Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P46937 (YAP1_HUMAN)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transcriptional coactivator YAP1

Gene

YAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (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
Isoform 2: Isoform 2 and isoform 3 can activate the C-terminal fragment (CTF) of ERBB4 (isoform 3).1 Publication

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionActivator, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-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-8951671. RUNX3 regulates YAP1-mediated transcription.
SignaLinkiP46937.
SIGNORiP46937.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional coactivator YAP1
Short name:
Yes-associated protein 1
Alternative name(s):
Protein yorkie homolog
Yes-associated protein YAP65 homolog
Gene namesi
Name:YAP1
Synonyms:YAP65
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16262. YAP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • TEAD-1-YAP complex Source: CAFA
  • TEAD-2-YAP complex Source: CAFA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Coloboma, ocular, with or without hearing impairment, cleft lip/palate, and/or mental retardation (COB1)1 Publication
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:120433

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi61S → 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 Publication1
Mutagenesisi80V → A: No change in interaction with TEAD4. Reduced interaction with TEAD4 and transforming ability; when associated with A-84 and A-85. 1 Publication1
Mutagenesisi84V → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-85. 1 Publication1
Mutagenesisi85P → A: Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-84. 1 Publication1
Mutagenesisi86M → A: Complete loss of interaction with TEAD1. 1 Publication1
Mutagenesisi89R → A: Complete loss of interaction with TEAD1. 1 Publication1
Mutagenesisi91L → A: Complete loss of interaction with TEAD1. 1 Publication1
Mutagenesisi94S → 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 Publications1
Mutagenesisi95F → A: Complete loss of interaction with TEAD1. 1 Publication1
Mutagenesisi96F → A: Loss of interaction with TEAD1. 1 Publication1
Mutagenesisi109S → 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 Publication1
Mutagenesisi122H → A, R, N or K: Loss of phosphorylation by LATS1. 2 Publications1
Mutagenesisi122H → L or Y: Significantly decreased phosphorylation at S-127 and decreased interaction with YWHAB. 2 Publications1
Mutagenesisi124R → A: Loss of phosphorylation by LATS1. 1 Publication1
Mutagenesisi127S → 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 Publications1
Mutagenesisi129P → D: No effect on phosphorylation but loss of interaction with YWHAB. 1 Publication1
Mutagenesisi164S → 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 Publication1
Mutagenesisi199W → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-202. 1 Publication1
Mutagenesisi202P → A: Loss of interaction with ERBB4 and loss of transcriptional coactivation function toward CTF; when associated with A-199. 1 Publication1
Mutagenesisi397S → A: Loss of phosphorylation by LATS1. 1 Publication1
Mutagenesisi407Y → E: Enhanced interaction with TP73. 1 Publication1
Mutagenesisi407Y → F: No phosphorylation by ABL1 and partial loss of binding to TP73. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi10413.
MalaCardsiYAP1.
MIMi120433. phenotype.
OpenTargetsiENSG00000137693.
Orphaneti1473. Uveal coloboma - cleft lip and palate - intellectual disability.
PharmGKBiPA38103.

Polymorphism and mutation databases

BioMutaiYAP1.
DMDMi294862479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760711 – 504Transcriptional coactivator YAP1Add BLAST504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61Phosphoserine; by LATS1 and LATS2Combined sources2 Publications1
Modified residuei63PhosphothreonineCombined sources1
Modified residuei105PhosphoserineBy similarity1
Modified residuei109Phosphoserine; by LATS1 and LATS2Combined sources2 Publications1
Modified residuei110PhosphothreonineBy similarity1
Modified residuei119Phosphothreonine; by MAPK8 and MAPK9Combined sources1 Publication1
Modified residuei127Phosphoserine; by LATS1 and LATS2Combined sources4 Publications1
Modified residuei128PhosphoserineCombined sources1
Modified residuei131PhosphoserineCombined sources1
Modified residuei138Phosphoserine; by MAPK8 and MAPK9Combined sources1 Publication1
Modified residuei154Phosphothreonine; by MAPK8 and MAPK9Combined sources1 Publication1
Modified residuei164Phosphoserine; by LATS1 and LATS22 Publications1
Modified residuei274PhosphoserineCombined sources1
Modified residuei289PhosphoserineCombined sources1
Modified residuei367Phosphoserine; by MAPK8 and MAPK9Combined sources1 Publication1
Modified residuei371PhosphoserineCombined sources1
Modified residuei381PhosphoserineCombined sources1
Modified residuei382PhosphoserineCombined sources1
Modified residuei388PhosphoserineCombined sources1
Modified residuei397Phosphoserine; by LATS1 and LATS24 Publications1
Modified residuei400Phosphoserine; by CK11 Publication1
Modified residuei403Phosphoserine; by CK11 Publication1
Modified residuei407Phosphotyrosine; by ABL11 Publication1
Modified residuei412Phosphothreonine; by MAPK8 and MAPK91 Publication1

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46937.
MaxQBiP46937.
PaxDbiP46937.
PeptideAtlasiP46937.
PRIDEiP46937.

PTM databases

iPTMnetiP46937.
PhosphoSitePlusiP46937.

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

BgeeiENSG00000137693.
CleanExiHS_YAP1.
ExpressionAtlasiP46937. baseline and differential.
GenevisibleiP46937. HS.

Organism-specific databases

HPAiCAB009370.
HPA038885.

Interactioni

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 similarity10 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • activating transcription factor binding Source: CAFA
  • proline-rich region binding Source: Ensembl
  • protein C-terminus binding Source: Ensembl
  • protein heterodimerization activity Source: CAFA
Complete GO annotation...

Protein-protein interaction databases

BioGridi115684. 130 interactors.
DIPiDIP-40839N.
IntActiP46937. 86 interactors.
MINTiMINT-110802.
STRINGi9606.ENSP00000282441.

Structurei

Secondary structure

1504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 57Combined sources6
Helixi61 – 73Combined sources13
Turni75 – 77Combined sources3
Helixi86 – 88Combined sources3
Helixi93 – 96Combined sources4
Beta strandi169 – 171Combined sources3
Beta strandi177 – 181Combined sources5
Beta strandi183 – 185Combined sources3
Beta strandi187 – 191Combined sources5
Turni192 – 195Combined sources4
Beta strandi196 – 200Combined sources5
Helixi202 – 206Combined sources5
Beta strandi233 – 235Combined sources3
Beta strandi238 – 241Combined sources4
Turni242 – 244Combined sources3
Beta strandi245 – 250Combined sources6
Turni251 – 254Combined sources4
Beta strandi255 – 259Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RE1X-ray2.20C/D50-171[»]
4REXX-ray1.60A165-209[»]
DisProtiDP00702.
ProteinModelPortaliP46937.
SMRiP46937.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 204WW 1PROSITE-ProRule annotationAdd BLAST34
Domaini230 – 263WW 2PROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni291 – 504Transactivation domainAdd BLAST214

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili86 – 1001 PublicationAdd BLAST15
Coiled coili298 – 359Sequence analysisAdd BLAST62

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3 – 49Pro-richAdd BLAST47

Domaini

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

Sequence similaritiesi

Belongs to the YAP1 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0940. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00510000046760.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
InParanoidiP46937.
KOiK16687.
OMAiDQTTTWQ.
OrthoDBiEOG091G095A.
PhylomeDBiP46937.
TreeFamiTF326941.

Family and domain databases

InterProiView protein in InterPro
IPR001202. WW_dom.
PfamiView protein in Pfam
PF00397. WW. 2 hits.
SMARTiView protein in SMART
SM00456. WW. 2 hits.
SUPFAMiSSF51045. SSF51045. 2 hits.
PROSITEiView protein in PROSITE
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoforms of the YAP1-1 form contain only one 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

        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
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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071125139P → L1 Publication1
Natural variantiVAR_071126227S → L1 PublicationCorresponds to variant dbSNP:rs376161041Ensembl.1
Natural variantiVAR_071127330M → V1 PublicationCorresponds to variant dbSNP:rs777949318Ensembl.1
Natural variantiVAR_071128462G → E1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451901 – 178Missing in isoform 4. 1 PublicationAdd BLAST178
Alternative sequenceiVSP_039053230 – 267Missing in isoform 3, isoform 5, isoform 6 and isoform 7. 2 PublicationsAdd BLAST38
Alternative sequenceiVSP_039054328 – 343Missing in isoform 2 and isoform 5. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_053483328Q → QVRPQ in isoform 7 and isoform 9. 1 Publication1
Alternative sequenceiVSP_039055329 – 343AMRNI…NSPKC → VRP in isoform 3 and isoform 8. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS73373.1. [P46937-9]
CCDS73374.1. [P46937-7]
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. [P46937-7]
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]
GeneIDi10413.
KEGGihsa:10413.
UCSCiuc001pgt.3. human. [P46937-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 20, 2010
Last modified: July 5, 2017
This is version 176 of the entry and version 2 of the sequence. See 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families