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ASG1_YEAST
ID   ASG1_YEAST              Reviewed;         964 AA.
AC   P40467; D6VVF7; Q45U13;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Activator of stress genes 1;
GN   Name=ASG1; OrderedLocusNames=YIL130W;
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], AND VARIANTS ASN-77; SER-149; PHE-353;
RP   SER-682; PHE-707; THR-770; SER-811; ASN-ASP-ASN-ASN-ASN-852 INS; ASN-887
RP   INS AND 926-ASN--GLN-933 DEL.
RC   STRAIN=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [2]
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   [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   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=11353088; DOI=10.1093/nar/29.10.2181;
RA   Akache B., Wu K., Turcotte B.;
RT   "Phenotypic analysis of genes encoding yeast zinc cluster proteins.";
RL   Nucleic Acids Res. 29:2181-2190(2001).
RN   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963, 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-166 AND SER-963, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-963, AND
RP   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).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Probable transcription factor involved in the stress
CC       response. {ECO:0000269|PubMed:11353088}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- DISRUPTION PHENOTYPE: No growth on non-fermentable carbon sources like
CC       glycerol and lactate and sensitivity to calcofluor white.
CC       {ECO:0000269|PubMed:11353088}.
CC   -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ASG1 family. {ECO:0000305}.
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DR   EMBL; DQ115392; AAZ22497.1; -; Genomic_DNA.
DR   EMBL; Z38059; CAA86148.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08423.1; -; Genomic_DNA.
DR   PIR; S48404; S48404.
DR   RefSeq; NP_012136.1; NM_001179478.1.
DR   AlphaFoldDB; P40467; -.
DR   SMR; P40467; -.
DR   BioGRID; 34861; 66.
DR   DIP; DIP-820N; -.
DR   IntAct; P40467; 4.
DR   MINT; P40467; -.
DR   STRING; 4932.YIL130W; -.
DR   iPTMnet; P40467; -.
DR   MaxQB; P40467; -.
DR   PaxDb; P40467; -.
DR   PRIDE; P40467; -.
DR   TopDownProteomics; P40467; -.
DR   EnsemblFungi; YIL130W_mRNA; YIL130W; YIL130W.
DR   GeneID; 854676; -.
DR   KEGG; sce:YIL130W; -.
DR   SGD; S000001392; ASG1.
DR   VEuPathDB; FungiDB:YIL130W; -.
DR   eggNOG; ENOG502QSY2; Eukaryota.
DR   GeneTree; ENSGT00940000176737; -.
DR   HOGENOM; CLU_010084_1_0_1; -.
DR   InParanoid; P40467; -.
DR   OMA; MAADRCA; -.
DR   BioCyc; YEAST:G3O-31381-MON; -.
DR   PRO; PR:P40467; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40467; protein.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Stress response; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..964
FT                   /note="Activator of stress genes 1"
FT                   /id="PRO_0000114997"
FT   DNA_BIND        21..47
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphoserine; by ATM or ATR"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         963
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   VARIANT         77
FT                   /note="S -> N (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         149
FT                   /note="N -> S (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         353
FT                   /note="I -> F (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         682
FT                   /note="F -> S (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         707
FT                   /note="S -> F (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         770
FT                   /note="I -> T (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         811
FT                   /note="N -> S (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         852
FT                   /note="D -> NDNNN (in strain: SK1)"
FT   VARIANT         887
FT                   /note="N -> NN (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
FT   VARIANT         926..933
FT                   /note="Missing (in strain: SK1)"
FT                   /evidence="ECO:0000269|PubMed:16273108"
SQ   SEQUENCE   964 AA;  108781 MW;  AD5ABE59E4B022CC CRC64;
     MPEQAQQGEQ SVKRRRVTRA CDECRKKKVK CDGQQPCIHC TVYSYECTYK KPTKRTQNSG
     NSGVLTLGNV TTGPSSSTVV AAAASNPNKL LSNIKTERAI LPGASTIPAS NNPSKPRKYK
     TKSTRLQSKI DRYKQIFDEV FPQLPDIDNL DIPVFLQIFH NFKRDSQSFL DDTVKEYTLI
     VNDSSSPIQP VLSSNSKNST PDEFLPNMKS DSNSASSNRE QDSVDTYSNI PVGREIKIIL
     PPKAIALQFV KSTWEHCCVL LRFYHRPSFI RQLDELYETD PNNYTSKQMQ FLPLCYAAIA
     VGALFSKSIV SNDSSREKFL QDEGYKYFIA ARKLIDITNA RDLNSIQAIL MLIIFLQCSA
     RLSTCYTYIG VAMRSALRAG FHRKLSPNSG FSPIEIEMRK RLFYTIYKLD VYINAMLGLP
     RSISPDDFDQ TLPLDLSDEN ITEVAYLPEN QHSVLSSTGI SNEHTKLFLI LNEIISELYP
     IKKTSNIISH ETVTSLELKL RNWLDSLPKE LIPNAENIDP EYERANRLLH LSFLHVQIIL
     YRPFIHYLSR NMNAENVDPL CYRRARNSIA VARTVIKLAK EMVSNNLLTG SYWYACYTIF
     YSVAGLLFYI HEAQLPDKDS AREYYDILKD AETGRSVLIQ LKDSSMAASR TYNLLNQIFE
     KLNSKTIQLT ALHSSPSNES AFLVTNNSSA LKPHLGDSLQ PPVFFSSQDT KNSFSLAKSE
     ESTNDYAMAN YLNNTPISEN PLNEAQQQDQ VSQGTTNMSN ERDPNNFLSI DIRLDNNGQS
     NILDATDDVF IRNDGDIPTN SAFDFSSSKS NASNNSNPDT INNNYNNVSG KNNNNNNITN
     NSNNNHNNNN NDNNNNNNNN NNNNNNNNNS GNSSNNNNNN NNNKNNNDFG IKIDNNSPSY
     EGFPQLQIPL SQDNLNIEDK EEMSPNIEIK NEQNMTDSND ILGVFDQLDA QLFGKYLPLN
     YPSE
 
 
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