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Reviewed, UniProtKB/Swiss-Prot P46937 (YAP1_HUMAN)

Last modified November 25, 2008. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    65 kDa Yes-associated protein
Alternative name(s):
    YAP65
Gene names
Name: YAP1
Synonyms: YAP65
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

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.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence similarities

Contains 1 WW domain.

Ontologies

Keywords

   PTMPhosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Molecular functionprotein binding Ref.1

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 45445465 kDa Yes-associated protein
PRO_0000076071

Regions

Domain171 – 20434WW
Compositional bias3 – 4947Pro-rich
Compositional bias221 – 31292Gln-rich

Amino acid modifications

Modified residue611Phosphoserine
Modified residue1091Phosphoserine
Modified residue1101Phosphothreonine
Modified residue1271Phosphoserine
Modified residue1281Phosphoserine
Modified residue1311Phosphoserine
Modified residue1381Phosphoserine
Modified residue1431Phosphothreonine
Modified residue1491Phosphoserine
Modified residue1541Phosphothreonine
Modified residue2361Phosphoserine
Modified residue2381Phosphoserine
Modified residue2511Phosphoserine
Modified residue3171Phosphoserine
Modified residue3211Phosphoserine

Secondary structure

........ 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46937-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 87CB840D3393EFC0

FASTA45448,755
        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 QQNMMNSASA MNQRISQSAP 

       250        260        270        280        290        300 
VKQPPPLAPQ SPQGGVMGGS NSNQQQQMRL QQLQMEKERL RLKQQELLRQ VRPQELALRS 

       310        320        330        340        350        360 
QLPTLEQDGG TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS GLSMSSYSVP 

       370        380        390        400        410        420 
RTPDDFLNSV DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG TNVDLGTLEG DGMNIEGEEL 

       430        440        450 
MPSLQEALSS DILNDMESVL AATKLDKESF LTWL 

« Hide

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: 7782338] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[2]"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: 9202023] [Abstract]
Cited for: INTERACTION WITH WBP1 AND WBP2.
[3]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND THR-110, MASS SPECTROMETRY.
Tissue: Epithelium.
[4]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; THR-143 AND THR-154, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, MASS SPECTROMETRY.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY.
[8]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-127; SER-128; SER-131; SER-138; THR-143; SER-149; THR-154; SER-236; SER-251 AND SER-317, MASS SPECTROMETRY.
[9]"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: 11743730] [Abstract]
Cited for: STRUCTURE BY NMR OF 165-210 OF WILD-TYPE AND MUTANT LYS-190 IN COMPLEX WITH PRO-RICH PEPTIDES.
+Additional computationally mapped references.

Cross-references

Sequence databases

X80507 Genomic DNA. Translation: CAA56672.1.
PIRA56954.
RefSeqNP_006097.1.
UniGeneHs.503692

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JMQNMR-A165-210[»]
1K5RNMR-A165-204[»]
1K9QNMR-A165-204[»]
1K9RNMR-A165-204[»]
SMRP46937. Positions 165-210.
ModBaseSearch...

Protein-protein interaction databases

IntActP46937.

PTM databases

PhosphoSiteP46937.

Genome annotation databases

EnsemblENSG00000137693. Homo sapiens. [Contig view]
GeneID10413.
KEGGhsa:10413.

Organism-specific databases

H-InvDBHIX0010062.
HGNCHGNC:16262. YAP1.
HPACAB009370.
MIM606608. gene.
PharmGKBPA24564.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP46937.

Gene expression databases

ArrayExpressP46937.
CleanExHS_YAP1.
GermOnlineENSG00000137693. Homo sapiens.

Family and domain databases

InterProIPR002349. WW.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
PfamPF00397. WW. 1 hit.
[Graphical view]
PRINTSPR00403. WWDOMAIN.
SMARTSM00456. WW. 1 hit.
[Graphical view]
PROSITEPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP46937.
NextBio39472.
SOURCESearch...

Entry information

Entry nameYAP1_HUMAN
AccessionPrimary (citable) accession number: P46937
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents