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P46937

- YAP1_HUMAN

UniProt

P46937 - YAP1_HUMAN

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Protein

Yorkie homolog

Gene
YAP1, YAP65
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. 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).6 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. protein binding Source: IntAct
  3. RNA polymerase II transcription factor binding transcription factor activity Source: Ensembl
  4. transcription coactivator activity Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB
  6. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. cellular response to gamma radiation Source: UniProtKB
  4. contact inhibition Source: UniProtKB
  5. embryonic heart tube morphogenesis Source: Ensembl
  6. gene expression Source: Reactome
  7. hippo signaling Source: UniProtKB
  8. keratinocyte differentiation Source: Ensembl
  9. lateral mesoderm development Source: Ensembl
  10. negative regulation of epithelial cell differentiation Source: Ensembl
  11. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  12. notochord development Source: Ensembl
  13. paraxial mesoderm development Source: Ensembl
  14. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  15. positive regulation of cell proliferation Source: Ensembl
  16. positive regulation of organ growth Source: Ensembl
  17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  18. regulation of keratinocyte proliferation Source: Ensembl
  19. regulation of stem cell proliferation Source: Ensembl
  20. somatic stem cell maintenance Source: Ensembl
  21. transcription initiation from RNA polymerase II promoter Source: Reactome
  22. vasculogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_116022. Nuclear signaling by ERBB4.
REACT_116145. PPARA activates gene expression.
REACT_118607. Signaling by Hippo.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
SignaLinkiP46937.

Names & Taxonomyi

Protein namesi
Recommended name:
Yorkie homolog
Alternative name(s):
65 kDa Yes-associated protein
Short name:
YAP65
Gene namesi
Name:YAP1
Synonyms:YAP65
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16262. YAP1.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801V → A: No change in interaction with TEAD4. Reduced interaction with TEAD4 and transforming ability; when associated with A-84 and A-85. 1 Publication
Mutagenesisi84 – 841V → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-85. 1 Publication
Mutagenesisi85 – 851P → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-84. 1 Publication
Mutagenesisi86 – 861M → A: Complete loss of interaction with TEAD1. 1 Publication
Mutagenesisi89 – 891R → A: Complete loss of interaction with TEAD1. 1 Publication
Mutagenesisi91 – 911L → A: Complete loss of interaction with TEAD1. 1 Publication
Mutagenesisi94 – 941S → 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
Mutagenesisi95 – 951F → A: Complete loss of interaction with TEAD1. 1 Publication
Mutagenesisi96 – 961F → A: Loss of interaction with TEAD1. 1 Publication
Mutagenesisi122 – 1221H → A, R, N or K: Loss of phosphorylation by LATS1. 2 Publications
Mutagenesisi122 – 1221H → L or Y: Significantly decreased phosphorylation at S-127 and decreased interaction with YWHAB. 2 Publications
Mutagenesisi124 – 1241R → A: Loss of phosphorylation by LATS1. 1 Publication
Mutagenesisi127 – 1271S → 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. 3 Publications
Mutagenesisi129 – 1291P → D: No effect on phosphorylation but loss of interaction with YWHAB. 1 Publication
Mutagenesisi199 – 1991W → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-202. 1 Publication
Mutagenesisi202 – 2021P → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-199. 1 Publication
Mutagenesisi397 – 3971S → A: Loss of phosphorylation by LATS1. 1 Publication
Mutagenesisi407 – 4071Y → E: Enhanced interaction with TP73. 1 Publication
Mutagenesisi407 – 4071Y → F: No phosphorylation by ABL1 and partial loss of binding to TP73. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti1473. Uveal coloboma - cleft lip and palate - intellectual disability.
PharmGKBiPA38103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Yorkie homologPRO_0000076071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine; by LATS1 and LATS25 Publications
Modified residuei63 – 631Phosphothreonine1 Publication
Modified residuei109 – 1091Phosphoserine; by LATS1 and LATS23 Publications
Modified residuei110 – 1101Phosphothreonine By similarity
Modified residuei119 – 1191Phosphothreonine; by MAPK8 and MAPK92 Publications
Modified residuei127 – 1271Phosphoserine; by LATS1 and LATS24 Publications
Modified residuei131 – 1311Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine; by MAPK8 and MAPK93 Publications
Modified residuei154 – 1541Phosphothreonine; by MAPK8 and MAPK92 Publications
Modified residuei164 – 1641Phosphoserine; by LATS1 and LATS22 Publications
Modified residuei274 – 2741Phosphoserine2 Publications
Modified residuei289 – 2891Phosphoserine3 Publications
Modified residuei367 – 3671Phosphoserine; by MAPK8 and MAPK94 Publications
Modified residuei371 – 3711Phosphoserine1 Publication
Modified residuei397 – 3971Phosphoserine; by LATS1 and LATS23 Publications
Modified residuei400 – 4001Phosphoserine; by CK11 Publication
Modified residuei403 – 4031Phosphoserine; by CK11 Publication
Modified residuei407 – 4071Phosphotyrosine; by ABL11 Publication
Modified residuei412 – 4121Phosphothreonine; by MAPK8 and MAPK91 Publication

Post-translational modificationi

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 YAP1.5 Publications
Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP46937.
PaxDbiP46937.
PRIDEiP46937.

PTM databases

PhosphoSiteiP46937.

Expressioni

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

Gene expression databases

ArrayExpressiP46937.
BgeeiP46937.
CleanExiHS_YAP1.
GenevestigatoriP46937.

Organism-specific databases

HPAiCAB009370.

Interactioni

Subunit structurei

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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P3522212EBI-1044059,EBI-491549
DDX17Q928417EBI-1044059,EBI-746012
LATS1O958355EBI-1044059,EBI-444209
MAP2K1Q027503EBI-1044059,EBI-492564
SMAD1Q157973EBI-1044059,EBI-1567153
TBX5Q995934EBI-1044059,EBI-297043
TEAD1P283474EBI-1044059,EBI-529156
TP53BP2Q13625-29EBI-1044059,EBI-287091
TP73O15350-17EBI-1044059,EBI-389619
Wbp1P9776413EBI-1044059,EBI-6304160From a different organism.
YWHABP319465EBI-1044059,EBI-359815
YWHAZP631043EBI-1044059,EBI-347088

Protein-protein interaction databases

BioGridi115684. 99 interactions.
DIPiDIP-40839N.
IntActiP46937. 68 interactions.
MINTiMINT-110802.
STRINGi9606.ENSP00000282441.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 576
Helixi61 – 7313
Helixi75 – 773
Helixi86 – 883
Helixi93 – 953
Beta strandi169 – 1713
Beta strandi175 – 1817
Beta strandi183 – 1853
Beta strandi188 – 1914
Turni192 – 1954
Beta strandi196 – 2005
Turni202 – 2043
Beta strandi205 – 2073
Beta strandi233 – 2353
Beta strandi238 – 2414
Turni242 – 2443
Beta strandi245 – 2506
Turni251 – 2544
Beta strandi255 – 2595

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00702.
ProteinModelPortaliP46937.
SMRiP46937. Positions 50-100, 165-265.

Miscellaneous databases

EvolutionaryTraceiP46937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 20434WW 1Add
BLAST
Domaini230 – 26334WW 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 504214Transactivation domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili86 – 100151 PublicationAdd
BLAST
Coiled coili298 – 35962 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 4947Pro-richAdd
BLAST

Domaini

The first coiled-coil region mediates most of the interaction with TEAD transcription factors.1 Publication

Sequence similaritiesi

Belongs to the YORKIE family.
Contains 2 WW domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5021.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
KOiK16687.
OMAiLRQSSYE.
PhylomeDBiP46937.
TreeFamiTF326941.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 2 hits.
[Graphical view]
SMARTiSM00456. WW. 2 hits.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Note: Isoforms of the YAP1-1 form contain only on WW domain.

Isoform 1 (identifier: P46937-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDPGQQPPPQ PAPQGQGQPP SQPPQGQGPP SGPGQPAPAA TQAAPQAPPA    50
GHQIVHVRGD SETDLEALFN AVMNPKTANV PQTVPMRLRK LPDSFFKPPE 100
PKSHSRQAST DAGTAGALTP QHVRAHSSPA SLQLGAVSPG TLTPTGVVSG 150
PAATPTAQHL RQSSFEIPDD VPLPAGWEMA KTSSGQRYFL NHIDQTTTWQ 200
DPRKAMLSQM NVTAPTSPPV QQNMMNSASG PLPDGWEQAM TQDGEIYYIN 250
HKNKTTSWLD PRLDPRFAMN QRISQSAPVK QPPPLAPQSP QGGVMGGSNS 300
NQQQQMRLQQ LQMEKERLRL KQQELLRQAM RNINPSTANS PKCQELALRS 350
QLPTLEQDGG TQNPVSSPGM SQELRTMTTN SSDPFLNSGT YHSRDESTDS 400
GLSMSSYSVP RTPDDFLNSV DEMDTGDTIN QSTLPSQQNR FPDYLEAIPG 450
TNVDLGTLEG DGMNIEGEEL MPSLQEALSS DILNDMESVL AATKLDKESF 500
LTWL 504
Length:504
Mass (Da):54,462
Last modified:April 20, 2010 - v2
Checksum:i6145F7049ED338AE
GO
Isoform 2 (identifier: P46937-2) [UniParc]FASTAAdd to Basket

Also known as: YAP1-2alpha, YAP2

The sequence of this isoform differs from the canonical sequence as follows:
     328-343: Missing.

Show »
Length:488
Mass (Da):52,748
Checksum:i675CC207C83A311E
GO
Isoform 3 (identifier: P46937-3) [UniParc]FASTAAdd to Basket

Also known as: YAP1-1beta

The sequence of this isoform differs from the canonical sequence as follows:
     230-267: Missing.
     329-343: AMRNINPSTANSPKC → VRP

Show »
Length:454
Mass (Da):48,755
Checksum:i87CB840D3393EFC0
GO
Isoform 4 (identifier: P46937-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.

Note: No experimental confirmation available.

Show »
Length:326
Mass (Da):36,232
Checksum:i5C94DABAC6D74ABA
GO
Isoform 5 (identifier: P46937-5) [UniParc]FASTAAdd to Basket

Also known as: YAP1-1alpha

The sequence of this isoform differs from the canonical sequence as follows:
     230-267: Missing.
     328-343: Missing.

Show »
Length:450
Mass (Da):48,275
Checksum:i295934FD185E7C59
GO
Isoform 6 (identifier: P46937-6) [UniParc]FASTAAdd to Basket

Also known as: YAP1-1gamma

The sequence of this isoform differs from the canonical sequence as follows:
     230-267: Missing.

Show »
Length:466
Mass (Da):49,989
Checksum:iF1E76E6DEB3F93C0
GO
Isoform 7 (identifier: P46937-7) [UniParc]FASTAAdd to Basket

Also known as: YAP1-1delta

The sequence of this isoform differs from the canonical sequence as follows:
     230-267: Missing.
     328-328: Q → QVRPQ

Show »
Length:470
Mass (Da):50,469
Checksum:i8935AAD2FA859F62
GO
Isoform 8 (identifier: P46937-8) [UniParc]FASTAAdd to Basket

Also known as: YAP1-2beta

The sequence of this isoform differs from the canonical sequence as follows:
     329-343: AMRNINPSTANSPKC → VRP

Show »
Length:492
Mass (Da):53,228
Checksum:i289722956D96193A
GO
Isoform 9 (identifier: P46937-9) [UniParc]FASTAAdd to Basket

Also known as: YAP1-2delta

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: Q → QVRPQ

Note: Highest expression in ovary and placenta, lowest in skeletal muscle and brain.

Show »
Length:508
Mass (Da):54,942
Checksum:iCFCC0BD04A27060B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 178178Missing in isoform 4. VSP_045190Add
BLAST
Alternative sequencei230 – 26738Missing in isoform 3, isoform 5, isoform 6 and isoform 7. VSP_039053Add
BLAST
Alternative sequencei328 – 34316Missing in isoform 2 and isoform 5. VSP_039054Add
BLAST
Alternative sequencei328 – 3281Q → QVRPQ in isoform 7 and isoform 9. VSP_053483
Alternative sequencei329 – 34315AMRNI…NSPKC → VRP in isoform 3 and isoform 8. VSP_039055Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links 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.
CCDSiCCDS44716.1. [P46937-1]
CCDS53699.1. [P46937-2]
CCDS53700.1. [P46937-4]
CCDS60944.1. [P46937-8]
CCDS60945.1. [P46937-3]
CCDS8314.2. [P46937-5]
PIRiA56954.
RefSeqiNP_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]
UniGeneiHs.503692.

Genome annotation databases

EnsembliENST00000282441; ENSP00000282441; ENSG00000137693. [P46937-1]
ENST00000345877; ENSP00000331023; ENSG00000137693. [P46937-3]
ENST00000524575; ENSP00000435602; ENSG00000137693. [P46937-4]
ENST00000526343; ENSP00000434134; ENSG00000137693. [P46937-5]
ENST00000531439; ENSP00000431574; ENSG00000137693. [P46937-2]
ENST00000537274; ENSP00000445635; ENSG00000137693. [P46937-8]
GeneIDi10413.
KEGGihsa:10413.
UCSCiuc001pgt.3. human. [P46937-1]
uc001pgu.3. human. [P46937-2]

Polymorphism databases

DMDMi294862479.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links 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 .
CCDSi CCDS44716.1. [P46937-1 ]
CCDS53699.1. [P46937-2 ]
CCDS53700.1. [P46937-4 ]
CCDS60944.1. [P46937-8 ]
CCDS60945.1. [P46937-3 ]
CCDS8314.2. [P46937-5 ]
PIRi A56954.
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 ]
UniGenei Hs.503692.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00702.
ProteinModelPortali P46937.
SMRi P46937. Positions 50-100, 165-265.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115684. 99 interactions.
DIPi DIP-40839N.
IntActi P46937. 68 interactions.
MINTi MINT-110802.
STRINGi 9606.ENSP00000282441.

PTM databases

PhosphoSitei P46937.

Polymorphism databases

DMDMi 294862479.

Proteomic databases

MaxQBi P46937.
PaxDbi P46937.
PRIDEi P46937.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282441 ; ENSP00000282441 ; ENSG00000137693 . [P46937-1 ]
ENST00000345877 ; ENSP00000331023 ; ENSG00000137693 . [P46937-3 ]
ENST00000524575 ; ENSP00000435602 ; ENSG00000137693 . [P46937-4 ]
ENST00000526343 ; ENSP00000434134 ; ENSG00000137693 . [P46937-5 ]
ENST00000531439 ; ENSP00000431574 ; ENSG00000137693 . [P46937-2 ]
ENST00000537274 ; ENSP00000445635 ; ENSG00000137693 . [P46937-8 ]
GeneIDi 10413.
KEGGi hsa:10413.
UCSCi uc001pgt.3. human. [P46937-1 ]
uc001pgu.3. human. [P46937-2 ]

Organism-specific databases

CTDi 10413.
GeneCardsi GC11P102015.
HGNCi HGNC:16262. YAP1.
HPAi CAB009370.
MIMi 606608. gene.
neXtProti NX_P46937.
Orphaneti 1473. Uveal coloboma - cleft lip and palate - intellectual disability.
PharmGKBi PA38103.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
HOGENOMi HOG000007854.
HOVERGENi HBG002748.
KOi K16687.
OMAi LRQSSYE.
PhylomeDBi P46937.
TreeFami TF326941.

Enzyme and pathway databases

Reactomei REACT_116022. Nuclear signaling by ERBB4.
REACT_116145. PPARA activates gene expression.
REACT_118607. Signaling by Hippo.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
SignaLinki P46937.

Miscellaneous databases

ChiTaRSi YAP1. human.
EvolutionaryTracei P46937.
GeneWikii YAP1.
GenomeRNAii 10413.
NextBioi 35497342.
PROi P46937.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46937.
Bgeei P46937.
CleanExi HS_YAP1.
Genevestigatori P46937.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
Pfami PF00397. WW. 2 hits.
[Graphical view ]
SMARTi SM00456. WW. 2 hits.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 2 hits.
PROSITEi PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "YAP is a candidate oncogene for esophageal squamous-cell carcinoma."
    Inazawa J., Imoto I., Muramatsu T.
    Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6).
    Tissue: Esophagus.
  4. "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.
    , 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 and Thalamus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "Identification, basic characterization and evolutionary analysis of differentially spliced mRNA isoforms of human YAP1 gene."
    Gaffney C.J., Oka T., Mazack V., Hilman D., Gat U., Muramatsu T., Inazawa J., Golden A., Carey D.J., Farooq A., Tromp G., Sudol M.
    Gene 509:215-222(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 206-369 (ISOFORMS 3; 7; 8 AND 9), ALTERNATIVE SPLICING.
    Tissue: Pancreas.
  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.
  10. "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.
  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.
  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.
  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.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  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.
  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.
  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.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-127; SER-131; SER-138; THR-154; SER-274; SER-289 AND SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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].
  20. "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.
  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.
  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.
  23. "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.
  24. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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.
  28. "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.
  29. Cited for: STRUCTURE BY NMR OF 165-204.
  30. "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.

Entry informationi

Entry nameiYAP1_HUMAN
AccessioniPrimary (citable) accession number: P46937
Secondary accession number(s): B4DTY1
, B7ZA01, E3WEB5, E3WEB6, E9PRV2, F5H202, K0KQ18, K0KYZ8, K0L195, K0L1G3, Q7Z574, Q8IUY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 20, 2010
Last modified: September 3, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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