UniProtKB - P46937 (YAP1_HUMAN)
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- BLAST>sp|P46937|YAP1_HUMAN Transcriptional coactivator YAP1 OS=Homo sapiens OX=9606 GN=YAP1 PE=1 SV=2 MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGD SETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTP QHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMA KTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAM TQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNS NQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGG TQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSV DEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSS DILNDMESVLAATKLDKESFLTWL
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Protein
Transcriptional coactivator YAP1
Gene
YAP1
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288). The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction (PubMed:18579750).6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.13"Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; SER-127 AND PRO-129, TISSUE SPECIFICITY. - Ref.15"TEAD mediates YAP-dependent gene induction and growth control."
Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y., Chinnaiyan A.M., Lai Z.C., Guan K.L.
Genes Dev. 22:1962-1971(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TEAD1; TEAD2; TEAD3 AND TEAD4, MUTAGENESIS OF SER-94. - Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.17"Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
Levy D., Adamovich Y., Reuven N., Shaul Y.
Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407, SUBCELLULAR LOCATION, INTERACTION WITH RUNX1 AND TP73. - Ref.21"JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis."
Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S.
Cell Death Dis. 1:E29-E29(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-119; SER-138; THR-154; SER-367 AND THR-412 BY MAPK8/JNK1 AND MAPK9/JNK2, FUNCTION. - Ref.31"YAP is essential for tissue tension to ensure vertebrate 3D body shape."
Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H., Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S., Miesfeld J.B., Link B.A., Senga T., Castillo-Morales A., Urrutia A.O. , Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H., Heisenberg C.P., Furutani-Seiki M.
Nature 521:217-221(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
Isoform 2: Isoform 2 and isoform 3 can activate the C-terminal fragment (CTF) of ERBB4 (isoform 3).1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus."
Komuro A., Nagai M., Navin N.E., Sudol M.
J. Biol. Chem. 278:33334-33341(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ERBB4, MUTAGENESIS OF SER-127; TRP-199 AND PRO-202.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- activating transcription factor binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- chromatin binding Source: Ensembl
- proline-rich region binding Source: Ensembl
- protein C-terminus binding Source: Ensembl
- protein heterodimerization activity Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA polymerase II proximal promoter sequence-specific DNA binding Source: Ensembl
- transcription coactivator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription corepressor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription factor activity, RNA polymerase II transcription factor binding Source: Ensembl
- transcription regulatory region DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- bud elongation involved in lung branching Source: Ensembl
- cell morphogenesis Source: Ensembl
- cell proliferation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to DNA damage stimulus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to gamma radiation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to retinoic acid Source: Ensembl
- contact inhibition Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- embryonic heart tube morphogenesis Source: Ensembl
- hippo signaling Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- keratinocyte differentiation Source: Ensembl
- lateral mesoderm development Source: Ensembl
- lung epithelial cell differentiation Source: Ensembl
- negative regulation of epithelial cell differentiation Source: Ensembl
- negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
- negative regulation of stem cell differentiation Source: Ensembl
- notochord development Source: Ensembl
- paraxial mesoderm development Source: Ensembl
- positive regulation of canonical Wnt signaling pathway Source: Ensembl
- positive regulation of cell proliferation Source: Ensembl
- positive regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of organ growth Source: Ensembl
- positive regulation of stem cell population maintenance Source: Ensembl
- positive regulation of transcription, DNA-templated Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription by RNA polymerase II Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- progesterone receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein complex assembly Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of hematopoietic stem cell differentiation Source: Reactome
- regulation of keratinocyte proliferation Source: Ensembl
- regulation of metanephric nephron tubule epithelial cell differentiation Source: Ensembl
- regulation of neurogenesis Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of stem cell proliferation Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to progesterone Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- somatic stem cell population maintenance Source: Ensembl
- transcription initiation from RNA polymerase II promoter Source: Reactome
- vasculogenesis Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Activator, Repressor |
| Biological process | Transcription, Transcription regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1251985. Nuclear signaling by ERBB4. R-HSA-1989781. PPARA activates gene expression. R-HSA-2028269. Signaling by Hippo. R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression. R-HSA-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs. R-HSA-8940973. RUNX2 regulates osteoblast differentiation. R-HSA-8951671. RUNX3 regulates YAP1-mediated transcription. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P46937. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P46937. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Transcriptional coactivator YAP1Short name: Yes-associated protein 1 Alternative name(s): Protein yorkie homolog Yes-associated protein YAP65 homolog |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:YAP1 Synonyms:YAP65 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000137693.13. |
Human Gene Nomenclature Database More...HGNCi | HGNC:16262. YAP1. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606608. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P46937. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.13"Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; SER-127 AND PRO-129, TISSUE SPECIFICITY. - Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.17"Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
Levy D., Adamovich Y., Reuven N., Shaul Y.
Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407, SUBCELLULAR LOCATION, INTERACTION WITH RUNX1 AND TP73. - Ref.22"A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-61; SER-109; SER-127 AND SER-164. - Ref.28"PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPN14, SUBCELLULAR LOCATION. - Ref.32"Loss of DLG5 promotes breast cancer malignancy by inhibiting the Hippo signaling pathway."
Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C., Wang R., Chen H., Zhou C., Zhang J., Yang J., Liu P.
Sci. Rep. 7:42125-42125(2017) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-127 AND SER-397.
- Nucleus 6 Publications
Other locations
- Cytoplasm 4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.17"Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
Levy D., Adamovich Y., Reuven N., Shaul Y.
Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407, SUBCELLULAR LOCATION, INTERACTION WITH RUNX1 AND TP73. - Ref.22"A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-61; SER-109; SER-127 AND SER-164. - Ref.28"PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPN14, SUBCELLULAR LOCATION.
Note: Both phosphorylation and cell density can regulate its subcellular localization. Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus. At low density, predominantly nuclear and is translocated to the cytoplasm at high density (PubMed:18158288, PubMed:20048001). PTPN14 induces translocation from the nucleus to the cytoplasm (PubMed:22525271).3 Publications- Cytoplasm 4 Publications
- Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.22"A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-61; SER-109; SER-127 AND SER-164. - Ref.28"PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPN14, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: Reactome
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- TEAD-1-YAP complex Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- TEAD-2-YAP complex Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- membrane Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim"><span class="caps">OMIM</span></a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Coloboma, ocular, with or without hearing impairment, cleft lip/palate, and/or mental retardation (COB1)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.29"Heterozygous loss-of-function mutations in YAP1 cause both isolated and syndromic optic fissure closure defects."
UK10K Consortium
Williamson K.A., Rainger J., Floyd J.A., Ansari M., Meynert A., Aldridge K.V., Rainger J.K., Anderson C.A., Moore A.T., Hurles M.E., Clarke A., van Heyningen V., Verloes A., Taylor M.S., Wilkie A.O., Fitzpatrick D.R., Hurles M., FitzPatrick D.R. , Al-Turki S., Anderson C., Barroso I., Beales P., Bentham J., Bhattacharya S., Carss K., Chatterjee K., Cirak S., Cosgrove C., Daly A., Floyd J., Franklin C., Futema M., Humphries S., McCarthy S., Mitchison H., Muntoni F., Onoufriadis A., Parker V., Payne F., Plagnol V., Raymond L., Savage D., Scambler P., Schmidts M., Semple R., Serra E., Stalker J., van Kogelenberg M., Vijayarangakannan P., Walter K., Wood G.
Am. J. Hum. Genet. 94:295-302(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN COB1, VARIANTS LEU-139; LEU-227; VAL-330 AND GLU-462.
Ref.29
"Heterozygous loss-of-function mutations in YAP1 cause both isolated and syndromic optic fissure closure defects."
UK10K Consortium
Williamson K.A., Rainger J., Floyd J.A., Ansari M., Meynert A., Aldridge K.V., Rainger J.K., Anderson C.A., Moore A.T., Hurles M.E., Clarke A., van Heyningen V., Verloes A., Taylor M.S., Wilkie A.O., Fitzpatrick D.R., Hurles M., FitzPatrick D.R. , Al-Turki S., Anderson C., Barroso I., Beales P., Bentham J., Bhattacharya S., Carss K., Chatterjee K., Cirak S., Cosgrove C., Daly A., Floyd J., Franklin C., Futema M., Humphries S., McCarthy S., Mitchison H., Muntoni F., Onoufriadis A., Parker V., Payne F., Plagnol V., Raymond L., Savage D., Scambler P., Schmidts M., Semple R., Serra E., Stalker J., van Kogelenberg M., Vijayarangakannan P., Walter K., Wood G.
Am. J. Hum. Genet. 94:295-302(2014) [PubMed] [Europe PMC] [Abstract]
UK10K Consortium
Williamson K.A., Rainger J., Floyd J.A., Ansari M., Meynert A., Aldridge K.V., Rainger J.K., Anderson C.A., Moore A.T., Hurles M.E., Clarke A., van Heyningen V., Verloes A., Taylor M.S., Wilkie A.O., Fitzpatrick D.R., Hurles M., FitzPatrick D.R. , Al-Turki S., Anderson C., Barroso I., Beales P., Bentham J., Bhattacharya S., Carss K., Chatterjee K., Cirak S., Cosgrove C., Daly A., Floyd J., Franklin C., Futema M., Humphries S., McCarthy S., Mitchison H., Muntoni F., Onoufriadis A., Parker V., Payne F., Plagnol V., Raymond L., Savage D., Scambler P., Schmidts M., Semple R., Serra E., Stalker J., van Kogelenberg M., Vijayarangakannan P., Walter K., Wood G.
Am. J. Hum. Genet. 94:295-302(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN COB1, VARIANTS LEU-139; LEU-227; VAL-330 AND GLU-462.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by uveal colobomata, microphthalmia, cataract and cleft lip/palate. Considerable variability is observed among patients, uveal colobomata being the most constant feature. Some patients manifest mental retardation of varying degree and/or sensorineural, mid-frequency hearing loss.
See also OMIM:120433Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 61 | S → A in YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-109; A-127 and A-164. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 80 | V → A: No change in interaction with TEAD4. Reduced interaction with TEAD4 and transforming ability; when associated with A-84 and A-85. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 84 | V → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-85. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 85 | P → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-84. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 86 | M → A: Complete loss of interaction with TEAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 89 | R → A: Complete loss of interaction with TEAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 91 | L → A: Complete loss of interaction with TEAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 94 | S → A: Loss of interaction with TEAD1, TEAD2, TEAD3 and TEAD4. Loss of transcriptional coactivation activity towards TEAD1, TEAD2, TEAD3 and TEAD4 but no effect on its activity towards RUNX2 and ERBB4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 95 | F → A: Complete loss of interaction with TEAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 96 | F → A: Loss of interaction with TEAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 109 | S → A in YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-127 and A-164. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 122 | H → A, R, N or K: Loss of phosphorylation by LATS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 122 | H → L or Y: Significantly decreased phosphorylation at S-127 and decreased interaction with YWHAB. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 124 | R → A: Loss of phosphorylation by LATS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 127 | S → A: Reduced phosphorylation by LATS2, loss of phosphorylation by LATS1, loss of interaction with YWHAB, decreased interaction with ERBB4 and increased nuclear localization and transcriptional coactivation activity toward ERBB4. In YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-109; A-127 and A-164. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 129 | P → D: No effect on phosphorylation but loss of interaction with YWHAB. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 164 | S → A in YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-109 and A-127. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 199 | W → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-202. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 202 | P → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-199. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 397 | S → A: Loss of phosphorylation by LATS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 407 | Y → E: Enhanced interaction with TP73. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 407 | Y → F: No phosphorylation by ABL1 and partial loss of binding to TP73. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 10413. |
MalaCards human disease database More...MalaCardsi | YAP1. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 120433. phenotype. |
Open Targets More...OpenTargetsi | ENSG00000137693. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 1473. Uveal coloboma - cleft lip and palate - intellectual disability. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA38103. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | YAP1. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 294862479. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000076071 | 1 – 504 | Transcriptional coactivator YAP1Add BLAST | 504 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 61 | Phosphoserine; by LATS1 and LATS2Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 63 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 105 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 109 | Phosphoserine; by LATS1 and LATS2Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 110 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 119 | Phosphothreonine; by MAPK8 and MAPK9Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 127 | Phosphoserine; by LATS1 and LATS2Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 128 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 131 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 138 | Phosphoserine; by MAPK8 and MAPK9Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 154 | Phosphothreonine; by MAPK8 and MAPK9Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 164 | Phosphoserine; by LATS1 and LATS22 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 274 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 289 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 367 | Phosphoserine; by MAPK8 and MAPK9Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 371 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 381 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 382 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 388 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 397 | Phosphoserine; by LATS1 and LATS24 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 400 | Phosphoserine; by CK11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 403 | Phosphoserine; by CK11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 407 | Phosphotyrosine; by ABL11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 412 | Phosphothreonine; by MAPK8 and MAPK91 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylated by LATS1 and LATS2; leading to cytoplasmic translocation and inactivation (PubMed:18158288, PubMed:20048001). Phosphorylated by ABL1; leading to YAP1 stabilization, enhanced interaction with TP73 and recruitment onto proapoptotic genes; in response to DNA damage (PubMed:18280240). Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (PubMed:20048001). Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (PubMed:21364637).4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.17"Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
Levy D., Adamovich Y., Reuven N., Shaul Y.
Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407, SUBCELLULAR LOCATION, INTERACTION WITH RUNX1 AND TP73. - Ref.21"JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis."
Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S.
Cell Death Dis. 1:E29-E29(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-119; SER-138; THR-154; SER-367 AND THR-412 BY MAPK8/JNK1 AND MAPK9/JNK2, FUNCTION. - Ref.22"A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-61; SER-109; SER-127 AND SER-164.
Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.22"A coordinated phosphorylation by Lats and CK1 regulates YAP stability through SCF(beta-TRCP)."
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.
Genes Dev. 24:72-85(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATION AT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BY SCF(BETA-TRCP), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-61; SER-109; SER-127 AND SER-164.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P46937. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P46937. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P46937. |
PeptideAtlas More...PeptideAtlasi | P46937. |
PRoteomics IDEntifications database More...PRIDEi | P46937. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P46937. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P46937. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Increased expression seen in some liver and prostate cancers. Isoforms lacking the transactivation domain found in striatal neurons of patients with Huntington disease (at protein level).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.1"Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain."
Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M., Huebner K., Lehman D.
J. Biol. Chem. 270:14733-14741(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. - Ref.11"Transcriptional repression induces a slowly progressive atypical neuronal death associated with changes of YAP isoforms and p73."
Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y., Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M., Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.
J. Cell Biol. 172:589-604(2006) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION OF ISOFORMS LACKING THE TRANSCRIPTIONAL ACTIVATION DOMAIN, TISSUE SPECIFICITY. - Ref.13"Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; SER-127 AND PRO-129, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000137693. |
CleanEx database of gene expression profiles More...CleanExi | HS_YAP1. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P46937. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P46937. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB009370. HPA038885. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Binds to the SH3 domain of the YES kinase. Binds to WBP1 and WBP2 (PubMed:9202023). Binds, in vitro, through the WW1 domain, to neural isoforms of ENAH that contain the PPSY motif (By similarity). The phosphorylated form interacts with YWHAB (PubMed:17974916). Interacts (via WW domains) with LATS1 (via PPxY motif 2) (PubMed:18158288). Interacts with LATS2 (PubMed:18158288). Isoform 2 and isoform 3 interact (via WW domain 1) with isoform 3 of ERBB4 (via PPxY motif 2) (PubMed:12807903). Interacts with TEAD1, TEAD2, TEAD3 and TEAD4 (PubMed:18579750, PubMed:20123905, PubMed:20123908). Interacts with TP73 (PubMed:18280240). Interacts with RUNX1 (PubMed:18280240). Interacts with HCK (PubMed:17535448). Interacts (via WW domains) with PTPN14 (via PPxY motif 2); this interaction leads to the cytoplasmic sequestration of YAP1 and inhibits its transcriptional coactivator activity (PubMed:22525271).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
10 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus."
Komuro A., Nagai M., Navin N.E., Sudol M.
J. Biol. Chem. 278:33334-33341(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ERBB4, MUTAGENESIS OF SER-127; TRP-199 AND PRO-202. - Ref.9"Characterization of the WW domain of human Yes-associated protein and its polyproline containing ligands."
Chen H.I., Einbond A., Kwak S.-J., Linn H., Koepf E., Peterson S., Kelly J.W., Sudol M.
J. Biol. Chem. 272:17070-17077(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH WBP1 AND WBP2. - Ref.12"Regulation of p73 by Hck through kinase-dependent and independent mechanisms."
Paliwal P., Radha V., Swarup G.
BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HCK. - Ref.13"Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control."
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., Lai Z.C., Guan K.L.
Genes Dev. 21:2747-2761(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; SER-127 AND PRO-129, TISSUE SPECIFICITY. - Ref.15"TEAD mediates YAP-dependent gene induction and growth control."
Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y., Chinnaiyan A.M., Lai Z.C., Guan K.L.
Genes Dev. 22:1962-1971(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TEAD1; TEAD2; TEAD3 AND TEAD4, MUTAGENESIS OF SER-94. - Ref.16"Tumor suppressor LATS1 is a negative regulator of oncogene YAP."
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.
J. Biol. Chem. 283:5496-5509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2, PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, MUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397. - Ref.17"Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
Levy D., Adamovich Y., Reuven N., Shaul Y.
Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407, SUBCELLULAR LOCATION, INTERACTION WITH RUNX1 AND TP73. - Ref.28"PTPN14 interacts with and negatively regulates the oncogenic function of YAP."
Liu X., Yang N., Figel S.A., Wilson K.E., Morrison C.D., Gelman I.H., Zhang J.
Oncogene 32:1266-1273(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPN14, SUBCELLULAR LOCATION. - Ref.35"Structural insights into the YAP and TEAD complex."
Li Z., Zhao B., Wang P., Chen F., Dong Z., Yang H., Guan K.L., Xu Y.
Genes Dev. 24:235-240(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 50-171 IN COMPLEX WITH TEAD1, COILED-COIL REGION, INTERACTION WITH TEAD1, MUTAGENESIS OF MET-86; ARG-89; LEU-91; SER-94; PHE-95 AND PHE-96.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- activating transcription factor binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- proline-rich region binding Source: Ensembl
- protein C-terminus binding Source: Ensembl
- protein heterodimerization activity Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115684. 137 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P46937. |
Database of interacting proteins More...DIPi | DIP-40839N. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P46937. |
Protein interaction database and analysis system More...IntActi | P46937. 100 interactors. |
Molecular INTeraction database More...MINTi | P46937. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000282441. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 52 – 57 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 65 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 75 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 86 – 88 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 93 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 169 – 171 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 177 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 183 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 187 – 191 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 192 – 195 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 196 – 200 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 202 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 233 – 235 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 238 – 241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 242 – 244 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 245 – 250 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 251 – 254 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 255 – 259 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1JMQ | NMR | - | A | 165-210 | [»] | |
| 1K5R | NMR | - | A | 165-204 | [»] | |
| 1K9Q | NMR | - | A | 165-204 | [»] | |
| 1K9R | NMR | - | A | 165-204 | [»] | |
| 2LAW | NMR | - | A | 230-263 | [»] | |
| 2LAX | NMR | - | A | 170-205 | [»] | |
| 2LAY | NMR | - | A | 170-205 | [»] | |
| 2LTV | NMR | - | A | 230-265 | [»] | |
| 2LTW | NMR | - | A | 170-205 | [»] | |
| 3KYS | X-ray | 2.80 | B/D | 50-171 | [»] | |
| 3MHR | X-ray | 1.15 | P | 124-133 | [»] | |
| 4RE1 | X-ray | 2.20 | C/D | 50-171 | [»] | |
| 4REX | X-ray | 1.60 | A | 165-209 | [»] | |
| 5OAQ | X-ray | 1.95 | L | 60-100 | [»] | |
Database of protein disorder More...DisProti | DP00702. | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P46937. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P46937. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P46937. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 171 – 204 | WW 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 34 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 230 – 263 | WW 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 34 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 291 – 504 | Transactivation domainAdd BLAST | 214 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 86 – 100 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 15 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 298 – 359 | Sequence analysisAdd BLAST | 62 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 3 – 49 | Pro-richAdd BLAST | 47 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The first coiled-coil region mediates most of the interaction with TEAD transcription factors.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.35"Structural insights into the YAP and TEAD complex."
Li Z., Zhao B., Wang P., Chen F., Dong Z., Yang H., Guan K.L., Xu Y.
Genes Dev. 24:235-240(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 50-171 IN COMPLEX WITH TEAD1, COILED-COIL REGION, INTERACTION WITH TEAD1, MUTAGENESIS OF MET-86; ARG-89; LEU-91; SER-94; PHE-95 AND PHE-96.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the YAP1 family.Curated
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Coiled coil, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0940. Eukaryota. COG5021. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00510000046760. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007854. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002748. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P46937. |
KEGG Orthology (KO) More...KOi | K16687. |
Identification of Orthologs from Complete Genome Data More...OMAi | DQTTTWQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G095A. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P46937. |
TreeFam database of animal gene trees More...TreeFami | TF326941. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00201. WW. 2 hits. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001202. WW_dom. IPR036020. WW_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00397. WW. 2 hits. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00456. WW. 2 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045. SSF51045. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01159. WW_DOMAIN_1. 2 hits. PS50020. WW_DOMAIN_2. 2 hits. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (9)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 9 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Note: Isoforms of the YAP1-1 form contain only one WW domain.
Isoform 1 (identifier: P46937-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-2gamma, YAP2L
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM TQDGEIYYIN
260 270 280 290 300
HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS
310 320 330 340 350
NQQQQMRLQQ LQMEKERLRL KQQELLRQAM RNINPSTANS PKCQELALRS
360 370 380 390 400
QLPTLEQDGG TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS
410 420 430 440 450
GLSMSSYSVP RTPDDFLNSV DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG
460 470 480 490 500
TNVDLGTLEG DGMNIEGEEL MPSLQEALSS DILNDMESVL AATKLDKESF
LTWL
Length:504
Mass (Da):54,462
Last modified:April 20, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i6145F7049ED338AE
Isoform 2 (identifier: P46937-2) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-2alpha, YAP2
The sequence of this isoform differs from the canonical sequence as follows:
328-343: Missing.
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM TQDGEIYYIN
260 270 280 290 300
HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS
310 320 330 340 350
NQQQQMRLQQ LQMEKERLRL KQQELLRQEL ALRSQLPTLE QDGGTQNPVS
360 370 380 390 400
SPGMSQELRT MTTNSSDPFL NSGTYHSRDE STDSGLSMSS YSVPRTPDDF
410 420 430 440 450
LNSVDEMDTG DTINQSTLPS QQNRFPDYLE AIPGTNVDLG TLEGDGMNIE
460 470 480
GEELMPSLQE ALSSDILNDM ESVLAATKLD KESFLTWL
Length:488
Mass (Da):52,748
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i675CC207C83A311E
Isoform 3 (identifier: P46937-3) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-1beta
The sequence of this isoform differs from the canonical sequence as follows:
230-267: Missing.
329-343: AMRNINPSTANSPKC → VRP
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASA MNQRISQSAP VKQPPPLAPQ
260 270 280 290 300
SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ VRPQELALRS
310 320 330 340 350
QLPTLEQDGG TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS
360 370 380 390 400
GLSMSSYSVP RTPDDFLNSV DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG
410 420 430 440 450
TNVDLGTLEG DGMNIEGEEL MPSLQEALSS DILNDMESVL AATKLDKESF
LTWL
Length:454
Mass (Da):48,755
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i87CB840D3393EFC0
Isoform 4 (identifier: P46937-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-178: Missing.
10 20 30 40 50
MAKTSSGQRY FLNHIDQTTT WQDPRKAMLS QMNVTAPTSP PVQQNMMNSA
60 70 80 90 100
SGPLPDGWEQ AMTQDGEIYY INHKNKTTSW LDPRLDPRFA MNQRISQSAP
110 120 130 140 150
VKQPPPLAPQ SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ
160 170 180 190 200
AMRNINPSTA NSPKCQELAL RSQLPTLEQD GGTQNPVSSP GMSQELRTMT
210 220 230 240 250
TNSSDPFLNS GTYHSRDEST DSGLSMSSYS VPRTPDDFLN SVDEMDTGDT
260 270 280 290 300
INQSTLPSQQ NRFPDYLEAI PGTNVDLGTL EGDGMNIEGE ELMPSLQEAL
310 320
SSDILNDMES VLAATKLDKE SFLTWL
Note: No experimental confirmation available.
Show »Length:326
Mass (Da):36,232
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i5C94DABAC6D74ABA
Isoform 5 (identifier: P46937-5) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-1alpha
The sequence of this isoform differs from the canonical sequence as follows:
230-267: Missing.
328-343: Missing.
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASA MNQRISQSAP VKQPPPLAPQ
260 270 280 290 300
SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ ELALRSQLPT
310 320 330 340 350
LEQDGGTQNP VSSPGMSQEL RTMTTNSSDP FLNSGTYHSR DESTDSGLSM
360 370 380 390 400
SSYSVPRTPD DFLNSVDEMD TGDTINQSTL PSQQNRFPDY LEAIPGTNVD
410 420 430 440 450
LGTLEGDGMN IEGEELMPSL QEALSSDILN DMESVLAATK LDKESFLTWL
Length:450
Mass (Da):48,275
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i295934FD185E7C59
Isoform 6 (identifier: P46937-6) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-1gamma
The sequence of this isoform differs from the canonical sequence as follows:
230-267: Missing.
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASA MNQRISQSAP VKQPPPLAPQ
260 270 280 290 300
SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ AMRNINPSTA
310 320 330 340 350
NSPKCQELAL RSQLPTLEQD GGTQNPVSSP GMSQELRTMT TNSSDPFLNS
360 370 380 390 400
GTYHSRDEST DSGLSMSSYS VPRTPDDFLN SVDEMDTGDT INQSTLPSQQ
410 420 430 440 450
NRFPDYLEAI PGTNVDLGTL EGDGMNIEGE ELMPSLQEAL SSDILNDMES
460
VLAATKLDKE SFLTWL
Length:466
Mass (Da):49,989
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iF1E76E6DEB3F93C0
Isoform 7 (identifier: P46937-7) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-1delta
The sequence of this isoform differs from the canonical sequence as follows:
230-267: Missing.
328-328: Q → QVRPQ
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASA MNQRISQSAP VKQPPPLAPQ
260 270 280 290 300
SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ VRPQAMRNIN
310 320 330 340 350
PSTANSPKCQ ELALRSQLPT LEQDGGTQNP VSSPGMSQEL RTMTTNSSDP
360 370 380 390 400
FLNSGTYHSR DESTDSGLSM SSYSVPRTPD DFLNSVDEMD TGDTINQSTL
410 420 430 440 450
PSQQNRFPDY LEAIPGTNVD LGTLEGDGMN IEGEELMPSL QEALSSDILN
460 470
DMESVLAATK LDKESFLTWL
Length:470
Mass (Da):50,469
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8935AAD2FA859F62
Isoform 8 (identifier: P46937-8) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: YAP1-2beta
The sequence of this isoform differs from the canonical sequence as follows:
329-343: AMRNINPSTANSPKC → VRP
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM TQDGEIYYIN
260 270 280 290 300
HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS
310 320 330 340 350
NQQQQMRLQQ LQMEKERLRL KQQELLRQVR PQELALRSQL PTLEQDGGTQ
360 370 380 390 400
NPVSSPGMSQ ELRTMTTNSS DPFLNSGTYH SRDESTDSGL SMSSYSVPRT
410 420 430 440 450
PDDFLNSVDE MDTGDTINQS TLPSQQNRFP DYLEAIPGTN VDLGTLEGDG
460 470 480 490
MNIEGEELMP SLQEALSSDI LNDMESVLAA TKLDKESFLT WL
Length:492
Mass (Da):53,228
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i289722956D96193A
Isoform 9 (identifier: P46937-9) [UniParc]FASTAAdd to basketAdded to basket
Also known as: YAP1-2delta
The sequence of this isoform differs from the canonical sequence as follows:
328-328: Q → QVRPQ
10 20 30 40 50
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA
60 70 80 90 100
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE
110 120 130 140 150
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG
160 170 180 190 200
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ
210 220 230 240 250
DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM TQDGEIYYIN
260 270 280 290 300
HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS
310 320 330 340 350
NQQQQMRLQQ LQMEKERLRL KQQELLRQVR PQAMRNINPS TANSPKCQEL
360 370 380 390 400
ALRSQLPTLE QDGGTQNPVS SPGMSQELRT MTTNSSDPFL NSGTYHSRDE
410 420 430 440 450
STDSGLSMSS YSVPRTPDDF LNSVDEMDTG DTINQSTLPS QQNRFPDYLE
460 470 480 490 500
AIPGTNVDLG TLEGDGMNIE GEELMPSLQE ALSSDILNDM ESVLAATKLD
KESFLTWL
Note: Highest expression in ovary and placenta, lowest in skeletal muscle and brain.
Show »Length:508
Mass (Da):54,942
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iCFCC0BD04A27060B
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071125 | 139 | P → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071126 | 227 | S → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071127 | 330 | M → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071128 | 462 | G → E1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045190 | 1 – 178 | Missing in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 178 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039053 | 230 – 267 | Missing in isoform 3, isoform 5, isoform 6 and isoform 7. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 38 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039054 | 328 – 343 | Missing in isoform 2 and isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 16 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_053483 | 328 | Q → QVRPQ in isoform 7 and isoform 9. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_039055 | 329 – 343 | AMRNI…NSPKC → VRP in isoform 3 and isoform 8. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 15 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X80507 Genomic DNA. Translation: CAA56672.1. AY316529 mRNA. Translation: AAP92710.1. AB567720 mRNA. Translation: BAJ41471.1. AB567721 mRNA. Translation: BAJ41472.1. AK300414 mRNA. Translation: BAG62143.1. AK316116 mRNA. Translation: BAH14487.1. AP000942 Genomic DNA. No translation available. AP001527 Genomic DNA. No translation available. AP002777 Genomic DNA. No translation available. CH471065 Genomic DNA. Translation: EAW67011.1. CH471065 Genomic DNA. Translation: EAW67015.1. BC038235 mRNA. Translation: AAH38235.1. HE864159 mRNA. Translation: CCI79618.1. HE864160 mRNA. Translation: CCI79619.1. HE864161 mRNA. Translation: CCI79620.1. HE864162 mRNA. Translation: CCI79621.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44716.1. [P46937-1] CCDS53699.1. [P46937-2] CCDS53700.1. [P46937-4] CCDS60944.1. [P46937-8] CCDS60945.1. [P46937-3] CCDS73373.1. [P46937-9] CCDS73374.1. [P46937-7] CCDS8314.2. [P46937-5] |
Protein sequence database of the Protein Information Resource More...PIRi | A56954. |
NCBI Reference Sequences More...RefSeqi | NP_001123617.1. NM_001130145.2. [P46937-1] NP_001181973.1. NM_001195044.1. [P46937-2] NP_001181974.1. NM_001195045.1. [P46937-4] NP_001269026.1. NM_001282097.1. [P46937-6] NP_001269027.1. NM_001282098.1. [P46937-3] NP_001269028.1. NM_001282099.1. [P46937-7] NP_001269029.1. NM_001282100.1. [P46937-8] NP_001269030.1. NM_001282101.1. [P46937-9] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.503692. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000282441; ENSP00000282441; ENSG00000137693. [P46937-1] ENST00000345877; ENSP00000331023; ENSG00000137693. [P46937-7] ENST00000524575; ENSP00000435602; ENSG00000137693. [P46937-4] ENST00000526343; ENSP00000434134; ENSG00000137693. [P46937-5] ENST00000531439; ENSP00000431574; ENSG00000137693. [P46937-2] ENST00000537274; ENSP00000445635; ENSG00000137693. [P46937-8] ENST00000615667; ENSP00000478927; ENSG00000137693. [P46937-9] ENST00000629586; ENSP00000487519; ENSG00000137693. [P46937-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10413. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10413. |
UCSC genome browser More...UCSCi | uc001pgt.3. human. [P46937-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
| Protein Spotlight Shaping life - Issue 175 of January 2016 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X80507 Genomic DNA. Translation: CAA56672.1. AY316529 mRNA. Translation: AAP92710.1. AB567720 mRNA. Translation: BAJ41471.1. AB567721 mRNA. Translation: BAJ41472.1. AK300414 mRNA. Translation: BAG62143.1. AK316116 mRNA. Translation: BAH14487.1. AP000942 Genomic DNA. No translation available. AP001527 Genomic DNA. No translation available. AP002777 Genomic DNA. No translation available. CH471065 Genomic DNA. Translation: EAW67011.1. CH471065 Genomic DNA. Translation: EAW67015.1. BC038235 mRNA. Translation: AAH38235.1. HE864159 mRNA. Translation: CCI79618.1. HE864160 mRNA. Translation: CCI79619.1. HE864161 mRNA. Translation: CCI79620.1. HE864162 mRNA. Translation: CCI79621.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS44716.1. [P46937-1] CCDS53699.1. [P46937-2] CCDS53700.1. [P46937-4] CCDS60944.1. [P46937-8] CCDS60945.1. [P46937-3] CCDS73373.1. [P46937-9] CCDS73374.1. [P46937-7] CCDS8314.2. [P46937-5] |
Protein sequence database of the Protein Information Resource More...PIRi | A56954. |
NCBI Reference Sequences More...RefSeqi | NP_001123617.1. NM_001130145.2. [P46937-1] NP_001181973.1. NM_001195044.1. [P46937-2] NP_001181974.1. NM_001195045.1. [P46937-4] NP_001269026.1. NM_001282097.1. [P46937-6] NP_001269027.1. NM_001282098.1. [P46937-3] NP_001269028.1. NM_001282099.1. [P46937-7] NP_001269029.1. NM_001282100.1. [P46937-8] NP_001269030.1. NM_001282101.1. [P46937-9] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.503692. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1JMQ | NMR | - | A | 165-210 | [»] | |
| 1K5R | NMR | - | A | 165-204 | [»] | |
| 1K9Q | NMR | - | A | 165-204 | [»] | |
| 1K9R | NMR | - | A | 165-204 | [»] | |
| 2LAW | NMR | - | A | 230-263 | [»] | |
| 2LAX | NMR | - | A | 170-205 | [»] | |
| 2LAY | NMR | - | A | 170-205 | [»] | |
| 2LTV | NMR | - | A | 230-265 | [»] | |
| 2LTW | NMR | - | A | 170-205 | [»] | |
| 3KYS | X-ray | 2.80 | B/D | 50-171 | [»] | |
| 3MHR | X-ray | 1.15 | P | 124-133 | [»] | |
| 4RE1 | X-ray | 2.20 | C/D | 50-171 | [»] | |
| 4REX | X-ray | 1.60 | A | 165-209 | [»] | |
| 5OAQ | X-ray | 1.95 | L | 60-100 | [»] | |
Database of protein disorder More...DisProti | DP00702. | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P46937. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P46937. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115684. 137 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P46937. |
Database of interacting proteins More...DIPi | DIP-40839N. |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P46937. |
Protein interaction database and analysis system More...IntActi | P46937. 100 interactors. |
Molecular INTeraction database More...MINTi | P46937. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000282441. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P46937. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P46937. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | YAP1. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 294862479. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P46937. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P46937. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P46937. |
PeptideAtlas More...PeptideAtlasi | P46937. |
PRoteomics IDEntifications database More...PRIDEi | P46937. |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000282441; ENSP00000282441; ENSG00000137693. [P46937-1] ENST00000345877; ENSP00000331023; ENSG00000137693. [P46937-7] ENST00000524575; ENSP00000435602; ENSG00000137693. [P46937-4] ENST00000526343; ENSP00000434134; ENSG00000137693. [P46937-5] ENST00000531439; ENSP00000431574; ENSG00000137693. [P46937-2] ENST00000537274; ENSP00000445635; ENSG00000137693. [P46937-8] ENST00000615667; ENSP00000478927; ENSG00000137693. [P46937-9] ENST00000629586; ENSP00000487519; ENSG00000137693. [P46937-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10413. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10413. |
UCSC genome browser More...UCSCi | uc001pgt.3. human. [P46937-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10413. |
DisGeNET More...DisGeNETi | 10413. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000137693.13. |
GeneCards: human genes, protein and diseases More...GeneCardsi | YAP1. |
Human Gene Nomenclature Database More...HGNCi | HGNC:16262. YAP1. |
Human Protein Atlas More...HPAi | CAB009370. HPA038885. |
MalaCards human disease database More...MalaCardsi | YAP1. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 120433. phenotype. 606608. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P46937. |
Open Targets More...OpenTargetsi | ENSG00000137693. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 1473. Uveal coloboma - cleft lip and palate - intellectual disability. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA38103. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0940. Eukaryota. COG5021. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00510000046760. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007854. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002748. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P46937. |
KEGG Orthology (KO) More...KOi | K16687. |
Identification of Orthologs from Complete Genome Data More...OMAi | DQTTTWQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G095A. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P46937. |
TreeFam database of animal gene trees More...TreeFami | TF326941. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1251985. Nuclear signaling by ERBB4. R-HSA-1989781. PPARA activates gene expression. R-HSA-2028269. Signaling by Hippo. R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression. R-HSA-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs. R-HSA-8940973. RUNX2 regulates osteoblast differentiation. R-HSA-8951671. RUNX3 regulates YAP1-mediated transcription. |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P46937. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P46937. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | YAP1. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P46937. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | YAP1. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10413. |
Protein Ontology More...PROi | PR:P46937. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000137693. |
CleanEx database of gene expression profiles More...CleanExi | HS_YAP1. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P46937. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P46937. HS. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00201. WW. 2 hits. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001202. WW_dom. IPR036020. WW_dom_sf. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00397. WW. 2 hits. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00456. WW. 2 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51045. SSF51045. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01159. WW_DOMAIN_1. 2 hits. PS50020. WW_DOMAIN_2. 2 hits. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | YAP1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P46937Primary (citable) accession number: P46937 Secondary accession number(s): B4DTY1 , B7ZA01, E3WEB5, E3WEB6, E9PRV2, F5H202, K0KQ18, K0KYZ8, K0L195, K0L1G3, Q7Z574, Q8IUY9 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
| Last sequence update: | April 20, 2010 | |
| Last modified: | March 28, 2018 | |
| This is version 184 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |