasmic reticulum. May act as an adapter for assembling multiprotein complexes. Interacts with RII subunit of PKA, phosphatase 2B (calcineurin) and AKAP79. Sarcoplasmic reticulum. Nucleus membrane. Note=In heart muscle. Participation of multiple targeting signals allow correct intracellular targeting. These may be repeated motifs rich in basic and hydrophobic amino acids, palmitoylated/myristoylated motifs or alternatively splice targeting sequences. Highly expressed in cardiac and skeletal muscle, followed by brain. RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Contains 2 spectrin repeats. Membrane Nucleus Polymorphism Repeat Sarcoplasmic reticulum A V N S K M M I A V E Q P T N D F Y D H W C MLTMSVTLSPLRSQDLDPMATDASPMAINMTPTVEQGEGEEAMKDMDSDQQYEKPPPLHTGADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDSDSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETKEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLSGLGDMTSSQVKTKPFDSWSYSEMEKEFPELIRSVGLLTVAADSISTNGSEAVTEEVSQVSLSVDDKGGCEEDNASAVEEQPGLTLGVSSSSGEALTNAAQPSSETVQQESSSSSHHDAKNQQPVPCENATPKRTIRDCFNYNEDSPTQPTLPKRGLFLKEETFKNDLKGNGGKRQMVDLKPEMSRSTPSLVDPPDRSKLCLVLQSSYPNSPSAASQSYECLHKVGNGNLENTVKFHIKEISSSLGRLNDCYKEKSRLKKPHKTSEEVPPCRTPKRGTGSGKQAKNTKSSAVPNGELSYTSKAIEGPQTNSASTSSLEPCNQRSWNAKLQLQSETSSSPAFTQSSESSVGSDNIMSPVPLLSKHKSKKGQASSPSHVTRNGEVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQNIDDWELSEMNSDSEIYPTYHVKKKHTRLGRVSPSSSSDIASSLGESIESGPLSDILSDEESSMPLAGMKKYADEKSERASSSEKNESHSATKSALIQKLMQDIQHQDNYEAIWEKIEGFVNKLDEFIQWLNEAMETTENWTPPKAEMDDLKLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLRMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEVQLCYLEAQRDAVEQMSLKLYSEQYTSSSKRKEEFADMSKVHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGVLLPNDLLEKVDSINEKWELLGKTLGEKIQDTMAGHSGSSPRDLLSPESGSLVRQLEVRIKELKGWLRDTELFIFNSCLRQEKEGTMNTEKQLQYFKSLCREIKQRRRGVASILRLCQHLLDDRETCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLQKKMGKESETLNVIDPGLMDLNGMSEDALEWDEMDISNKLISLNEESNDLDQELQPVIPSLKLGETSNEDPGYDEEADNHGGSQYASNITAPSSPHIYQVYSLHNVELYEDNHMPFLKNNPKVTGMTQPNVLTKSLSKDSSFSSTKSLPDLLGGSNLVKPCACHGGDMSQNSGSESGIVSEGDTETTTNSEMCLLNAVDGSPSNLETEHLDPQMGDAVNVLKQKFTDEGESIKLPNSSQSSISPVGCVNGKVGDLNSITKHTPDCLGEELQGKHDVFTFYDYSYLQGSKLKLPMIMKQSQSEKAHVEDPLLRGFYFDKKSCKSKHQTTELQPDVPPHERILASASHEMDRISYKSGNIEKTFTGMQNAKQLSLLSHSSSIESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFTGQMSLDIASSINEDSAASLTELSSSDELSLCSEDIVLHKNKIPESNASFRKRLTRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCIKDEDDDSSIATDDEIYEDCTLMSGLDYIKNELQTWIRPKLSLTRDKKRCNVSDEMKGSKDISSSEMTNPSDTLNIETLLNGSVKRVSENNGNGKNSSHTHELGTKRENKKTIFKVNKDPYVADMENGNIEGIPERQKGKPNVTSKVSENLGSHGKEISESEHCKCKALMDSLDDSNTAGKEFVSQDVRHLPKKCPNHHHFENQSTASTPTEKSFSELALETRFNNRQDSDALKSSDDAPSMAGKSAGCCLALEQNGTEENASISNISCCNCEPDVFHQKDAEDCSVHNFVKEIIDMASTALKSKSQPENEVAAPTSLTQIKEKVLEHSHRPIQLRKGDFYSYLSLSSHDSDCGEVTNYIEEKSSTPLPLDTTDSGLDDKEDIECFFEACVEGDSDGEEPCFSSAPPNESAVPSEAAMPLQATACSSEFSDSSLSADDADTVALSSPSSQERAEVGKEVNGLPQTSSGCAENLEFTPSKLDSEKESSGKPGESGMPEEHNAASAKSKVQDLSLKANQPTDKAALHPSPKTLTCEENLLNLHEKRHRNMHR Q9UI08 O95884 Q7Z522 Q8TBV1 Q9UF25 Q9UIC2 EVL_HUMAN Ena/VASP-like protein Ena/vasodilator-stimulated phosphoprotein-like EVL RNB6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Adrenal gland The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Lung Pancreas NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416 Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-364 Uterus The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain. INTERACTION WITH SEMA6A Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. INTERACTION WITH RAPH1 Large-scale characterization of HeLa cell nuclear phosphoproteins. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-331 MASS SPECTROMETRY Epithelium Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS Spectra. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250 MASS SPECTROMETRY Epithelium The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247 Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization. Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes. Homotetramer (By similarity). Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA. P08631 false 1 Cytoplasm, cytoskeleton (By similarity). Cell projection, lamellipodium (By similarity). Note=Targeted to the leading edge of lamellipodia and the dital tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes. Q9UI08-1 2 Q9UI08-2 1 The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC. Belongs to the Ena/VASP family. Contains 1 WH1 domain. Actin-binding Alternative splicing Cell projection Cytoplasm Cytoskeleton Phosphoprotein Polymorphism SH3-binding M MAT P L P L P S S N M Y MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSSQRQVQNGPSPDEMDIQRRQVMEQHQQQRQESLERRTSATGPILPPGHPSSAASAPVSCSGPPPPPPPPVPPPPTGATPPPPPPLPAGGAQGSSHDESSMSGLAAAIAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQSDKPAEKKEDESQMEDPSTSPSPGTRAASQPPNSSEAGRKPWERSNSVEKPVSSILSRTPSVAKSPEAKSPLQSQPHSRMKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT P08670 Q15867 Q15868 Q15869 Q6LER9 Q8N850 Q96ML2 Q9NTM3 VIME_HUMAN Vimentin VIM Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Coding sequence and growth regulation of the human vimentin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene. NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta Stomach Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The DNA sequence and comparative analysis of human chromosome 10. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cervix Placenta Testis Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells. NUCLEOTIDE SEQUENCE OF 1-135 TISSUE SPECIFICITY Mammary carcinoma PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291; 322-333 AND 381-389 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT SER-2 MASS SPECTROMETRY T-cell Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. PROTEIN SEQUENCE OF 17-25 AND 55-70 Mammary carcinoma PROTEIN SEQUENCE OF 79-97 AND 411-424 MASS SPECTROMETRY Brain Cajal-Retzius cell Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466 TISSUE SPECIFICITY Fibroblast Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63). NUCLEOTIDE SEQUENCE [MRNA] OF 167-466 Osteosarcoma Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments. PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42; SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459 MASS SPECTROMETRY Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117 MASS SPECTROMETRY Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein. INTERACTION WITH HCV CORE PROTEIN MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation. IDENTIFICATION IN A COMPLEX WITH ACTB; AP2M1; AP2A1; AP2A2 AND MEGF10 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-56; SER-73; SER-214 AND SER-412 MASS SPECTROMETRY Epithelium A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 MASS SPECTROMETRY Epithelium Phosphoproteome analysis of the human mitotic spindle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 MASS SPECTROMETRY Epithelium Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS Spectra. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412; THR-446 AND SER-459 MASS SPECTROMETRY Epithelium Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-47; SER-55; SER-56; TYR-61; SER-430; THR-458 AND SER-459 MASS SPECTROMETRY Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138 Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411 Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Homopolymer. Component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. Interacts with HCV core protein. Q14194 false 1 Q00987 false 1 O95251 false 2 Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines. One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Belongs to the intermediate filament family. Vimentin entry Intron retention. 3D-structure Acetylation Coiled coil Direct protein sequencing Host-virus interaction Intermediate filament Phosphoprotein S D R P E G N S L S S I S C N K L F MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE P09917 Q5JQ14 LOX5_HUMAN Arachidonate 5-lipoxygenase 5-lipoxygenase 5-LO ALOX5 LOG5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning of the cDNA for human 5-lipoxygenase. NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE Molecular cloning and amino acid sequence of human 5-lipoxygenase. NUCLEOTIDE SEQUENCE [MRNA] ERRATUM Molecular cloning and amino acid sequence of human 5-lipoxygenase. NUCLEOTIDE SEQUENCE PARTIAL PROTEIN SEQUENCE The DNA sequence and comparative analysis of human chromosome 10. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Characterization of the human 5-lipoxygenase gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 Characterization of the human 5-lipoxygenase gene promoter. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 Reversible, calcium-dependent membrane association of human leukocyte 5-lipoxygenase. SUBCELLULAR LOCATION Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase. MUTAGENESIS OF SOME HISTIDINE RESIDUES Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. MUTAGENESIS OF SOME RESIDUES Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2). PHOSPHORYLATION AT SER-272 Protein kinase A inhibits leukotriene synthesis by phosphorylation of 5-lipoxygenase on serine 523. PHOSPHORYLATION AT SER-524 MUTAGENESIS OF SER-524 Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk. VARIANT LYS-254 Arachidonate + O(2) = (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate. (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O. Binds 1 iron ion per subunit. Binds 2 calcium ions per subunit. Leukotrienes biosynthesis; first step. Leukotrienes biosynthesis; second step. Q14019 false 3 Cytoplasm; Peripheral membrane protein. Note=Calcium binding promotes binding to membranes. Serine phosphorylation of LOX5 by MAPKAPK2 is stimulated by arachidonic acid. Serine phosphorylation of LOX5 on Ser-523 by PKA has an inhibitory effect. Belongs to the lipoxygenase family. Contains 1 PLAT domain. 3D-structure Calcium Cytoplasm Dioxygenase Direct protein sequencing Iron Leukotriene biosynthesis Membrane Metal-binding Oxidoreductase Phosphoprotein Polymorphism E K D N H S N H S N A H S N E Q H A H S N H A H S N H N A S A H N A MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI P22102 O14659 PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 Phosphoribosylamine--glycine ligase GARS Glycinamide ribonucleotide synthetase Phosphoribosylglycinamide synthetase Phosphoribosylformylglycinamidine cyclo-ligase AIRS Phosphoribosyl-aminoimidazole synthetase AIR synthase Phosphoribosylglycinamide formyltransferase GART GAR transformylase 5'-phosphoribosylglycinamide transformylase GART PGFT PRGS Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. NUCLEOTIDE SEQUENCE [MRNA] ALTERNATIVE SPLICING The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT) Testis Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-432 VARIANT ILE-421 Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. NUCLEOTIDE SEQUENCE [MRNA] OF 709-1010 Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348 MASS SPECTROMETRY Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 808-1010 IN COMPLEX WITH SUBSTRATE Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 808-1010 IN COMPLEX WITH FORMYLTETRAHYDROFOLATE ANALOG The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 808-1010 IN COMPLEX WITH SUBSTRATE ANALOGS ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. 10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. Nucleotide biosynthesis; IMP biosynthesis; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. Nucleotide biosynthesis; IMP biosynthesis; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. Nucleotide biosynthesis; IMP biosynthesis; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. Context: Purine biosynthesis. P62330 false 1 P22102-1 Long P22102-2 Short In the N-terminal section; belongs to the GARS family. In the central section; belongs to the AIR synthase family. In the C-terminal section; belongs to the GART family. Contains 1 ATP-grasp domain. 3D-structure Alternative splicing ATP-binding Ligase Multifunctional enzyme Nucleotide-binding Phosphoprotein Polymorphism Purine biosynthesis Transferase L F V I D G MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKDVGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTRIYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEGHLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKNLIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE P30101 Q13453 Q14255 Q8IYF8 Q9UMU7 PDIA3_HUMAN Protein disulfide-isomerase A3 precursor Disulfide isomerase ER-60 ERp60 58 kDa microsomal protein p58 ERp57 58 kDa glucose-regulated protein PDIA3 ERP57 ERP60 GRP58 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and characterization of a cDNA for bovine phospholipase C-alpha: proposal of redesignation of phospholipase C-alpha. NUCLEOTIDE SEQUENCE [MRNA] cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase. NUCLEOTIDE SEQUENCE [MRNA] Liver ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase. NUCLEOTIDE SEQUENCE [MRNA] Heart Cloning, expression and genomic organization of human placental protein disulfide isomerase (previously identified as phospholipase C alpha). NUCLEOTIDE SEQUENCE [MRNA] Placenta Structures of the human gene for the protein disulfide isomerase-related polypeptide ERp60 and a processed gene and assignment of these genes to 15q15 and 1q21. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 25-34 AND 504-505 MUTAGENESIS OF CYS-57; CYS-60; CYS-406 AND CYS-409 Liver epithelium The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver Lung Lymph A two-dimensional gel database of human colon carcinoma proteins. PROTEIN SEQUENCE OF 25-54; 62-75 AND 95-104 Colon carcinoma Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 25-38 Platelet Human liver protein map: a reference database established by microsequencing and gel comparison. PROTEIN SEQUENCE OF 25-33 Liver Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. PROTEIN SEQUENCE OF 26-42 Mammary carcinoma Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. PROTEIN SEQUENCE OF 95-104 AND 472-479 Keratinocyte PROTEIN SEQUENCE OF 306-329 AND 472-482 MASS SPECTROMETRY Brain Cajal-Retzius cell Cluster analysis of an extensive human breast cancer cell line protein expression map database. MASS SPECTROMETRY Mammary cancer Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] MASS SPECTROMETRY ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57. INTERACTION WITH ERP27 Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] MASS SPECTROMETRY The solution structure of the second thioredoxin domain of human protein disulfide-isomerase A3. STRUCTURE BY NMR OF 357-485 Catalyzes the rearrangement of -S-S- bonds in proteins. Interacts with ERP27. Q03103 true 1 P61823 true 1 Q03518 false 3 Endoplasmic reticulum lumen (By similarity). Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. PubMed:11840567 Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains. Was originally thought to be a phosphatidylinositol-4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha). 3D-structure Direct protein sequencing Endoplasmic reticulum Isomerase Polymorphism Redox-active center Repeat Signal K R C A C S C S C A C S C S A G A V D Y Q P E G N D D G D G E D MRLRRLALFPGVALLLAAARLAAASDVLELTDDNFESRISDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASIVGFFDDSFSEAHSEFLKAASNLRDNYRFAHTNVESLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL Q02952 O00310 O00498 Q4LE68 Q5SZ80 Q5TGN1 Q68D82 Q99970 AKA12_HUMAN A-kinase anchor protein 12 A-kinase anchor protein 250 kDa AKAP 250 Gravin Myasthenia gravis autoantigen AKAP12 AKAP250 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT GLN-216 Heart Changes of gene expression by lysophosphatidylcholine in vascular endothelial cells: 12 up-regulated distinct genes including 5 cell growth-related, 3 thrombosis-related, and 4 others. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) VARIANT LYS-117 Umbilical vein endothelial cell NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) VARIANTS GLN-216; GLY-920 AND LYS-1355 Testis Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANTS GLN-216 AND ASP-1600 Brain The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT LYS-117 Sequence of gravin cDNA isolated from a human umbilical vein endothelial cell library. NUCLEOTIDE SEQUENCE [MRNA] OF 43-1782 VARIANT GLN-216 Umbilical vein endothelial cell Molecular cloning and preliminary characterization of a novel cytoplasmic antigen recognized by myasthenia gravis sera. NUCLEOTIDE SEQUENCE [MRNA] OF 1478-1782 Umbilical vein endothelial cell Multiple promoters direct expression of three AKAP12 isoforms with distinct subcellular and tissue distribution profiles. ALTERNATIVE SPLICING Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-312; SER-565; SER-566; SER-568; SER-569; SER-598 AND SER-612 MASS SPECTROMETRY Epithelium Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-283; SER-286; SER-627; SER-629 AND SER-1331 MASS SPECTROMETRY ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-505; SER-732 AND SER-887 MASS SPECTROMETRY The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] LYS-240 Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC). Binds to dimeric RII-alpha regulatory subunit of PKC. Cytoplasm, cell cortex (Probable). Cytoplasm, cytoskeleton (Probable). Note=May be part of the cortical cytoskeleton. Q02952-1 1 Alpha Q02952-2 2 Beta Q02952-3 3 Gamma Expressed in endothelial cells, cultured fibroblasts and osteosarcoma, but not in platelets, leukocytes, monocytic cell lines or peripherical blood cells. Activated by lysophosphatidylcholine (lysoPC). Polybasic regions located between residues 266 and 557 are involved in binding PKC. Phosphorylated upon DNA damage, probably by ATM or ATR. Antibodies to the C-terminal of gravin can be produced by patients with myasthenia gravis (MG). Contains 3 AKAP domains. Alternative splicing Cytoplasm Cytoskeleton Phosphoprotein Polymorphism Repeat EEEVIVTE MLGTITIT E M E K K Q E K E G V I R L E K E D E D TPEI NRN T I E G G R S G E G A S A T E EE V M Q L MGAGSSTEQRSPEQPPEGSSTPAEPEPSGGGPSAEAAPDTTADPAIAASDPATKLLQKNGQLSTINGVAEQDELSLQEGDLNGQKGALNGQGALNSQEEEEVIVTEVGQRDSEDVSERDSDKEMATKSAVVHDITDDGQEETPEIIEQIPSSESNLEELTQPTESQANDIGFKKVFKFVGFKFTVKKDKTEKPDTVQLLTVKKDEGEGAAGAGDHKDPSLGAGEAASKESEPKQSTEKPEETLKREQSHAEISPPAESGQAVEECKEEGEEKQEKEPSKSAESPTSPVTSETGSTFKKFFTQGWAGWRKKTSFRKPKEDEVEASEKKKEQEPEKVDTEEDGKAEVASEKLTASEQAHPQEPAESAHEPRLSAEYEKVELPSEEQVSGSQGPSEEKPAPLATEVFDEKIEVHQEEVVAEVHVSTVEERTEEQKTEVEETAGSVPAEELVEMDAEPQEAEPAKELVKLKETCVSGEDPTQGADLSPDEKVLSKPPEGVVSEVEMLSSQERMKVQGSPLKKLFTSTGLKKLSGKKQKGKRGGGDEESGEHTQVPADSPDSQEEQKGESSASSPEEPEEITCLEKGLAEVQQDGEAEEGATSDGEKKREGVTPWASFKKMVTPKKRVRRPSESDKEDELDKVKSATLSSTESTASEMQEEMKGSVEEPKPEEPKRKVDTSVSWEALICVGSSKKRARRGSSSDEEGGPKAMGGDHQKADEAGKDKETGTDGILAGSQEHDPGQGSSSPEQAGSPTEGEGVSTWESFKRLVTPRKKSKSKLEEKSEDSIAGSGVEHSTPDTEPGKEESWVSIKKFIPGRRKKRPDGKQEQAPVEDAGPTGANEDDSDVPAVVPLSEYDAVEREKMEAQQAQKSAEQPEQKAATEVSKELSESQVHMMAAAVADGTRAATIIEERSPSWISASVTEPLEQVEAEAALLTEEVLEREVIAEEEPPTVTEPLPENREARGDTVVSEAELTPEAVTAAETAGPLGAEEGTEASAAEETTEMVSAVSQLTDSPDTTEEATPVQEVEGGVPDIEEQERRTQEVLQAVAEKVKEESQLPGTGGPEDVLQPVQRAEAERPEEQAEASGLKKETDVVLKVDAQEAKTEPFTQGKVVGQTTPESFEKAPQVTESIESSELVTTCQAETLAGVKSQEMVMEQAIPPDSVETPTDSETDGSTPVADFDAPGTTQKDEIVEIHEENEVASGTQSGGTEAEAVPAQKERPPAPSSFVFQEETKEQSKMEDTLEHTDKEVSVETVSILSKTEGTQEADQYADEKTKDVPFFEGLEGSIDTGITVSREKVTEVALKGEGTEEAECKKDDALELQSHAKSPPSPVEREMVVQVEREKTEAEPTHVNEEKLEHETAVTVSEEVSKQLLQTVNVPIIDGAKEVSSLEGSPPPCLGQEEAVCTKIQVQSSEASFTLTAAAEEEKVLGETANILETGETLEPAGAHLVLEEKSSEKNEDFAAHPGEDAVPTGPDCQAKSTPVIVSATTKKGLSSDLEGEKTTSLKWKSDEVDEQVACQEVKVSVAIEDLEPENGILELETKSSKLVQNIIQTAVDQFVRTEETATEMLTSELQTQAHVIKADSQDAGQETEKEGEEPQASAQDETPITSAKEESESTAVGQAHSDISKDMSEASEKTMTVEVEGSTVNDQQLEEVVLPSEEEGGGAGTKSVPEDDGHALLAERIEKSLVEPKEDEKGDDVDDPENQNSALADTDASGGLTKESPDTNGPKQKEKEDAQEVELQEGKVHSESDKAITPQAQEELQKQERESAKSELTES O75969 O75945 Q9UM61 AKAP3_HUMAN A-kinase anchor protein 3 Protein kinase A-anchoring protein 3 PRKA3 A-kinase anchor protein 110 kDa AKAP 110 Sperm oocyte-binding protein Fibrousheathin-1 Fibrousheathin I Fibrous sheath protein of 95 kDa FSP95 Cancer/testis antigen 82 CT82 AKAP3 AKAP110 SOB1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of SOB1, a new testis-specific cDNA encoding a human sperm protein probably involved in oocyte recognition. NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE Testis FSP95, a testis-specific 95-kilodalton fibrous sheath antigen that undergoes tyrosine phosphorylation in capacitated human spermatozoa. NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE Testis Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein. NUCLEOTIDE SEQUENCE [MRNA] Testis Identification of sperm-specific proteins that interact with A-kinase anchoring proteins in a manner similar to the type II regulatory subunit of PKA. INTERACTION WITH ROPN1 AND ROPN1L MUTAGENESIS OF LEU-131 Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208; SER-403; TYR-404; SER-440; SER-612; SER-635 AND SER-636 MASS SPECTROMETRY Sperm The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] CYS-831 May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction. Interacts with ROPN1 AND ROPN1L. Acrosome (By similarity). Note=Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment. Testis specific; only expressed in spermatids. RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Phosphorylated on tyrosine residues. Belongs to the AKAP110 family. Direct protein sequencing Phosphoprotein Polymorphism R C L P G E E D S G K N I T F S S L MSEKVDWLQSQNGVCKVDVYSPGDNQAQDWKMDTSTDPVRVLSWLRRDLEKSTAEFQDVRFKPGESFGGETSNSGDPHKGFSVDYYNTTTKGTPERLHFEMTHKEIPCQGPRAQLGNGSSVDEVSFYANRLTNLVIAMARKEINEKIDGSENKCVYQSLYMGNEPTPTKSLSKIASELVNETVSACSRNAAPDKAPGSGDRVSGSSQSPPNLKYKSTLKIKESTKERQGPDDKPPSKKSFFYKEVFESRNGDYAREGGRFFPRERKRFRGQERPDDFTASVSEGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLLKHAKEVVSDLIDSFLRNLHSVTGTLMTDTQFVSAVKRTVFSHGSQKATDIMDAMLRKLYNVMFAKKVPEHVRKAQDKAESYSLISMKGMGDPKNRNVNFAMKSETKLREKMYSEPKSEEETCAKTLGEHIIKEGLTLWHKSQQKECKSLGFQHAAFEAPNTQRKPASDISFEYPEDIGNLSLPPYPPEKPENFMYDSDSWAKDLIVSALLLIQYHLAQGGRRDARSFVEAAGTTNFPANEPPVAPDESCLKSAPIVGDQEQAEKKDLRSVFFNFIRNLLSETIFKRDQSPEPKVPEQPVKEDRKLCERPLASSPPRLYEDDETPGALSGLTKMAVSQIDGHMSGQMVEHLMNSVMKLCVIIAKSCDASLAELGDDKSGDASRLTSAFPDSLYECLPAKGTGSAEAVLQNAYQAIHNEMRGTSGQPPEGCAAPTVIVSNHNLTDTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSAAAVDKGCSVGEVLQSVLRYEKERQLNEAVGNVTPLQLLDWLMVNL Q9Y250 Q9Y5V7 Q9Y5V8 Q9Y5V9 Q9Y5W0 Q9Y5W1 Q9Y5W2 LZTS1_HUMAN Leucine zipper putative tumor suppressor 1 F37/esophageal cancer-related gene-coding leucine-zipper motif Fez1 LZTS1 FEZ1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein, and its expression is altered in multiple human tumors. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7) VARIANTS ESOPHAGEAL CANCER PRO-29 AND GLU-119 FUNCTION TISSUE SPECIFICITY The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Fetal brain Functional identification of LZTS1 as a candidate prostate tumor suppressor gene on human chromosome 8p22. FUNCTION ALTERNATIVE SPLICING FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis. FUNCTION PHOSPHORYLATION SUBCELLULAR LOCATION INTERACTION WITH EEF1G AND CDC2 Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as tumor suppressor. Binds EEF1G and CDC2. P30307 false 1 Cytoplasm (By similarity). Cell membrane (By similarity). Cell projection, dendritic spine (By similarity). Cell junction, synapse, postsynaptic cell membrane, postsynaptic density (By similarity). Cell junction, synapse (By similarity). Note=Associated with the plasma membrane and with microtubules. Detected in dendritic spines, especially in the postsynaptic density. Q9Y250-1 1 Q9Y250-2 2 Q9Y250-3 3 Q9Y250-4 4 Q9Y250-5 5 Q9Y250-6 6 Q9Y250-7 7 Highly expressed in testis, prostate, spleen, thymus, ovary and brain. Detected at lower levels in heart, placenta, small intestine, colon, liver, kidney, skeletal muscle and pancreas. Not detectable in primary tumors from breast and prostate and in many cancer cell lines. Phorphorylated on serine residues. Hyperphosphorylated by the cAMP-dependent kinase PKA during cell-cycle progression. Defects in LZTS1 are found in many types of tumors. Belongs to the LZTS family. Alternative splicing Anti-oncogene Cell cycle Cell junction Cell projection Coiled coil Cytoplasm Lipoprotein Membrane Myristate Phosphoprotein Polymorphism Postsynaptic cell membrane Synapse SSSKMGKSEDFFYIKVSQKARG AMTRCPRASSMSGSC GRRRRRR S P K E L V MGSVSSLISGHSFHSKHCRASQYKLRKSSHLKKLNRYSDGLLRFGFSQDSGHGKSSSKMGKSEDFFYIKVSQKARGSHHPDYTALSSGDLGGQAGVDFDPSTPPKLMPFSNQLEMGSEKGAVRPTAFKPVLPRSGAILHSSPESASHQLHPAPPDKPKEQELKPGLCSGALSDSGRNSMSSLPTHSTSSSYQLDPLVTPVGPTSRFGGSAHNITQGIVLQDSNMMSLKALSFSDGGSKLGHSNKADKGPSCVRSPISTDECSIQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGPPTFPEDVPALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVDLEGADIPYEDIIATEI P19838 Q68D84 Q86V43 Q8N4X7 Q9NZC0 NFKB1_HUMAN Nuclear factor NF-kappa-B p105 subunit DNA-binding factor KBF1 EBP-1 Nuclear factor NF-kappa-B p50 subunit NFKB1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA binding subunit of NF-kappa B is identical to factor KBF1 and homologous to the rel oncogene product. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) PARTIAL PROTEIN SEQUENCE Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding protein with homology to the rel oncogene and to cell-cycle motifs. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Cloning of the DNA-binding subunit of human nuclear factor kappa B: the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) PARTIAL PROTEIN SEQUENCE The complete exon-intron structure of the 156-kb human gene NFKB1, which encodes the p105 and p50 proteins of transcription factors NF-kappa B and I kappa B-gamma: implications for NF-kappa B-mediated signal transduction. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Genome sequencing of the chromosome 4q region implicated in human hepatocellular carcinoma pathogenesis. NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Rectum tumor NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu). NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS ILE-489; VAL-506; ILE-566; LYS-578; GLN-711 AND THR-901 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Muscle Uterus The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. UBIQUITINATION A glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit. PROTEOLYTIC PROCESSING OF P105 GENERATION OF P50 AND P105 Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome. COTRANSLATIONAL FOLDING/PROCESSING OF P105 GENERATION OF P50/P105 NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes. MUTAGENESIS OF SER-921; SER-923 AND SER-932 TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105. INTERACTION WITH MAP3K8 Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production. COTRANSLATIONAL FOLDING/PROCESSING OF P105 GENERATION OF P50/P105 P50/P105 TRANSIENT HETERODIMER FORMATION RAC-3 is a NF-kappa B coactivator. INTERACTION WITH NCOA3 Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappa B. INTERACTION WITH DSIPI Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase complex on serine 927 is essential for signal-induced p105 proteolysis. PHOSPHORYLATION AT SER-927 Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10. INTERACTION WITH DSIPI Identification of a ZU5 and death domain-containing inhibitor of NF-kappaB. INTERACTION WITH UNC5CL A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. INTERACTION WITH SPAG9 Structure of the NF-kappa B p50 homodimer bound to DNA. X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-365 Structure of an IkappaBalpha/NF-kappaB complex. X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-354 Appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. Plays a role in the regulation of apoptosis. Active NF-kappa-B is a heterodimer of an about 50 kDa DNA-binding subunit and the weak DNA-binding subunit p65. Two heterodimers might form a labile tetramer. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. Q13547 false 2 Q14690 false 1 O60271 false 1 Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). P19838-1 1 P19838-2 2 By phorbol ester and TNF-alpha. The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation. Glycine-rich region (GRR) appears to be a critical element in the generation of p50. While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing. Polyubiquitination seems to allow p105 processing. Contains 7 ANK repeats. Contains 1 death domain. Contains 1 RHD (Rel-like) domain. 3D-structure Activator Alternative splicing ANK repeat Apoptosis Cytoplasm Direct protein sequencing DNA-binding Nucleus Phosphoprotein Polymorphism Repeat Transcription Transcription regulation Ubl conjugation T TA T I M V T I R K H Q A T S A S A S A K SE R G II SS A V I T V I S T MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI O95477 Q96S56 Q96T85 Q9NQV4 Q9UN06 Q9UN07 Q9UN08 Q9UN09 ABCA1_HUMAN ATP-binding cassette sub-family A member 1 ATP-binding cassette transporter 1 ATP-binding cassette 1 ABC-1 Cholesterol efflux regulatory protein ABCA1 ABC1 CERP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete genomic sequence of the human ABCA1 gene: analysis of the human and mouse ATP-binding cassette A promoter. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] ABCA1 gene expression and apoA-I-mediated cholesterol efflux are regulated by LXR. NUCLEOTIDE SEQUENCE Skin Human and mouse ABCA1 comparative sequencing and transgenesis studies revealing novel regulatory sequences. NUCLEOTIDE SEQUENCE [GENOMIC DNA] A new topological model of functional human ABCA1-signal peptide cleavage and glycosylation of a large extracellular domain. NUCLEOTIDE SEQUENCE Molecular cloning of the human ATP-binding cassette transporter 1 (hABC1): evidence for sterol-dependent regulation in macrophages. NUCLEOTIDE SEQUENCE [MRNA] OF 21-2261 Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 21-2261 Protein kinase A site-specific phosphorylation regulates ATP-binding cassette A1 (ABCA1)-mediated phospholipid efflux. PHOSPHORYLATION AT SER-1042 AND SER-2054 The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a modulator of cellular lipid efflux. REPRESSION BY ZNF202 Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway. INDUCTION BY LIPOPOLYSACCHARIDE Cooperation between engulfment receptors: the case of ABCA1 and MEGF10. INTERACTION WITH MEGF10 Efflux and atherosclerosis: the clinical and biochemical impact of variations in the ABCA1 gene. REVIEW ON VARIANTS Mutations in the ABC1 gene in familial HDL deficiency with defective cholesterol efflux. VARIANTS HDLD2 THR-1091 AND 1893-GLU-ASP-1894 DEL Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency. VARIANTS HDLD1 ARG-597 AND ARG-1477 VARIANT HDLD2 LEU-693 DEL The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease. VARIANTS HDLD1 SER-590; SER-935 AND VAL-937 VARIANTS ALA-399 AND MET-883 Age and residual cholesterol efflux affect HDL cholesterol levels and coronary artery disease in ABCA1 heterozygotes. VARIANTS HDLD1 ARG-597; ILE-929 AND ARG-1477 VARIANTS HDLD2 LEU-693 DEL; THR-1091; 1893-GLU-ASP-1894 DEL AND LEU-2150 Novel mutations in the gene encoding ATP-binding cassette 1 in four tangier disease kindreds. VARIANTS HDLD1 ASN-1289 AND HIS-1800 Common and rare ABCA1 variants affecting plasma HDL cholesterol. VARIANT HDLD1 ASP-1046 VARIANT HDLD2 CYS-230 VARIANTS LYS-219; ILE-825; MET-883 AND LYS-1587 A point mutation in ABC1 gene in a patient with severe premature coronary heart disease and mild clinical phenotype of Tangier disease. VARIANT HDLD1 TRP-587 VARIANT LEU-2168 Common variants in the gene encoding ATP-binding cassette transporter 1 in men with low HDL cholesterol levels and coronary heart disease. VARIANTS LYS-219; MET-883 AND ASP-1172 Homogeneous assay based on 52 primer sets to scan for mutations of the ABCA1 gene and its application in genetic analysis of a new patient with familial high-density lipoprotein deficiency syndrome. VARIANT HDLD1 LEU-1506 Novel mutations in ABCA1 gene in Japanese patients with Tangier disease and familial high density lipoprotein deficiency with coronary heart disease. VARIANTS HDLD1 ASN-1289 AND TRP-2081 VARIANT LYS-219 Common genetic variation in ABCA1 is associated with altered lipoprotein levels and a modified risk for coronary artery disease. VARIANTS LYS-219; ALA-399; MET-771; PRO-774; ASN-776; ILE-825; MET-883; ASP-1172; LYS-1587 AND CYS-1731 ABCA1(Alabama): a novel variant associated with HDL deficiency and premature coronary artery disease. VARIANT HDLD2 LEU-85 Novel ABCA1 compound variant associated with HDL cholesterol deficiency. VARIANT HDLD2 TYR-1099 Expression and functional analyses of novel mutations of ATP-binding cassette transporter-1 in Japanese patients with high-density lipoprotein deficiency. VARIANT HDLD1 THR-255 VARIANT ATHEROSCLEROSIS ASP-1611 Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. VARIANTS LYS-219; MET-771; ILE-825; MET-883; ASP-1172; PHE-1181 AND LYS-1587 A common variant in the ABCA1 gene is associated with a lower risk for premature coronary heart disease in familial hypercholesterolaemia. VARIANT LYS-219 The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] ASP-210; TYR-917; THR-1407 AND THR-2109 cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport. Interacts with MEGF10. O15085 false 1 Q9NZN5 false 1 Q15700 false 1 Q92796 false 1 Q9Z250 true 1 Q9HAP6 false 1 O88952 true 1 O75970 false 1 Q13424 false 1 Q13884 false 2 Widely expressed, but most abundant in macrophages. By bacterial lipopolysaccharides (LPS). LPS regulates expression through a liver X receptor (LXR) -independent mechanism. Repressed by ZNF202. Multifunctional polypeptide with two homologous halves, each containing an hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain. Phosphorylation on Ser-2054 regulates phospholipid efflux. Defects in ABCA1 are a cause of high density lipoprotein deficiency type 1 (HDLD1) [MIM:205400]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by absence of high density lipoprotein (HDL) cholesterol from plasma, accumulation of cholesteryl esters, premature coronary artery disease (CAD), hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness{EC3,EC4,EC5,EC6,EC7,EC8,EC9,EC10,EC11}. Defects in ABCA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:604091]; also known as familial hypoalphalipoproteinemia (FHA). HDLD2 is inherited as autosomal dominant trait. It is characterized by moderately low HDL cholesterol, predilection toward premature coronary artery disease (CAD) and a reduction in cellular cholesterol efflux. Belongs to the ABC transporter family. ABCA subfamily. Contains 2 ABC transporter domains. The Singapore human mutation and polymorphism database Atherosclerosis ATP-binding Cholesterol metabolism Disease mutation Glycoprotein Lipid metabolism Membrane Nucleotide-binding Phosphoprotein Polymorphism Repeat Steroid metabolism Transmembrane Transport P L E D R K R C A T V A R W W S Q R V M T P K N V I I M D Y T I N S A V A D M T D Y E D S F D N A T C R S L I R T I R K N D P L S C N H R W A T P L P L Y C D N E K MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDATKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTRNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVAPMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVPKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV P22460 Q4KKT8 Q4VAJ1 Q4VAJ2 KCNA5_HUMAN Potassium voltage-gated channel subfamily A member 5 Voltage-gated potassium channel subunit Kv1.5 HK2 HPCN1 KCNA5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle. NUCLEOTIDE SEQUENCE [MRNA] Heart Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel. NUCLEOTIDE SEQUENCE [MRNA] Insulinoma Molecular cloning, characterization, and genomic localization of a human potassium channel gene. NUCLEOTIDE SEQUENCE [MRNA] Heart The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] SER-300 Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potasssium ions may pass in accordance with their electrochemical gradient. May play a role in regulating the secretion of insulin in normal pancreatic islets. Heterotetramer of potassium channel proteins. Interacts via its PDZ-binding motif with DLG1. Forms a ternary complex with DLG1 and CAV3. Membrane; Multi-pass membrane protein. Pancreatic islets and insulinoma. The amino terminus may be important in determining the rate of inactivation of the channel while the C-terminal PDZ-binding motif may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Belongs to the potassium channel family. A (Shaker) subfamily. Glycoprotein Ion transport Ionic channel Lipoprotein Membrane Palmitate Phosphoprotein Polymorphism Potassium Potassium channel Potassium transport Repeat Transmembrane Transport Voltage-gated channel G S L Q R P RP G R G P V L V P A GSCPLEKCNVKAKSNVDLRRSLYALCLDTSRETDL QLPPREV MEIALVPLENGGAMTVRGGDEARAGCGQATGGELQCPPTAGLSDGPKEPAPKGRGAQRDADSGVRPLPPLPDPGVRPLPPLPEELPRPRRPPPEDEEEEGDPGLGTVEDQALGTASLHHQRVHINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPAPHQPPAPAPGANGSGVMAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAGFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEPAVLKEEQGTQSQGPGLDRGVQRKVSGSRGSFCKAGGTLENADSARRGSCPLEKCNVKAKSNVDLRRSLYALCLDTSRETDL O15530 PDPK1_HUMAN 3-phosphoinositide-dependent protein kinase 1 hPDK1 PDPK1 PDK1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3) Myeloid The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Kidney Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B. MUTAGENESIS OF ARG-474 ALTERNATIVE SPLICING Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo. PHOSPHORYLATION AT SER-25; SER-241; SER-393; SER-396 AND SER-410 MUTAGENESIS OF SER-25; SER-241; SER-393; SER-396 AND SER-410 A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans. MUTAGENESIS OF ALA-277 Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity. PHOSPHORYLATION AT TYR-9; SER-241; TYR-373 AND TYR-376 MUTAGENESIS OF TYR-9; TYR-373 AND TYR-376 Large-scale characterization of HeLa cell nuclear phosphoproteins. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 MASS SPECTROMETRY Epithelium Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-245 MASS SPECTROMETRY Epithelium Phosphoproteomic analysis of the human pituitary. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 MASS SPECTROMETRY Pituitary Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development (By similarity). Isoform 3 is catalytically inactive. ATP + a protein = ADP + a phosphoprotein. Cytoplasm. Membrane; Peripheral membrane protein. Note=Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane. O15530-1 1 O15530-2 2 O15530-3 3 Appears to be expressed ubiquitously. Phosphorylated on tyrosine and serine/threonine. Phosphorylation on Ser-241 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Ser-241, leading to its own activation. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDK1 subfamily. Contains 1 PH domain. Contains 1 protein kinase domain. 3D-structure Alternative splicing ATP-binding Cytoplasm Kinase Membrane Nucleotide-binding Phosphoprotein Serine/threonine-protein kinase Transferase Y F S A S A A V Y F Y F S A S A S A R A MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ Q92934 O14803 BAD_HUMAN Bcl2 antagonist of cell death BAD Bcl-2-binding component 6 Bcl-XL/Bcl-2-associated death promoter Bcl-2-like 8 protein BAD BBC6 BCL2L8 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A human protein that interacts with Bcl-2 and have homology to mouse BAD. NUCLEOTIDE SEQUENCE [MRNA] Bcl-2 targets the protein kinase Raf-1 to mitochondria. NUCLEOTIDE SEQUENCE [MRNA] PHOSPHORYLATION BY RAF-1 NUCLEOTIDE SEQUENCE [MRNA] Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins. NUCLEOTIDE SEQUENCE [MRNA] DIMERIZATION Bone marrow Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. STRUCTURE BY NMR OF 103-127 Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity). The Ser-75/Ser-99 phosphorylated form binds 14-3-3 proteins. P10415 false 3 Q07817-1 false 3 Q92843 false 1 O60238 false 1 P62136 false 1 Mitochondrion outer membrane. Cytoplasm. Note=Upon phosphorylation, locates to the cytoplasm. Expressed in a wide variety of tissues. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Belongs to the Bcl-2 family. Bcl 2-associated death promoter entry 3D-structure Apoptosis Cytoplasm Membrane Mitochondrion Phosphoprotein Polymorphism A S MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSHHGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ Q93100 Q8N4T5 KPBB_HUMAN Phosphorylase b kinase regulatory subunit beta Phosphorylase kinase subunit beta PHKB Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Structure of the human gene encoding the phosphorylase kinase beta subunit (PHKB). NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] ALTERNATIVE SPLICING The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) Uterus Autosomal recessive phosphorylase kinase deficiency in liver, caused by mutations in the gene encoding the beta subunit (PHKB). VARIANT CYS-770 Phosphorylase-kinase-deficient liver glycogenosis with an unusual biochemical phenotype in blood cells associated with a missense mutation in the beta subunit gene (PHKB). VARIANT GSD9B PRO-118 Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases. VARIANTS LYS-657 AND CYS-770 The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] VAL-867 AND ARG-877 Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation. By phosphorylation of various serine residues. Glycan biosynthesis; glycogen metabolism. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. Cell membrane; Lipid-anchor; Cytoplasmic side . Q93100-1 1 Q93100-2 2 Q93100-3 3 Q93100-4 4 Defects in PHKB are the cause of glycogen storage disease type 9B (GSD9B) [MIM:261750]; also known as phosphorylase kinase deficiency of liver and muscle (PKD). GSD9B is a metabolic disorder characterized by hepathomegaly, only slightly elevated transaminases and plasma lipids, clinical improvement with increasing age, and remarkably no clinical muscle involvement. Biochemical observations suggest that this mild phenotype is caused by an incomplete holoenzyme that lacks the beta subunit, but that may possess residual activity. Belongs to the phosphorylase b kinase regulatory chain family. Acetylation Alternative splicing Calmodulin-binding Carbohydrate metabolism Disease mutation Glycogen metabolism Glycogen storage disease Lipoprotein Membrane Phosphoprotein Polymorphism Prenylation MAGAAGLTAEVSWKVLERRARTK MACSPDAVVSPSSA FL LAVRYGAAFTQKFSSSIAPHITTFLVH SVVRRAASLL SKVVDSLAPSITNVLVQ A P Q K Y C E V L V G R MAGAAGLTAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDHYYRIVKSTLLLYQSPTTGLFPTKTCGGDQKAKIQDSLYCAAGAWALALAYRRIDDDKGRTHELEHSAIKCMRGILYCYMRQADKVQQFKQDPRPTTCLHSVFNVHTGDELLSYEEYGHLQINAVSLYLLYLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCISYPAFALDDEVLFSQTLDKVVRKLKGKYGFKRFLRDGYRTSLEDPNRCYYKPAEIKLFDGIECEFPIFFLYMMIDGVFRGNPKQVQEYQDLLTPVLHHTTEGYPVVPKYYYVPADFVEYEKNNPGSQKRFPSNCGRDGKLFLWGQALYIIAKLLADELISPKDIDPVQRYVPLKDQRNVSMRFSNQGPLENDLVVHVALIAESQRLQVFLNTYGIQTQTPQQVEPIQIWPQQELVKAYLQLGINEKLGLSGRPDRPIGCLGTSKIYRILGKTVVCYPIIFDLSDFYMSQDVFLLIDDIKNALQFIKQYWKMHGRPLFLVLIREDNIRGSRFNPILDMLAALKKGIIGGVKVHVDRLQTLISGAVVEQLDFLRISDTEELPEFKSFEELEPPKHSKVKRQSSTPSAPELGQQPDVNISEWKDKPTHEILQKLNDCSCLASQAILLGILLKREGPNFITKEGTVSDHIERVYRRAGSQKLWLAVRYGAAFTQKFSSSIAPHITTFLVHGKQVTLGAFGHEEEVISNPLSPRVIQNIIYYKCNTHDEREAVIQQELVIHIGWIISNNPELFSGMLKIRIGWIIHAMEYELQIRGGDKPALDLYQLSPSEVKQLLLDILQPQQNGRCWLNRRQIDGSLNRTPTGFYDRVWQILERTPNGIIVAGKHLPQQPTLSDMTMYEMNFSLLVEDTLGNIDQPQYRQIVVELLMVVSIVLERNPELEFQDKVDLDRLVKEAFNEFQKDQSRLKEIEKQDDMTSFYNTPPLGKRGTCSYLTKAVMNLLLEGEVKPNNDDPCLIS Q96PU5 O43165 Q7Z5F1 Q7Z5F2 Q7Z5N3 Q8N5A7 Q8WUU9 Q9BW58 Q9H2W4 Q9NT88 NED4L_HUMAN E3 ubiquitin-protein ligase NEDD4-like protein Nedd4-2 NEDD4.2 NEDD4L KIAA0439 NEDL3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NEDD4L on human chromosome 18q21 has multiple forms of transcripts and is a homologue of the mouse Nedd4-2 gene. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4) ALTERNATIVE SPLICING Identification of new partners of the epithelial sodium channel alpha subunit. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G Kidney Androgens differentially regulate the expression of NEDD4L transcripts in LNCaP human prostate cancer cells. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 7) TISSUE SPECIFICITY INDUCTION Prostate Homo sapiens NEDD4-like ubiquitin ligase 3. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5) The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-975 (ISOFORM 5) Skin Uterus Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 8) Brain NUCLEOTIDE SEQUENCE [MRNA] OF 52-975 (ISOFORM 3) Testis 14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase. PROTEIN SEQUENCE OF 448-462 INTERACTION WITH YWHAB; YWHAG; YWHAE; YWHAQ AND YWHAH PHOSPHORYLATION AT SER-448 MUTAGENESIS OF SER-448 MASS SPECTROMETRY Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. INTERACTION WITH SGK AND SCNN1A PHOSPHORYLATION N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein. INTERACTION WITH NDFIP1 Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B. FUNCTION Cardiac voltage-gated sodium channel Nav1.5 is regulated by Nedd4-2 mediated ubiquitination. FUNCTION MUTAGENESIS OF CYS-942 INTERACTION WITH SCN5A Nedd4-2 functionally interacts with ClC-5: involvement in constitutive albumin endocytosis in proximal tubule cells. FUNCTION INTERACTION WITH CLCN5 INDUCTION cAMP and serum and glucocorticoid-inducible kinase (SGK) regulate the epithelial Na(+) channel through convergent phosphorylation of Nedd4-2. PHOSPHORYLATION AT SER-342; THR-367 AND SER-448 Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1. FUNCTION Molecular determinants of voltage-gated sodium channel regulation by the Nedd4/Nedd4-like proteins. INTERACTION WITH SCN2A; SCN3A AND SCN5A NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor. FUNCTION INTERACTION WITH SMAD2; SMAD3; SMAD6 AND SMAD7 SUBCELLULAR LOCATION TISSUE SPECIFICITY Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation. FUNCTION Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-483 AND SER-487 MASS SPECTROMETRY Epithelium A naturally occurring human Nedd4-2 variant displays impaired ENaC regulation in Xenopus laevis oocytes. VARIANTS LEU-355 AND ARG-497 E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Inhibits TGF-beta signaling by triggering SMAD2 and TGFR1 ubiquitination and proteasome-dependent degradation. Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of SGK. Protein degradation; protein ubiquitinylation. Interacts with NDFIP2 and UBE2E3 (By similarity). Interacts via its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A, SCN2A, SCN3A, SCN5A, SCN8A, SCN9A, SCN10A and CLCN5. Interacts with SMAD2, SMAD3, SMAD6 and SMAD7. The phosphorylated form interacts with 14-3-3 proteins. Interacts with Epstein-Barr virus LMP2A. Interacts with NDFIP1 in vitro. Cytoplasm. Q96PU5-1 1 Nedd4-2c Q96PU5-2 2 No experimental confirmation available Q96PU5-3 3 NEDD4Le No experimental confirmation available Q96PU5-4 4 NEDD4La,NEDD4Lb,NEDD4Lf Q96PU5-5 5 NEDD4Ld Q96PU5-6 6 NEDD4Lh Q96PU5-7 7 NEDD4Lg Q96PU5-8 8 NEDD4Lc,Nedd4-2a Incomplete sequence Ubiquitously expressed, with highest levels in prostate, pancreas and kidney. By androgens in prostate, and by albumin in kidney. Phosphorylated by SGK or PKA; which impairs interaction with SCNN. Interaction with YWHAH inhibits dephosphorylation. Contains 1 C2 domain. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 4 WW domains. 3D-structure Alternative splicing Cytoplasm Direct protein sequencing Host-virus interaction Ligase Phosphoprotein Polymorphism Repeat Ubl conjugation pathway MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGAS PGGWLRRALPGRERLQSPVHAVPPQHGTSHSRLLVTWP GAGRDQDFSSPPLLLLGETDHLHLDLPLSPLPTSDELFLPG IC MATGLGEPVYGLSEDE MRRLAFEQ P L S R S A C S A P E K MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGSRTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPAGRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKTSLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD P60853 LZTS1_MOUSE Leucine zipper putative tumor suppressor 1 F37/Esophageal cancer-related gene-coding leucine-zipper motif Fez1 Lzts1 Fez1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Sciurognathi Muroidea Muridae Murinae Mus The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein, and its expression is altered in multiple human tumors. NUCLEOTIDE SEQUENCE [MRNA] 129/J Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as tumor suppressor. Binds EEF1G and CDC2. Cytoplasm (By similarity). Cell membrane (By similarity). Cell projection, dendritic spine (By similarity). Cell junction, synapse, postsynaptic cell membrane, postsynaptic density (By similarity). Cell junction, synapse (By similarity). Note=Associated with the plasma membrane and with microtubules. Detected in dendritic spines, especially in the postsynaptic density. Phorphorylated on serine residues. Hyperphosphorylated by the cAMP-dependent kinase PKA during cell-cycle progression. Belongs to the LZTS family. Anti-oncogene Cell cycle Cell junction Cell projection Coiled coil Cytoplasm Lipoprotein Membrane Myristate Phosphoprotein Postsynaptic cell membrane Synapse MGSVSSLISGHSFHSKHCRASQYKLRKSSHLKKLNRYSDGLLRFGFSQDSGRGKSSSKMGKSEDFFYIKVSQKARGSHRPDYTALSSGDMGGQTGVDFDPATPPKLMPFSNQLEMSSDKGAVRPTAFKPVLPRSGAILHSSPESTSHQLHPMPPDKPKEQELKPGLCSGALSDSGRNSMSSLPTHSTTSSYQLDPLVTPVGPTSRFGGSAHNITQGIILQDSNMMSLKALSFSDGGSKLAHPGKADKGASCVRSPLSTDECTIQELEQKLLQRETALQKLQRSFDEKEFASGQTFEERPRRTRDELECLEPKSKLKPPSQKSQRTQQVLQLQVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQLEVNTKASEILSLKAQLKDTRGKLDGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELMELRAQAALHPAPLGPPGVGLTFSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEEKEKVIQYQRQLQQSYLAMYQRNQRLEKALQQLARGDGPGEPFEIDLEGADIPYEDIIATEI Q7Z6R9 Q8IWX0 AP2D_HUMAN Transcription factor AP-2 delta AP2-delta Activating enhancer-binding protein 2 delta Transcription factor AP-2 beta-like 1 TFAP2D TFAP2BL1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of a novel human transcription factor AP-2 beta like gene (TFAP2BL1). NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] PHE-214 Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Nucleus. Highly expressed in brain, placenta, skeletal muscle, thymus, small intestine, and prostate, and expressed at lower levels in leukocyte, spleen, testis, ovary and colon. Barely detectable in heart, kidney, liver, lung or pancreas. Belongs to the AP-2 family. Activatin protein 2 entry Activator DNA-binding Nucleus Phosphoprotein Polymorphism Transcription Transcription regulation V F H Y S N MSTTFPGLVHDAEIRHDGSNSYRLMQLGCLESVANSTVAYSSSSPLTYSTTGTEFASPYFSTNHQYTPLHHQSFHYEFQHSHPAVTPDAYSLNSLHHSQQYYQQIHHGEPTDFINLHNARALKSSCLDEQRRELGCLDAYRRHDLSLMSHGSQYGMHPDQRLLPGPSLGLAAAGADDLQGSVEAQCGLVLNGQGGVIRRGGTCVVNPTDLFCSVPGRLSLLSSTSKYKVTIAEVKRRLSPPECLNASLLGGILRRAKSKNGGRCLREKLDRLGLNLPAGRRKAANVTLLTSLVEGEALHLARDFGYTCETEFPAKAVGEHLARQHMEQKEQTARKKMILATKQICKEFQDLLSQDRSPLGSSRPTPILDLDIQRHLTHFSLITHGFGTPAICAALSTFQTVLSEMLNYLEKHTTHKNGGAADSGQGHANSEKAPLRKTSEAAVKEGKTEKTD Q96T88 Q8J022 Q9H6S6 Q9P115 Q9P1U7 UHRF1_HUMAN E3 ubiquitin-protein ligase UHRF1 Ubiquitin-like PHD and RING finger domain-containing protein 1 Ubiquitin-like-containing PHD and RING finger domains protein 1 Inverted CCAAT box-binding protein of 90 kDa Transcription factor ICBP90 Nuclear zinc finger protein Np95 Nuclear protein 95 HuNp95 RING finger protein 106 UHRF1 ICBP90 NP95 RNF106 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo ICBP90, a novel human CCAAT binding protein, involved in the regulation of topoisomerase IIa expression. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY DEVELOPMENTAL STAGE SUBCELLULAR LOCATION DNA-BINDING INDUCTION FUNCTION Thymus LMO2-induced T cell leukemias overexpress Np95, a gene containing RING and PHD zinc fingers and an ubiquitin-like domain. NUCLEOTIDE SEQUENCE [MRNA] NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu). NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS HIS-240; LYS-379; THR-638; MET-642 AND PHE-713 The DNA sequence and biology of human chromosome 19. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 479-745 Genomic structure and chromosomal mapping of the gene coding for huNp95, a protein involved in DNA repair and DNA replication processes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 607-745 ICBP90 belongs to a new family of proteins with an expression that is deregulated in cancer cells. INDUCTION TISSUE SPECIFICITY Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase IIalpha expression. PHOSPHORYLATION PHOSPHORYLATION AT SER-298 MUTAGENESIS OF SER-298; SER-651 AND SER-666 Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-dependent DNA-damage checkpoint signals contributes to cell cycle arrest at G1/S transition. INDUCTION UBIQUITINATION FUNCTION ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. FUNCTION INDUCTION TISSUE SPECIFICITY DNA-BINDING INTERACTION WITH HDAC1 AND UHRF1BP1 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-639 MASS SPECTROMETRY Epithelium A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639 MASS SPECTROMETRY Epithelium Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-385 MASS SPECTROMETRY Ubiquitin-like domain of human nuclear zinc finger protein NP95. X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-76 Putative E3 ubiquitin-protein ligase. May participate in methylation-dependent transcriptional regulation. Binds to inverted 5'-CCAAT-3' box 2 in the TOP2A promoter, and activates TOP2A expression. Important for G1/S transition. May be involved in DNA repair and chromosomal stability. Protein degradation; protein ubiquitinylation. Interacts with histones H3, H1 and H2B (By similarity). Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Binds methylated CpG containing oligonucleotides. Nucleus. Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. Expressed in fetal thymus, liver and kidney. Up-regulated in proliferating cells, and down-regulated in quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in a TP53/p53 and CDKN1A-dependent way. Induced by E2F1 transcription factor. The RING finger is required for ubiquitin ligase activity. The YDG domain mediates the interaction with histone H3. Phosphorylated on serine residues. Phosphorylation may enhance DNA-binding activity. Ubiquitinated; which leads to proteasomal degradation. Polyubiquitination may be stimulated by DNA damage. Contains 1 PHD-type zinc finger. Contains 2 RING-type zinc fingers. Contains 1 ubiquitin-like domain. Contains 1 YDG domain. 3D-structure Cell cycle DNA damage DNA repair DNA-binding Ligase Metal-binding Nucleus Phosphoprotein Polymorphism Transcription Transcription regulation Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger D H E K A T T M L F S A S A S A K N A S MWIQVRTMDGRQTHTVDSLSRLTKVEELRRKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYEVRLNDTIQLLVRQSLVLPHSTKERDSELSDTDSGCCLGQSESDKSSTHGEAAAETDSRPADEDMWDETELGLYKVNEYVDARDTNMGAWFEAQVVRVTRKAPSRDEPCSSTSRPALEEDVIYHVKYDDYPENGVVQMNSRDVRARARTIIKWQDLEVGQVVMLNYNPDNPKERGFWYDAEISRKRETRTARELYANVVLGDDSLNDCRIIFVDEVFKIERPGEGSPMVDNPMRRKSGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDEWYCPECRNDASEVVLAGERLRESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHYGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDHGNFFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDQEGAEAKDWRSGKPVRVVRNVKGGKNSKYAPAEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDDEPGPWTKEGKDRIKKLGLTMQYPEGYLEALANREREKENSKREEEEQQEGGFASPRTGKGKWKRKSAGGGPSRAGSPRRTSKKTKVEPYSLTAQQSSLIREDKSNAKLWNEVLASLKDRPASGSPFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQTVLNQLFPGYGNGR P50552 Q6PIZ1 Q93035 VASP_HUMAN Vasodilator-stimulated phosphoprotein VASP VASP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 11-32; 87-96; 140-154; 255-282 AND 297-322 SUBCELLULAR LOCATION TISSUE SPECIFICITY POSSIBLE FUNCTION Promyelocyte Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION INTERACTION WITH L.MONOCYTOGENES ACTA The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Fetal lung Fetal spleen Skin Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 2-10 ACETYLATION AT SER-2 Platelet Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-380 cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285 PHOSPHORYLATION AT SER-157; SER-239 AND THR-278 Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition. PHOSPHORYLATION AT SER-157 FIBRINOGEN RECEPTOR INHIBITION The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. INTERACTION WITH ACTG1 AND PFN1 The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. FUNCTION OF EVH2 DOMAIN Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. INTERACTION WITH ZYX LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. INTERACTION WITH LPP Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. INTERACTION WITH RAPH1 Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C. PHOSPHORYLATION BY PKC Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. FUNCTION Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 MASS SPECTROMETRY Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser 157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. PHOSPHORYLATION AT SER-157 SUBCELLULAR LOCATION Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 MASS SPECTROMETRY The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-380 TETRAMERIZATION MUTAGENESIS OF PHE-370 Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. STRUCTURE BY NMR OF 1-115 Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. VASP promotes actin nucleation and increases the rate of actin polymerization in the presence of capping protein. Plays a role in actin-based activity of Listeria monocytogenes in platelets. Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Highly expressed in platelets. The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Belongs to the Ena/VASP family. Contains 1 WH1 domain. 3D-structure Acetylation Actin-binding Cell junction Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Membrane Phosphoprotein Repeat SH3-binding F A F I K S SS MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQVGEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQELLEEVKKELQKVKEEIIEAFVQELRKRGSP Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.