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POG1_YEAST
ID   POG1_YEAST              Reviewed;         351 AA.
AC   P40473; D6VVG5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Transcriptional activator POG1;
DE   AltName: Full=Promoter of growth protein 1;
GN   Name=POG1; OrderedLocusNames=YIL122W;
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   FUNCTION.
RX   PubMed=9927449; DOI=10.1093/genetics/151.2.531;
RA   Leza M.A., Elion E.A.;
RT   "POG1, a novel yeast gene, promotes recovery from pheromone arrest via the
RT   G1 cyclin CLN2.";
RL   Genetics 151:531-543(1999).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12464632; DOI=10.1101/gad.1039602;
RA   Horak C.E., Luscombe N.M., Qian J., Bertone P., Piccirrillo S.,
RA   Gerstein M., Snyder M.;
RT   "Complex transcriptional circuitry at the G1/S transition in Saccharomyces
RT   cerevisiae.";
RL   Genes Dev. 16:3017-3033(2002).
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 BY CDC28.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [8]
RP   INDUCTION.
RX   PubMed=16278933; DOI=10.1002/yea.1302;
RA   de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA   Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT   "New weakly expressed cell cycle-regulated genes in yeast.";
RL   Yeast 22:1191-1201(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=17986087; DOI=10.1111/j.1574-6968.2007.00947.x;
RA   Demae M., Murata Y., Hisano M., Haitani Y., Shima J., Takagi H.;
RT   "Overexpression of two transcriptional factors, Kin28 and Pog1, suppresses
RT   the stress sensitivity caused by the rsp5 mutation in Saccharomyces
RT   cerevisiae.";
RL   FEMS Microbiol. Lett. 277:70-78(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-314, 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).
CC   -!- FUNCTION: Transcriptional activator which promotes cell cycle recovery
CC       with CLN2, after pheromone induced G1 arrest, probably inhibiting the
CC       ability of STE20 to activate the pheromone response pathway. Binds the
CC       promoters of genes that function in cell cycle regulation, cytoskeletal
CC       organization, and spindle assembly. May also be involved in stress-
CC       resistance. {ECO:0000269|PubMed:12464632, ECO:0000269|PubMed:17986087,
CC       ECO:0000269|PubMed:9927449}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Expressed periodically during cell division. Regulated by
CC       the SBF complex which is one critical regulator of the start of the
CC       cell cycle. {ECO:0000269|PubMed:12464632, ECO:0000269|PubMed:16278933}.
CC   -!- PTM: Phosphorylated by CDC28. {ECO:0000305|PubMed:14574415}.
CC   -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the POG1 family. {ECO:0000305}.
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DR   EMBL; Z46833; CAA86870.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08431.1; -; Genomic_DNA.
DR   PIR; S49887; S49887.
DR   RefSeq; NP_012144.1; NM_001179470.1.
DR   AlphaFoldDB; P40473; -.
DR   BioGRID; 34869; 114.
DR   DIP; DIP-2755N; -.
DR   IntAct; P40473; 8.
DR   MINT; P40473; -.
DR   STRING; 4932.YIL122W; -.
DR   iPTMnet; P40473; -.
DR   MaxQB; P40473; -.
DR   PaxDb; P40473; -.
DR   PRIDE; P40473; -.
DR   EnsemblFungi; YIL122W_mRNA; YIL122W; YIL122W.
DR   GeneID; 854684; -.
DR   KEGG; sce:YIL122W; -.
DR   SGD; S000001384; POG1.
DR   VEuPathDB; FungiDB:YIL122W; -.
DR   eggNOG; ENOG502S5H5; Eukaryota.
DR   HOGENOM; CLU_792700_0_0_1; -.
DR   InParanoid; P40473; -.
DR   OMA; PQANIYG; -.
DR   BioCyc; YEAST:G3O-31375-MON; -.
DR   PRO; PR:P40473; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40473; protein.
DR   GO; GO:0000785; C:chromatin; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0000321; P:re-entry into mitotic cell cycle after pheromone arrest; IMP:SGD.
PE   1: Evidence at protein level;
KW   Activator; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..351
FT                   /note="Transcriptional activator POG1"
FT                   /id="PRO_0000202962"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   351 AA;  39498 MW;  35EE3E9F93FDCE0C CRC64;
     MKQEPHRQSE EKEKPKGPMA VEREQHTSLS SGTTVTASTG DESTNSRPVE SSQTEKSLSL
     RIRILKQLGF DDIQELNACD TGLVEQFLNV RLINDTKELE KIRESNLAKL NQIIDKCMES
     DKISDSTLNK ILDMSMNRDT NNDNNNHLTI PSPITTKKRK INASELASPR GHRRYRSDIP
     TVSEVETGVG YPQIHQQPGA YTLPMPANQW MSNPYMQPPQ PQVQQIMPQY LYPPGMGPQA
     QLPTMSSNSE SQTPVMSSQF LSLNQHGLYQ QNIGAHPVMS MGPQANIYGQ QHQLQPGQER
     DQSRKSFSHR RSQSANISMA NFRSPMRNPQ PASSQRPVNF LIHTPKHPPP T
 
 
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