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MET31_YEAST
ID   MET31_YEAST             Reviewed;         177 AA.
AC   Q03081; D6W3X6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Transcriptional regulator MET31;
DE   AltName: Full=Methionine-requiring protein 31;
GN   Name=MET31; OrderedLocusNames=YPL038W; ORFNames=P7102.12;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
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   [3]
RP   FUNCTION, AND INTERACTION WITH MET4 AND MET28.
RX   PubMed=9799240; DOI=10.1093/emboj/17.21.6327;
RA   Blaiseau P.L., Thomas D.;
RT   "Multiple transcriptional activation complexes tether the yeast activator
RT   Met4 to DNA.";
RL   EMBO J. 17:6327-6336(1998).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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   [6]
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).
CC   -!- FUNCTION: Auxiliary transcriptional regulator of sulfur amino acid
CC       metabolism. Involved in the transcriptional activation of MET28.
CC       {ECO:0000269|PubMed:9799240}.
CC   -!- SUBUNIT: Interacts with MET4 and MET28. {ECO:0000269|PubMed:9799240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U44030; AAB68182.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11392.1; -; Genomic_DNA.
DR   PIR; S62037; S62037.
DR   RefSeq; NP_015287.1; NM_001183852.1.
DR   AlphaFoldDB; Q03081; -.
DR   SMR; Q03081; -.
DR   BioGRID; 36141; 72.
DR   ComplexPortal; CPX-999; MET4-MET28-MET31 sulfur metabolism transcription factor complex.
DR   DIP; DIP-1445N; -.
DR   IntAct; Q03081; 16.
DR   MINT; Q03081; -.
DR   STRING; 4932.YPL038W; -.
DR   iPTMnet; Q03081; -.
DR   MaxQB; Q03081; -.
DR   PaxDb; Q03081; -.
DR   PRIDE; Q03081; -.
DR   EnsemblFungi; YPL038W_mRNA; YPL038W; YPL038W.
DR   GeneID; 856069; -.
DR   KEGG; sce:YPL038W; -.
DR   SGD; S000005959; MET31.
DR   VEuPathDB; FungiDB:YPL038W; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000176515; -.
DR   HOGENOM; CLU_040688_2_0_1; -.
DR   InParanoid; Q03081; -.
DR   OMA; CELVFRR; -.
DR   BioCyc; YEAST:G3O-33952-MON; -.
DR   PRO; PR:Q03081; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q03081; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005667; C:transcription regulator complex; IC:ComplexPortal.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IDA:SGD.
DR   GO; GO:0042762; P:regulation of sulfur metabolic process; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..177
FT                   /note="Transcriptional regulator MET31"
FT                   /id="PRO_0000046808"
FT   ZN_FING         95..117
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ   SEQUENCE   177 AA;  19557 MW;  BAF5C76E24A25AEE CRC64;
     MKLAQDMNVD EIFLKQAAEA IAVISSSPTH TDPIIRELLH RIRQSSPLSA VIPAPENVLK
     AGEPENMARG LIRIPETQTK RTGGNNHSKE GAQLYSCAKC QLKFSRSSDL RRHEKVHSLV
     LPHICSNCGK GFARKDALKR HSNTLTCQRN RKKLSEGSDV DVDELIKDAI KNGTGLL
 
 
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