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P46937 (YAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Yorkie homolog
Alternative name(s):
65 kDa Yes-associated protein
Short name=YAP65
Gene names
Name:YAP1
Synonyms:YAP65
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. 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. 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. Isoform 2 and isoform 3 can activate the C-terminal fragment (CTF) of ERBB4 (isoform 3). Ref.2 Ref.11 Ref.13 Ref.14 Ref.15 Ref.19

Subunit structure

Binds to the SH3 domain of the YES kinase. Binds to WBP1 and WBP2. 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. Interacts (via WW domains) with LATS1 (via PPxY motif 2). Interacts with LATS2. Isoform 2 and isoform 3 interact (via WW domain 1) with isoform 3 of ERBB4 (via PPxY motif 2). Interacts with TEAD1, TEAD2, TEAD3 and TEAD4. Interacts with TP73. Interacts with RUNX1. Interacts with HCK. 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. Ref.2 Ref.7 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.21 Ref.22 Ref.26

Subcellular location

Cytoplasm. Nucleus. 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. PTPN14 induces translocation from the nucleus to the cytoplasm. Ref.11 Ref.14 Ref.15 Ref.20 Ref.26

Tissue specificity

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). Ref.1 Ref.9 Ref.11

Post-translational modification

Phosphorylated by LATS1 and LATS2; leading to cytoplasmic translocation and inactivation. Phosphorylated by ABL1; leading to YAP1 stabilization, enhanced interaction with TP73 and recruitment onto proapoptotic genes; in response to DNA damage. 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. Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regukation of apoptosis by YAP1. Ref.11 Ref.14 Ref.15 Ref.19 Ref.20

Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase. Ref.20

Sequence similarities

Belongs to the YORKIE family.

Contains 2 WW domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainRepeat
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from direct assay Ref.11. Source: UniProtKB

cellular response to gamma radiation

Inferred from direct assay Ref.15. Source: UniProtKB

contact inhibition

Inferred from direct assay Ref.11. Source: UniProtKB

embryonic heart tube morphogenesis

Inferred from electronic annotation. Source: Ensembl

hippo signaling cascade

Traceable author statement Ref.14. Source: UniProtKB

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

lateral mesoderm development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

notochord development

Inferred from electronic annotation. Source: Ensembl

paraxial mesoderm development

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of organ growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of stem cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to DNA damage stimulus

Inferred from direct assay Ref.15. Source: UniProtKB

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II transcription factor binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.14. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms lacking the transactivation domain exist.
Isoform 1 (identifier: P46937-1)

Also known as: 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.
Isoform 2 (identifier: P46937-2)

Also known as: YAP2;

The sequence of this isoform differs from the canonical sequence as follows:
     328-343: Missing.
Isoform 3 (identifier: P46937-3)

Also known as: YAP1;

The sequence of this isoform differs from the canonical sequence as follows:
     230-267: Missing.
     329-343: AMRNINPSTANSPKC → VRP
Isoform 4 (identifier: P46937-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 504504Yorkie homolog
PRO_0000076071

Regions

Domain171 – 20434WW 1
Domain230 – 26334WW 2
Region291 – 504214Transactivation domain
Compositional bias3 – 4947Pro-rich

Amino acid modifications

Modified residue611Phosphoserine; by LATS1 and LATS2 Ref.11 Ref.14 Ref.16 Ref.23 Ref.25
Modified residue631Phosphothreonine Ref.23
Modified residue1091Phosphoserine; by LATS1 and LATS2 Ref.11 Ref.14 Ref.23
Modified residue1101Phosphothreonine By similarity
Modified residue1191Phosphothreonine; by MAPK8 and MAPK9 Ref.19 Ref.23
Modified residue1271Phosphoserine; by LATS1 and LATS2 Ref.11 Ref.14 Ref.16 Ref.20
Modified residue1311Phosphoserine Ref.16
Modified residue1381Phosphoserine; by MAPK8 and MAPK9 Ref.16 Ref.19 Ref.23
Modified residue1541Phosphothreonine; by MAPK8 and MAPK9 Ref.16 Ref.19
Modified residue1641Phosphoserine; by LATS1 and LATS2 Ref.11 Ref.14
Modified residue2741Phosphoserine Ref.16 Ref.23
Modified residue2891Phosphoserine Ref.16 Ref.23 Ref.25
Modified residue3671Phosphoserine; by MAPK8 and MAPK9 Ref.16 Ref.19 Ref.23 Ref.25
Modified residue3711Phosphoserine Ref.12
Modified residue3971Phosphoserine; by LATS1 and LATS2 Ref.11 Ref.14 Ref.20
Modified residue4001Phosphoserine; by CK1 Ref.20
Modified residue4031Phosphoserine; by CK1 Ref.20
Modified residue4071Phosphotyrosine; by ABL1 Ref.15
Modified residue4121Phosphothreonine; by MAPK8 and MAPK9 Ref.19

Natural variations

Alternative sequence1 – 178178Missing in isoform 4.
VSP_045190
Alternative sequence230 – 26738Missing in isoform 3.
VSP_039053
Alternative sequence328 – 34316Missing in isoform 2.
VSP_039054
Alternative sequence329 – 34315AMRNI…NSPKC → VRP in isoform 3.
VSP_039055

Experimental info

Mutagenesis801V → A: No change in interaction with TEAD4. Reduced interaction with TEAD4 and transforming ability; when associated with A-84 and A-85. Ref.22
Mutagenesis841V → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-85. Ref.22
Mutagenesis851P → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-84. Ref.22
Mutagenesis861M → A: Complete loss of interaction with TEAD1. Ref.21
Mutagenesis891R → A: Complete loss of interaction with TEAD1. Ref.21
Mutagenesis911L → A: Complete loss of interaction with TEAD1. Ref.21
Mutagenesis941S → 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. Ref.13 Ref.21
Mutagenesis951F → A: Complete loss of interaction with TEAD1. Ref.21
Mutagenesis961F → A: Loss of interaction with TEAD1. Ref.21
Mutagenesis1221H → A, R, N or K: Loss of phosphorylation by LATS1. Ref.11 Ref.14
Mutagenesis1221H → L or Y: Significantly decreased phosphorylation at S-127 and decreased interaction with YWHAB. Ref.11 Ref.14
Mutagenesis1241R → A: Loss of phosphorylation by LATS1. Ref.14
Mutagenesis1271S → 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. Ref.2 Ref.11 Ref.14
Mutagenesis1291P → D: No effect on phosphorylation but loss of interaction with YWHAB. Ref.11
Mutagenesis1991W → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-202. Ref.2
Mutagenesis2021P → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-199. Ref.2
Mutagenesis3971S → A: Loss of phosphorylation by LATS1. Ref.14
Mutagenesis4071Y → E: Enhanced interaction with TP73. Ref.15
Mutagenesis4071Y → F: No phosphorylation by ABL1 and partial loss of binding to TP73. Ref.15

Secondary structure

1 ................................ 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (YAP2L) [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 6145F7049ED338AE

FASTA50454,462
        10         20         30         40         50         60 
MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA GHQIVHVRGD 

        70         80         90        100        110        120 
SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE PKSHSRQAST DAGTAGALTP 

       130        140        150        160        170        180 
QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG PAATPTAQHL RQSSFEIPDD VPLPAGWEMA 

       190        200        210        220        230        240 
KTSSGQRYFL NHIDQTTTWQ DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM 

       250        260        270        280        290        300 
TQDGEIYYIN HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS 

       310        320        330        340        350        360 
NQQQQMRLQQ LQMEKERLRL KQQELLRQAM RNINPSTANS PKCQELALRS QLPTLEQDGG 

       370        380        390        400        410        420 
TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS GLSMSSYSVP RTPDDFLNSV 

       430        440        450        460        470        480 
DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG TNVDLGTLEG DGMNIEGEEL MPSLQEALSS 

       490        500 
DILNDMESVL AATKLDKESF LTWL

« Hide

Isoform 2 (YAP2) [UniParc].

Checksum: 675CC207C83A311E
Show »

FASTA48852,748
Isoform 3 (YAP1) [UniParc].

Checksum: 87CB840D3393EFC0
Show »

FASTA45448,755
Isoform 4 [UniParc].

Checksum: 5C94DABAC6D74ABA
Show »

FASTA32636,232

References

« Hide 'large scale' references
[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.
Tissue: Lung.
[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.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Placenta.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pancreas.
[7]"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.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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.
[10]"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.
[11]"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.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[13]"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.
[14]"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.
[15]"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.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-127; SER-131; SER-138; THR-154; SER-274; SER-289 AND SER-367, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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.
[20]"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.
[21]"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: INTERACTION WITH TEAD1, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 50-171 IN COMPLEX WITH TEAD1, MUTAGENESIS OF MET-86; ARG-89; LEU-91; SER-94; PHE-95 AND PHE-96.
[22]"Structural basis of YAP recognition by TEAD4 in the hippo pathway."
Chen L., Chan S.W., Zhang X., Walsh M., Lim C.J., Hong W., Song H.
Genes Dev. 24:290-300(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TEAD4, MUTAGENESIS OF VAL-80; VAL-84 AND PRO-85.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; THR-63; SER-109; THR-119; SER-138; SER-274; SER-289 AND SER-367, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-289 AND SER-367, MASS SPECTROMETRY.
[26]"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.
[27]"Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope."
Pires J.R., Taha-Nejad F., Toepert F., Ast T., Hoffmueller U., Schneider-Mergener J., Kuehne R., Macias M.J., Oschkinat H.
J. Mol. Biol. 314:1147-1156(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 165-210 OF WILD-TYPE AND MUTANT LYS-190 IN COMPLEX WITH PRO-RICH PEPTIDES.
[28]"Using flexible loop mimetics to extend phi-value analysis to secondary structure interactions."
Ferguson N., Pires J.R., Toepert F., Johnson C.M., Pan Y.P., Volkmer-Engert R., Schneider-Mergener J., Daggett V., Oschkinat H., Fersht A.
Proc. Natl. Acad. Sci. U.S.A. 98:13008-13013(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 165-204.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X80507 Genomic DNA. Translation: CAA56672.1.
AY316529 mRNA. Translation: AAP92710.1.
AK300414 mRNA. Translation: BAG62143.1.
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.
IPIIPI00009326.
IPI00216919.
IPI00956212.
IPI00978761.
PIRA56954.
RefSeqNP_001123617.1. NM_001130145.2.
NP_001181973.1. NM_001195044.1.
NP_001181974.1. NM_001195045.1.
NP_001269027.1. NM_001282098.1.
NP_001269028.1. NM_001282099.1.
NP_001269029.1. NM_001282100.1.
NP_001269030.1. NM_001282101.1.
UniGeneHs.503692.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMQNMR-A165-210[»]
1K5RNMR-A165-204[»]
1K9QNMR-A165-204[»]
1K9RNMR-A165-204[»]
2LAWNMR-A230-263[»]
2LAXNMR-A170-205[»]
2LAYNMR-A170-205[»]
2LTVNMR-A230-265[»]
2LTWNMR-A170-205[»]
3KYSX-ray2.80B/D50-171[»]
3MHRX-ray1.15P124-133[»]
DisProtDP00702.
ProteinModelPortalP46937.
SMRP46937. Positions 50-100, 165-265.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-40839N.
IntActP46937. 28 interactions.
MINTMINT-110802.
STRING9606.ENSP00000282441.

PTM databases

PhosphoSiteP46937.

Polymorphism databases

DMDM294862479.

Proteomic databases

PaxDbP46937.
PRIDEP46937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282441; ENSP00000282441; ENSG00000137693.
ENST00000345877; ENSP00000331023; ENSG00000137693.
ENST00000524575; ENSP00000435602; ENSG00000137693.
ENST00000531439; ENSP00000431574; ENSG00000137693.
GeneID10413.
KEGGhsa:10413.
UCSCuc001pgt.3. human.

Organism-specific databases

CTD10413.
GeneCardsGC11P102015.
HGNCHGNC:16262. YAP1.
HPACAB009370.
MIM606608. gene.
neXtProtNX_P46937.
PharmGKBPA38103.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000007854.
HOVERGENHBG002748.
KOK16687.
OMALRQSSYE.
PhylomeDBP46937.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_71. Gene Expression.
SignaLinkP46937.

Gene expression databases

ArrayExpressP46937.
BgeeP46937.
CleanExHS_YAP1.
GenevestigatorP46937.

Family and domain databases

InterProIPR001202. WW_dom.
[Graphical view]
PfamPF00397. WW. 2 hits.
[Graphical view]
SMARTSM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF51045. SSF51045. 2 hits.
PROSITEPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYAP1. human.
EvolutionaryTraceP46937.
GeneWikiYAP1.
GenomeRNAi10413.
NextBio39472.
PROP46937.
SOURCESearch...

Entry information

Entry nameYAP1_HUMAN
AccessionPrimary (citable) accession number: P46937
Secondary accession number(s): B4DTY1, Q7Z574, Q8IUY9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 20, 2010
Last modified: November 13, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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