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YAP1_DANRE
ID   YAP1_DANRE              Reviewed;         442 AA.
AC   Q1L8J7; A1L1U5;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Transcriptional coactivator YAP1;
DE            Short=Yes-associated protein 1;
DE            Short=zYAP {ECO:0000303|PubMed:21687713};
DE   AltName: Full=Protein yorkie homolog;
DE   AltName: Full=Yes-associated protein YAP65 homolog;
GN   Name=yap1; ORFNames=CH211-181P1.5-001 {ECO:0000312|EMBL:CAK04259.2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19393221; DOI=10.1016/j.bbrc.2009.04.070;
RA   Jiang Q., Liu D., Gong Y., Wang Y., Sun S., Gui Y., Song H.;
RT   "yap is required for the development of brain, eyes, and neural crest in
RT   zebrafish.";
RL   Biochem. Biophys. Res. Commun. 384:114-119(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21687713; DOI=10.1371/journal.pone.0020309;
RA   Gee S.T., Milgram S.L., Kramer K.L., Conlon F.L., Moody S.A.;
RT   "Yes-associated protein 65 (YAP) expands neural progenitors and regulates
RT   Pax3 expression in the neural plate border zone.";
RL   PLoS ONE 6:E20309-E20309(2011).
RN   [5]
RP   FUNCTION.
RX   PubMed=25778702; DOI=10.1038/nature14215;
RA   Porazinski S., Wang H., Asaoka Y., Behrndt M., Miyamoto T., Morita H.,
RA   Hata S., Sasaki T., Krens S.F., Osada Y., Asaka S., Momoi A., Linton S.,
RA   Miesfeld J.B., Link B.A., Senga T., Castillo-Morales A., Urrutia A.O.,
RA   Shimizu N., Nagase H., Matsuura S., Bagby S., Kondoh H., Nishina H.,
RA   Heisenberg C.P., Furutani-Seiki M.;
RT   "YAP is essential for tissue tension to ensure vertebrate 3D body shape.";
RL   Nature 521:217-221(2015).
CC   -!- FUNCTION: Transcriptional regulator which can act both as a coactivator
CC       and a corepressor and is the critical downstream regulatory target in
CC       the Hippo signaling pathway that plays a pivotal role in organ size
CC       control and tumor suppression by restricting proliferation and
CC       promoting apoptosis (By similarity). Required for expansion of the
CC       neural plate and neural plate border zone progenitor pools. Acts as a
CC       direct regulator of pax3 expression via interaction with tead1
CC       (PubMed:21687713). Plays a key role in tissue tension and 3D tissue
CC       shape by regulating cortical actomyosin network formation
CC       (PubMed:25778702). {ECO:0000250|UniProtKB:P46937,
CC       ECO:0000269|PubMed:21687713}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46937}. Nucleus
CC       {ECO:0000250|UniProtKB:P46937}. Note=Both phosphorylation and cell
CC       density can regulate its subcellular localization. Phosphorylation
CC       sequesters it in the cytoplasm by inhibiting its translocation into the
CC       nucleus. At low density, predominantly nuclear and is translocated to
CC       the cytoplasm at high density. {ECO:0000250|UniProtKB:P46937}.
CC   -!- TISSUE SPECIFICITY: Expressed in the notochord, brain, eyes, branchial
CC       arches and pectoral fins. {ECO:0000269|PubMed:19393221}.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed in the embryo: maternal
CC       expression is ubiquitous. {ECO:0000269|PubMed:19393221}.
CC   -!- PTM: Phosphorylated by lats1 and lats2; leading to cytoplasmic
CC       translocation and inactivation. {ECO:0000250|UniProtKB:P46937}.
CC   -!- DISRUPTION PHENOTYPE: Embryos display a small head with smaller eyes
CC       than normal and fewer cartilages in the branchial arches. Marked
CC       increase in cell death in brain (PubMed:19393221). Incomplete epiboly
CC       at gastrulation, characterized by blastopore closure defects and
CC       impaired axis formation (PubMed:21687713).
CC       {ECO:0000269|PubMed:19393221, ECO:0000269|PubMed:21687713}.
CC   -!- SIMILARITY: Belongs to the YAP1 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shaping life - Issue 175 of
CC       January 2016;
CC       URL="https://web.expasy.org/spotlight/back_issues/175/";
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DR   EMBL; CR762425; CAK04259.2; -; Genomic_DNA.
DR   EMBL; CT573116; CAK04259.2; JOINED; Genomic_DNA.
DR   EMBL; BC129216; AAI29217.1; -; mRNA.
DR   RefSeq; NP_001132952.1; NM_001139480.1.
DR   AlphaFoldDB; Q1L8J7; -.
DR   SMR; Q1L8J7; -.
DR   STRING; 7955.ENSDARP00000089684; -.
DR   iPTMnet; Q1L8J7; -.
DR   PaxDb; Q1L8J7; -.
DR   Ensembl; ENSDART00000098914; ENSDARP00000089684; ENSDARG00000068401.
DR   Ensembl; ENSDART00000188193; ENSDARP00000152736; ENSDARG00000112952.
DR   GeneID; 561411; -.
DR   KEGG; dre:561411; -.
DR   CTD; 10413; -.
DR   ZFIN; ZDB-GENE-030131-9710; yap1.
DR   eggNOG; KOG0940; Eukaryota.
DR   GeneTree; ENSGT00510000046760; -.
DR   HOGENOM; CLU_041917_0_1_1; -.
DR   InParanoid; Q1L8J7; -.
DR   OMA; YYLNHIT; -.
DR   OrthoDB; 1006566at2759; -.
DR   PhylomeDB; Q1L8J7; -.
DR   TreeFam; TF326941; -.
DR   Reactome; R-DRE-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-DRE-2028269; Signaling by Hippo.
DR   Reactome; R-DRE-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DRE-8951671; RUNX3 regulates YAP1-mediated transcription.
DR   PRO; PR:Q1L8J7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000068401; Expressed in swim bladder and 25 other tissues.
DR   GO; GO:0000785; C:chromatin; IDA:ZFIN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:ZFIN.
DR   GO; GO:0030509; P:BMP signaling pathway; IMP:ZFIN.
DR   GO; GO:0007420; P:brain development; IMP:ZFIN.
DR   GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:CACAO.
DR   GO; GO:0048566; P:embryonic digestive tract development; IMP:ZFIN.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:CACAO.
DR   GO; GO:0007492; P:endoderm development; IMP:ZFIN.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:ZFIN.
DR   GO; GO:0060914; P:heart formation; IMP:CACAO.
DR   GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR   GO; GO:0001889; P:liver development; IMP:ZFIN.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR   GO; GO:0031016; P:pancreas development; IMP:ZFIN.
DR   GO; GO:1905480; P:positive regulation of glutamate-ammonia ligase activity; IMP:ZFIN.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048916; P:posterior lateral line development; IMP:ZFIN.
DR   GO; GO:0039022; P:pronephric duct development; IMP:ZFIN.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:ZFIN.
DR   GO; GO:0046620; P:regulation of organ growth; IMP:ZFIN.
DR   GO; GO:0003406; P:retinal pigment epithelium development; IMP:ZFIN.
DR   GO; GO:0003139; P:secondary heart field specification; IMP:ZFIN.
DR   GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR   GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
DR   GO; GO:0003173; P:ventriculo bulbo valve development; IMP:ZFIN.
DR   CDD; cd00201; WW; 2.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51045; SSF51045; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Activator; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..442
FT                   /note="Transcriptional coactivator YAP1"
FT                   /id="PRO_0000433905"
FT   DOMAIN          126..159
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          186..219
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   REGION          51..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..442
FT                   /note="Transactivation domain"
FT                   /evidence="ECO:0000250|UniProtKB:P46937"
FT   REGION          286..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          258..279
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        60..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine; by LATS1 and LATS2"
FT                   /evidence="ECO:0000250|UniProtKB:P46937"
FT   MOD_RES         69
FT                   /note="Phosphoserine; by LATS1 and LATS2"
FT                   /evidence="ECO:0000250|UniProtKB:P46937"
FT   MOD_RES         87
FT                   /note="Phosphoserine; by LATS1 and LATS2"
FT                   /evidence="ECO:0000250|UniProtKB:P46937"
FT   MOD_RES         119
FT                   /note="Phosphoserine; by LATS1 and LATS2"
FT                   /evidence="ECO:0000250|UniProtKB:P46937"
FT   CONFLICT        370
FT                   /note="G -> S (in Ref. 2; AAI29217)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  48362 MW;  F1B0FC36035C535C CRC64;
     MDPNQHNPPA GHQIVHVRGD SETDLEALFN AVMNPKNTIV PPSVPMRLRK LPDSFFTPPE
     PKSHSRQAST DAGTAGTVTP HHVRAHSSPA SLQLGAVSPG ALTSMGPANA PPQHLRQSSY
     EIPDDMPLPP GWEMAKTPSG QRYFLNHNDQ TTTWQDPRKA LLQMNQAAPA SPVPVQQQNI
     MNPASGPLPD GWEQAITSEG EIYYINHKNK TTSWLDPRLD PRFAMNQQRI SQSAPVKQGS
     QLPSSPQSGV MSGNNPIRLQ QIHIEKERLR IKQELLRQRP QELALRNQLP TSMEQDGGTQ
     NPVSSPGMGQ DARNMTTNSS DPFLNSGTYH SRDESTDSGL SMSSYSVPRT PDDFLNSVDE
     METGDTLGPG SMATQPSRFP DYLDAIPGTD VDLGTLEGES MAVEGEELMP SLQEALSSDI
     LNDMESVLAA TKIDKENFLT WL
 
 
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