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VHR1_YEAST
ID   VHR1_YEAST              Reviewed;         640 AA.
AC   P40522; D6VVM6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Transcription factor VHR1;
DE   AltName: Full=VHT1 regulator 1;
GN   Name=VHR1; OrderedLocusNames=YIL056W;
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=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   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   [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   INDUCTION.
RX   PubMed=15713640; DOI=10.1128/mcb.25.5.1860-1868.2005;
RA   Lucau-Danila A., Lelandais G., Kozovska Z., Tanty V., Delaveau T.,
RA   Devaux F., Jacq C.;
RT   "Early expression of yeast genes affected by chemical stress.";
RL   Mol. Cell. Biol. 25:1860-1868(2005).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16533810; DOI=10.1074/jbc.m512158200;
RA   Weider M., Machnik A., Klebl F., Sauer N.;
RT   "Vhr1p, a new transcription factor from budding yeast, regulates biotin-
RT   dependent expression of VHT1 and BIO5.";
RL   J. Biol. Chem. 281:13513-13524(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP   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: Transcription factor that binds to the VHRE consensus
CC       sequence in promoters of VHT1 and BIO5, and regulates their biotin-
CC       dependent expression. {ECO:0000269|PubMed:16533810}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16533810}.
CC   -!- INDUCTION: By stress, probably through the induction by the
CC       transcription factor PDR1. {ECO:0000269|PubMed:15713640}.
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VHR1 family. {ECO:0000305}.
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DR   EMBL; Z38060; CAA86175.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08492.1; -; Genomic_DNA.
DR   PIR; S48423; S48423.
DR   RefSeq; NP_012208.1; NM_001179406.1.
DR   AlphaFoldDB; P40522; -.
DR   SMR; P40522; -.
DR   BioGRID; 34935; 66.
DR   DIP; DIP-5411N; -.
DR   IntAct; P40522; 8.
DR   MINT; P40522; -.
DR   STRING; 4932.YIL056W; -.
DR   iPTMnet; P40522; -.
DR   MaxQB; P40522; -.
DR   PaxDb; P40522; -.
DR   PRIDE; P40522; -.
DR   EnsemblFungi; YIL056W_mRNA; YIL056W; YIL056W.
DR   GeneID; 854755; -.
DR   KEGG; sce:YIL056W; -.
DR   SGD; S000001318; VHR1.
DR   VEuPathDB; FungiDB:YIL056W; -.
DR   eggNOG; ENOG502QVE1; Eukaryota.
DR   GeneTree; ENSGT00940000176700; -.
DR   HOGENOM; CLU_006698_0_0_1; -.
DR   InParanoid; P40522; -.
DR   OMA; FVMERFF; -.
DR   BioCyc; YEAST:G3O-31326-MON; -.
DR   PRO; PR:P40522; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40522; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0061420; P:regulation of transcription from RNA polymerase II promoter in response to biotin starvation; IMP:SGD.
DR   InterPro; IPR007147; TF_Vhr.
DR   Pfam; PF04001; Vhr1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..640
FT                   /note="Transcription factor VHR1"
FT                   /id="PRO_0000202988"
FT   REGION          118..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   640 AA;  71421 MW;  F9A1D5753C272602 CRC64;
     MNGPPTFTQY RINKFSGNGA THKIRELLNF NDEKKWKQFS SRRLELIDKF QLSQYKASEQ
     DQNIKQIATI LRTEFGYPVS CSKEFEKLVT AAVQSVRRNR KRSKKRYALS IANGSGGNVN
     NSISSNSTSD DEISPSIYQR SNSDFLPSSN YAADFQFSNK FQPLMSHQSH NGTIFPTVGT
     QNDSSPSVTS TQQKYNDIVT MLVHDLVTNV VPLSEQALKD PYTGPNLSHF ATSSLSQQPN
     ITTNIPIDST VPFFLREKLL LQIQRSRTCQ DISQAAGSID IYANLEILGE MSIRMSIAFV
     IERFFSNLVS SSMKYITAKT CSPENLALLS QRLFGAATRH NLSHFPAAQV QLRLLYLVIG
     GIVKDFGFDP TLYPLSEIIH HIVMVQYPLA SSCASEPPSS SPNKRVKRSP PVVSSDVMLN
     NNNTLSNRAT LLTTLPMKPQ SANKDVNRRV IIRFNDREQA FTFHQLSNGP PTVSEVLENC
     KNLFNIINKN KNFGIFHNDN LLNDESLAKL FDSFSTSEIH LVIKDISTIP LQDAKIPVPI
     TLPKMSCIGE NPSMPSIPLV PQEKDDPKKS SLTAFDNILN RISKSPMNEE NSNTTLNTGT
     STSNTNNNDH NESVPAPYVT KNKNSFQNGN LPQPVFQPLL
 
 
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