Skip Header

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

P46937 - YAP1_HUMAN

UniProt

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. 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. transcription coactivator activity Source: UniProtKB
  2. transcription corepressor activity Source: UniProtKB
  3. 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. gene expression Source: Reactome
  6. hippo signaling Source: UniProtKB
  7. negative regulation of nucleic acid-templated transcription Source: GOC
  8. regulation of transcription, DNA-templated Source: UniProtKB-KW
  9. transcription initiation from RNA polymerase II promoter Source: Reactome
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:
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
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.

GO - Cellular componenti

  1. cell junction Source: HPA
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
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 retardation1 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)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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Transcriptional coactivator YAP1PRO_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 – 1101PhosphothreonineBy 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 YAP1.9 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

BgeeiP46937.
CleanExiHS_YAP1.
ExpressionAtlasiP46937. baseline and differential.
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.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P3522212EBI-1044059,EBI-491549
DDX17Q928417EBI-1044059,EBI-746012
ERBB4Q153033EBI-1044059,EBI-80371
LATS1O958358EBI-1044059,EBI-444209
MAP2K1Q027503EBI-1044059,EBI-492564
PRRG2O146693EBI-1044059,EBI-9824765
PTCH1Q136353EBI-1044059,EBI-8775406
PTPN14Q156786EBI-1044059,EBI-1237156
RUNX1Q011963EBI-1044059,EBI-925904
SMAD1Q157973EBI-1044059,EBI-1567153
SMAD7O151053EBI-1044059,EBI-3861591
TBX5Q995934EBI-1044059,EBI-297043
TEAD1P283475EBI-1044059,EBI-529156
TP53BP2Q13625-29EBI-1044059,EBI-287091
TP73O153503EBI-1044059,EBI-389606
TP73O15350-17EBI-1044059,EBI-389619
WBP1Q96G273EBI-1044059,EBI-3867685
Wbp1P9776413EBI-1044059,EBI-6304160From a different organism.
WBP2Q969T96EBI-1044059,EBI-727055
YWHABP319465EBI-1044059,EBI-359815
YWHAZP631043EBI-1044059,EBI-347088

Protein-protein interaction databases

BioGridi115684. 107 interactions.
DIPiDIP-40839N.
IntActiP46937. 74 interactions.
MINTiMINT-110802.
STRINGi9606.ENSP00000282441.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4RE1X-ray2.20C/D50-171[»]
DisProtiDP00702.
ProteinModelPortaliP46937.
SMRiP46937. Positions 50-100, 165-265.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 20434WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini230 – 26334WW 2PROSITE-ProRule annotationAdd
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 – 35962Sequence AnalysisAdd
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.

Sequence similaritiesi

Belongs to the YAP1 family.Curated
Contains 2 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00510000046760.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
InParanoidiP46937.
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 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391P → L.1 Publication
VAR_071125
Natural varianti227 – 2271S → L.1 Publication
VAR_071126
Natural varianti330 – 3301M → V.1 Publication
VAR_071127
Natural varianti462 – 4621G → E.1 Publication
VAR_071128

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 178178Missing in isoform 4. 1 PublicationVSP_045190Add
BLAST
Alternative sequencei230 – 26738Missing in isoform 3, isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_039053Add
BLAST
Alternative sequencei328 – 34316Missing in isoform 2 and isoform 5. 1 PublicationVSP_039054Add
BLAST
Alternative sequencei328 – 3281Q → QVRPQ in isoform 7 and isoform 9. 1 PublicationVSP_053483
Alternative sequencei329 – 34315AMRNI…NSPKC → VRP in isoform 3 and isoform 8. 1 PublicationVSP_039055Add
BLAST

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]
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]
GeneIDi10413.
KEGGihsa:10413.
UCSCiuc001pgt.3. human. [P46937-1]
uc001pgu.3. human. [P46937-2]

Polymorphism databases

DMDMi294862479.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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]
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4RE1X-ray2.20C/D50-171[»]
DisProtiDP00702.
ProteinModelPortaliP46937.
SMRiP46937. Positions 50-100, 165-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115684. 107 interactions.
DIPiDIP-40839N.
IntActiP46937. 74 interactions.
MINTiMINT-110802.
STRINGi9606.ENSP00000282441.

PTM databases

PhosphoSiteiP46937.

Polymorphism databases

DMDMi294862479.

Proteomic databases

MaxQBiP46937.
PaxDbiP46937.
PRIDEiP46937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
GeneIDi10413.
KEGGihsa:10413.
UCSCiuc001pgt.3. human. [P46937-1]
uc001pgu.3. human. [P46937-2]

Organism-specific databases

CTDi10413.
GeneCardsiGC11P102015.
HGNCiHGNC:16262. YAP1.
HPAiCAB009370.
MIMi120433. phenotype.
606608. gene.
neXtProtiNX_P46937.
Orphaneti1473. Uveal coloboma - cleft lip and palate - intellectual disability.
PharmGKBiPA38103.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00510000046760.
HOGENOMiHOG000007854.
HOVERGENiHBG002748.
InParanoidiP46937.
KOiK16687.
OMAiLRQSSYE.
PhylomeDBiP46937.
TreeFamiTF326941.

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.

Miscellaneous databases

ChiTaRSiYAP1. human.
EvolutionaryTraceiP46937.
GeneWikiiYAP1.
GenomeRNAii10413.
NextBioi35497342.
PROiP46937.
SOURCEiSearch...

Gene expression databases

BgeeiP46937.
CleanExiHS_YAP1.
ExpressionAtlasiP46937. baseline and differential.
GenevestigatoriP46937.

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]
ProtoNetiSearch...

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. "Heterozygous loss-of-function mutations in YAP1 cause both isolated and syndromic optic fissure closure defects."
    UK10K Consortium
    Williamson K.A., Rainger J., Floyd J.A., Ansari M., Meynert A., Aldridge K.V., Rainger J.K., Anderson C.A., Moore A.T., Hurles M.E., Clarke A., van Heyningen V., Verloes A., Taylor M.S., Wilkie A.O., Fitzpatrick D.R., Hurles M., FitzPatrick D.R.
    , Al-Turki S., Anderson C., Barroso I., Beales P., Bentham J., Bhattacharya S., Carss K., Chatterjee K., Cirak S., Cosgrove C., Daly A., Floyd J., Franklin C., Futema M., Humphries S., McCarthy S., Mitchison H., Muntoni F., Onoufriadis A., Parker V., Payne F., Plagnol V., Raymond L., Savage D., Scambler P., Schmidts M., Semple R., Serra E., Stalker J., van Kogelenberg M., Vijayarangakannan P., Walter K., Wood G.
    Am. J. Hum. Genet. 94:295-302(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN COB1, VARIANTS LEU-139; LEU-227; VAL-330 AND GLU-462.
  29. "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.
  30. Cited for: STRUCTURE BY NMR OF 165-204.
  31. "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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 151 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. 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.