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GATA4_MOUSE
ID   GATA4_MOUSE             Reviewed;         441 AA.
AC   Q08369; B9EHF7; P97491; Q9QZK4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 4.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Transcription factor GATA-4;
DE   AltName: Full=GATA-binding factor 4;
GN   Name=Gata4; Synonyms=Gata-4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8455608; DOI=10.1128/mcb.13.4.2235-2246.1993;
RA   Arceci R.J., King A.A., Simon M.C., Orkin S.H., Wilson D.B.;
RT   "Mouse GATA-4: a retinoic acid-inducible GATA-binding transcription factor
RT   expressed in endodermally derived tissues and heart.";
RL   Mol. Cell. Biol. 13:2235-2246(1993).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX   PubMed=8083222; DOI=10.1016/s0021-9258(17)31636-8;
RA   Laverriere A.C., Macneill C., Mueller C., Poelmann R.E., Burch J.B.E.,
RA   Evans T.;
RT   "GATA-4/5/6, a subfamily of three transcription factors transcribed in
RT   developing heart and gut.";
RL   J. Biol. Chem. 269:23177-23184(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Morrisey E.E., Parmacek M.S.;
RT   "Murine GATA-4 is expressed in heart and gut tissues.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Heart;
RA   Katsuoka F., Motohashi H., Yamamoto M.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   CHARACTERIZATION.
RX   PubMed=7717974; DOI=10.1042/bj3070183;
RA   Bielinska M., Wilson D.B.;
RT   "Regulation of J6 gene expression by transcription factor GATA-4.";
RL   Biochem. J. 307:183-189(1995).
RN   [9]
RP   INTERACTION WITH NFATC4.
RX   PubMed=9568714; DOI=10.1016/s0092-8674(00)81573-1;
RA   Molkentin J.D., Lu J.-R., Antos C.L., Markham B., Richardson J.,
RA   Robbins J., Grant S.R., Olson E.N.;
RT   "A calcineurin-dependent transcriptional pathway for cardiac hypertrophy.";
RL   Cell 93:215-228(1998).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH NKX2-5.
RX   PubMed=9584153; DOI=10.1128/mcb.18.6.3120;
RA   Lee Y., Shioi T., Kasahara H., Jobe S.M., Wiese R.J., Markham B.E.,
RA   Izumo S.;
RT   "The cardiac tissue-restricted homeobox protein Csx/Nkx2.5 physically
RT   associates with the zinc finger protein GATA4 and cooperatively activates
RT   atrial natriuretic factor gene expression.";
RL   Mol. Cell. Biol. 18:3120-3129(1998).
RN   [11]
RP   INTERACTION WITH JARID2.
RX   PubMed=15542826; DOI=10.1128/mcb.24.23.10151-10160.2004;
RA   Kim T.-G., Chen J., Sadoshima J., Lee Y.;
RT   "Jumonji represses atrial natriuretic factor gene expression by inhibiting
RT   transcriptional activities of cardiac transcription factors.";
RL   Mol. Cell. Biol. 24:10151-10160(2004).
RN   [12]
RP   INTERACTION WITH LMCD1.
RX   PubMed=16199866; DOI=10.1128/mcb.25.20.8864-8873.2005;
RA   Rath N., Wang Z., Lu M.M., Morrisey E.E.;
RT   "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6
RT   function by inhibiting DNA binding.";
RL   Mol. Cell. Biol. 25:8864-8873(2005).
RN   [13]
RP   INTERACTION WITH TBX18.
RX   PubMed=17584735; DOI=10.1074/jbc.m703724200;
RA   Farin H.F., Bussen M., Schmidt M.K., Singh M.K., Schuster-Gossler K.,
RA   Kispert A.;
RT   "Transcriptional repression by the T-box proteins Tbx18 and Tbx15 depends
RT   on Groucho corepressors.";
RL   J. Biol. Chem. 282:25748-25759(2007).
RN   [14]
RP   METHYLATION AT LYS-299.
RX   PubMed=22215809; DOI=10.1101/gad.173930.111;
RA   He A., Shen X., Ma Q., Cao J., von Gise A., Zhou P., Wang G., Marquez V.E.,
RA   Orkin S.H., Pu W.T.;
RT   "PRC2 directly methylates GATA4 and represses its transcriptional
RT   activity.";
RL   Genes Dev. 26:37-42(2012).
RN   [15]
RP   FUNCTION.
RX   PubMed=35182466; DOI=10.1016/j.cell.2022.01.021;
RA   Gonzalez-Teran B., Pittman M., Felix F., Thomas R., Richmond-Buccola D.,
RA   Huettenhain R., Choudhary K., Moroni E., Costa M.W., Huang Y.,
RA   Padmanabhan A., Alexanian M., Lee C.Y., Maven B.E.J., Samse-Knapp K.,
RA   Morton S.U., McGregor M., Gifford C.A., Seidman J.G., Seidman C.E.,
RA   Gelb B.D., Colombo G., Conklin B.R., Black B.L., Bruneau B.G., Krogan N.J.,
RA   Pollard K.S., Srivastava D.;
RT   "Transcription factor protein interactomes reveal genetic determinants in
RT   heart disease.";
RL   Cell 0:0-0(2022).
CC   -!- FUNCTION: Transcriptional activator that binds to the consensus
CC       sequence 5'-AGATAG-3' and plays a key role in cardiac development
CC       (PubMed:35182466). In cooperation with TBX5, it binds to cardiac super-
CC       enhancers and promotes cardiomyocyte gene expression, while it down-
CC       regulates endocardial and endothelial gene expression (By similarity).
CC       Involved in bone morphogenetic protein (BMP)-mediated induction of
CC       cardiac-specific gene expression (By similarity). Binds to BMP response
CC       element (BMPRE) DNA sequences within cardiac activating regions (By
CC       similarity). Acts as a transcriptional activator of ANF in cooperation
CC       with NKX2-5 (PubMed:9584153). Promotes cardiac myocyte enlargement (By
CC       similarity). Required during testicular development (By similarity).
CC       May play a role in sphingolipid signaling by regulating the expression
CC       of sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate
CC       lyase (By similarity). {ECO:0000250|UniProtKB:P43694,
CC       ECO:0000250|UniProtKB:P46152, ECO:0000269|PubMed:35182466,
CC       ECO:0000269|PubMed:9584153}.
CC   -!- SUBUNIT: Interacts with ZNF260 (By similarity). Interacts with the
CC       homeobox domain of NKX2-5 through its C-terminal zinc finger. Also
CC       interacts with JARID2 which represses its ability to activate
CC       transcription of ANF. Interacts (via the second Zn finger) with NFATC4
CC       (PubMed:9568714). Interacts with LMCD1 (PubMed:16199866). Forms a
CC       complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates
CC       hypertrophy in cardiomyocytes. Interacts with NR5A1, ZFPM2 and TBX5.
CC       Interacts with TBX18. Interacts with GLYR1; the interaction is required
CC       for a synergistic activation of GATA4 target genes transcription (By
CC       similarity). {ECO:0000250|UniProtKB:P43694,
CC       ECO:0000269|PubMed:15542826, ECO:0000269|PubMed:16199866,
CC       ECO:0000269|PubMed:17584735, ECO:0000269|PubMed:9568714,
CC       ECO:0000269|PubMed:9584153}.
CC   -!- INTERACTION:
CC       Q08369; Q62315: Jarid2; NbExp=3; IntAct=EBI-297008, EBI-493592;
CC       Q08369; P42582: Nkx2-5; NbExp=4; IntAct=EBI-297008, EBI-297021;
CC       Q08369; Q99593: TBX5; Xeno; NbExp=2; IntAct=EBI-297008, EBI-297043;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43694}.
CC   -!- TISSUE SPECIFICITY: Heart, intestine, liver, primative endoderm and
CC       gonads.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- PTM: Methylation at Lys-299 attenuates transcriptional activity.
CC       {ECO:0000269|PubMed:22215809}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37662.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M98339; AAA37662.1; ALT_FRAME; mRNA.
DR   EMBL; U85046; AAB42015.1; -; mRNA.
DR   EMBL; AF179424; AAD55266.1; -; mRNA.
DR   EMBL; AC090654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466535; EDL36067.1; -; Genomic_DNA.
DR   EMBL; BC137824; AAI37825.1; -; mRNA.
DR   CCDS; CCDS49519.1; -.
DR   PIR; A48099; A48099.
DR   RefSeq; NP_032118.2; NM_008092.4.
DR   AlphaFoldDB; Q08369; -.
DR   SMR; Q08369; -.
DR   BioGRID; 199841; 17.
DR   DIP; DIP-33032N; -.
DR   IntAct; Q08369; 3.
DR   MINT; Q08369; -.
DR   STRING; 10090.ENSMUSP00000066927; -.
DR   BindingDB; Q08369; -.
DR   ChEMBL; CHEMBL1687680; -.
DR   iPTMnet; Q08369; -.
DR   PhosphoSitePlus; Q08369; -.
DR   MaxQB; Q08369; -.
DR   PaxDb; Q08369; -.
DR   PRIDE; Q08369; -.
DR   ProteomicsDB; 271190; -.
DR   Antibodypedia; 3405; 770 antibodies from 45 providers.
DR   DNASU; 14463; -.
DR   Ensembl; ENSMUST00000118022; ENSMUSP00000113891; ENSMUSG00000021944.
DR   GeneID; 14463; -.
DR   KEGG; mmu:14463; -.
DR   UCSC; uc007uhn.1; mouse.
DR   CTD; 2626; -.
DR   MGI; MGI:95664; Gata4.
DR   VEuPathDB; HostDB:ENSMUSG00000021944; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   GeneTree; ENSGT00940000158349; -.
DR   HOGENOM; CLU_027524_0_0_1; -.
DR   InParanoid; Q08369; -.
DR   PhylomeDB; Q08369; -.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 14463; 7 hits in 75 CRISPR screens.
DR   PRO; PR:Q08369; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q08369; protein.
DR   Bgee; ENSMUSG00000021944; Expressed in epithelium of stomach and 113 other tissues.
DR   ExpressionAtlas; Q08369; baseline and differential.
DR   Genevisible; Q08369; MM.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0051525; F:NFAT protein binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0003180; P:aortic valve morphogenesis; ISO:MGI.
DR   GO; GO:0060413; P:atrial septum morphogenesis; ISO:MGI.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003290; P:atrial septum secundum morphogenesis; ISO:MGI.
DR   GO; GO:0036302; P:atrioventricular canal development; IGI:BHF-UCL.
DR   GO; GO:0003190; P:atrioventricular valve formation; IGI:BHF-UCL.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IGI:MGI.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IGI:MGI.
DR   GO; GO:0061026; P:cardiac muscle tissue regeneration; IDA:BHF-UCL.
DR   GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003279; P:cardiac septum development; IGI:BHF-UCL.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
DR   GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:MGI.
DR   GO; GO:0060540; P:diaphragm morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR   GO; GO:0035054; P:embryonic heart tube anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR   GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
DR   GO; GO:0003197; P:endocardial cushion development; IMP:BHF-UCL.
DR   GO; GO:0001706; P:endoderm formation; IMP:MGI.
DR   GO; GO:0072148; P:epithelial cell fate commitment; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060575; P:intestinal epithelial cell differentiation; ISO:MGI.
DR   GO; GO:0060464; P:lung lobe formation; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0008584; P:male gonad development; ISO:MGI.
DR   GO; GO:0003192; P:mitral valve formation; TAS:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR   GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IGI:BHF-UCL.
DR   GO; GO:1905204; P:negative regulation of connective tissue replacement; IDA:BHF-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0003151; P:outflow tract morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
DR   GO; GO:0051891; P:positive regulation of cardioblast differentiation; IEP:BHF-UCL.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IDA:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:MGI.
DR   GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR   GO; GO:0051896; P:regulation of protein kinase B signaling; IDA:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0043627; P:response to estrogen; IDA:MGI.
DR   GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR   GO; GO:0060008; P:Sertoli cell differentiation; IMP:MGI.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; NAS:UniProtKB.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0060290; P:transdifferentiation; ISO:MGI.
DR   GO; GO:0003195; P:tricuspid valve formation; TAS:BHF-UCL.
DR   GO; GO:0035239; P:tube morphogenesis; IGI:MGI.
DR   GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR   GO; GO:0003229; P:ventricular cardiac muscle tissue development; IGI:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:BHF-UCL.
DR   GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
DR   CDD; cd00202; ZnF_GATA; 2.
DR   Gene3D; 3.30.50.10; -; 2.
DR   InterPro; IPR008013; GATA_N.
DR   InterPro; IPR016375; TF_GATA_4/5/6.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071; PTHR10071; 1.
DR   Pfam; PF00320; GATA; 2.
DR   Pfam; PF05349; GATA-N; 1.
DR   PIRSF; PIRSF003028; TF_GATA_4/5/6; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 2.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Methylation; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..441
FT                   /note="Transcription factor GATA-4"
FT                   /id="PRO_0000083414"
FT   ZN_FING         216..240
FT                   /note="GATA-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   ZN_FING         270..294
FT                   /note="GATA-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          60..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         299
FT                   /note="N6-methyllysine; by EZH2"
FT                   /evidence="ECO:0000269|PubMed:22215809"
FT   CONFLICT        385..402
FT                   /note="FSTVSGHGPSIHPVLSAL -> SVCVRPRALHPSSAVCS (in Ref. 1;
FT                   AAA37662 and 3; AAB42015)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  44580 MW;  E9521771741DD08E CRC64;
     MYQSLAMAAN HGPPPGAYEA GGPGAFMHSA GAASSPVYVP TPRVPSSVLG LSYLQGGGSA
     AAAGTTSGGS SGAGPSGAGP GTQQGSPGWS QAGAEGAAYT PPPVSPRFSF PGTTGSLAAA
     AAAAAAREAA AYGSGGGAAG AGLAGREQYG RPGFAGSYSS PYPAYMADVG ASWAAAAAAS
     AGPFDSPVLH SLPGRANPGR HPNLDMFDDF SEGRECVNCG AMSTPLWRRD GTGHYLCNAC
     GLYHKMNGIN RPLIKPQRRL SASRRVGLSC ANCQTTTTTL WRRNAEGEPV CNACGLYMKL
     HGVPRPLAMR KEGIQTRKRK PKNLNKSKTP AGPAGETLPP SSGASSGNSS NATSSSSSSE
     EMRPIKTEPG LSSHYGHSSS MSQTFSTVSG HGPSIHPVLS ALKLSPQGYA SPVTQTSQAS
     SKQDSWNSLV LADSHGDIIT A
 
 
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