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P46937

- YAP1_HUMAN

UniProt

P46937 - YAP1_HUMAN

Protein

Yorkie homolog

Gene

YAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    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

    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.

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Coloboma, ocular, with or without hearing impairment, cleft lip/palate, and/or mental retardation (COCLEMR) [MIM:120433]: An 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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 – 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 – 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

    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.By similarity11 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. 100 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.
    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 YORKIE family.Curated
    Contains 2 WW domains.PROSITE-ProRule annotation

    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

    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:
    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, Polymorphism

    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. 100 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 120433. phenotype.
    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

    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 COCLEMR, 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.

    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: October 1, 2014
    This is version 147 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