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GAT1_YEAST
ID   GAT1_YEAST              Reviewed;         510 AA.
AC   P43574; D6VTK9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Transcriptional regulatory protein GAT1;
GN   Name=GAT1; OrderedLocusNames=YFL021W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=8622686; DOI=10.1128/mcb.16.3.847;
RA   Coffman J.A., Rai R., Cunningham T., Svetlov V., Cooper T.G.;
RT   "Gat1p, a GATA family protein whose production is sensitive to nitrogen
RT   catabolite repression, participates in transcriptional activation of
RT   nitrogen-catabolic genes in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 16:847-858(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-399 AND SER-418, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-262 AND SER-418, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262; SER-270; THR-369 AND
RP   SER-399, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Positive regulator of multiple nitrogen catabolic genes.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U27344; AAB03516.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09217.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12419.1; -; Genomic_DNA.
DR   PIR; S56233; S56233.
DR   RefSeq; NP_116632.1; NM_001179945.1.
DR   AlphaFoldDB; P43574; -.
DR   SMR; P43574; -.
DR   BioGRID; 31125; 79.
DR   DIP; DIP-4276N; -.
DR   IntAct; P43574; 7.
DR   MINT; P43574; -.
DR   STRING; 4932.YFL021W; -.
DR   iPTMnet; P43574; -.
DR   MaxQB; P43574; -.
DR   PaxDb; P43574; -.
DR   PRIDE; P43574; -.
DR   EnsemblFungi; YFL021W_mRNA; YFL021W; YFL021W.
DR   GeneID; 850523; -.
DR   KEGG; sce:YFL021W; -.
DR   SGD; S000001873; GAT1.
DR   VEuPathDB; FungiDB:YFL021W; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   HOGENOM; CLU_534434_0_0_1; -.
DR   InParanoid; P43574; -.
DR   BioCyc; YEAST:G3O-30439-MON; -.
DR   Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR   PRO; PR:P43574; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43574; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IGI:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0090294; P:nitrogen catabolite activation of transcription; IMP:SGD.
DR   GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IMP:SGD.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR013860; AreA_GATA.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071; PTHR10071; 1.
DR   Pfam; PF08550; DUF1752; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..510
FT                   /note="Transcriptional regulatory protein GAT1"
FT                   /id="PRO_0000083484"
FT   ZN_FING         310..334
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          220..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         369
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   510 AA;  56328 MW;  62D805E42695F35F CRC64;
     MHVFFPLLFR PSPVLFIACA YIYIDIYIHC TRCTVVNITM STNRVPNLDP DLNLNKEIWD
     LYSSAQKILP DSNRILNLSW RLHNRTSFHR INRIMQHSNS IMDFSASPFA SGVNAAGPGN
     NDLDDTDTDN QQFFLSDMNL NGSSVFENVF DDDDDDDDVE THSIVHSDLL NDMDSASQRA
     SHNASGFPNF LDTSCSSSFD DHFIFTNNLP FLNNNSINNN HSHNSSHNNN SPSIANNTNA
     NTNTNTSAST NTNSPLLRRN PSPSIVKPGS RRNSSVRKKK PALKKIKSST SVQSSATPPS
     NTSSNPDIKC SNCTTSTTPL WRKDPKGLPL CNACGLFLKL HGVTRPLSLK TDIIKKRQRS
     STKINNNITP PPSSSLNPGA AGKKKNYTAS VAASKRKNSL NIVAPLKSQD IPIPKIASPS
     IPQYLRSNTR HHLSSSVPIE AETFSSFRPD MNMTMNMNLH NASTSSFNNE AFWKPLDSAI
     DHHSGDTNPN SNMNTTPNGN LSLDWLNLNL
 
 
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