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WHI3_YEAST
ID   WHI3_YEAST              Reviewed;         661 AA.
AC   P34761; D6W0Z0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Protein WHI3;
GN   Name=WHI3; OrderedLocusNames=YNL197C; ORFNames=N1382;
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 FUNCTION.
RX   PubMed=11290704; DOI=10.1093/genetics/157.4.1469;
RA   Nash R.S., Volpe T., Futcher B.;
RT   "Isolation and characterization of WHI3, a size-control gene of
RT   Saccharomyces cerevisiae.";
RL   Genetics 157:1469-1480(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7725799; DOI=10.1002/yea.320101213;
RA   Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT   "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT   WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT   new open reading frames of unknown function.";
RL   Yeast 10:1639-1645(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [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=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, 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: Involved in size control and cell cycle.
CC       {ECO:0000269|PubMed:11290704}.
CC   -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U01095; AAA03320.1; -; Genomic_DNA.
DR   EMBL; X78898; CAA55511.1; -; Genomic_DNA.
DR   EMBL; Z71473; CAA96092.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10356.1; -; Genomic_DNA.
DR   PIR; S50734; S50734.
DR   RefSeq; NP_014202.1; NM_001183035.1.
DR   AlphaFoldDB; P34761; -.
DR   SMR; P34761; -.
DR   BioGRID; 35636; 539.
DR   IntAct; P34761; 17.
DR   MINT; P34761; -.
DR   STRING; 4932.YNL197C; -.
DR   iPTMnet; P34761; -.
DR   MaxQB; P34761; -.
DR   PaxDb; P34761; -.
DR   PRIDE; P34761; -.
DR   TopDownProteomics; P34761; -.
DR   EnsemblFungi; YNL197C_mRNA; YNL197C; YNL197C.
DR   GeneID; 855524; -.
DR   KEGG; sce:YNL197C; -.
DR   SGD; S000005141; WHI3.
DR   VEuPathDB; FungiDB:YNL197C; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000176750; -.
DR   HOGENOM; CLU_018359_0_0_1; -.
DR   InParanoid; P34761; -.
DR   OMA; PQPEHMY; -.
DR   BioCyc; YEAST:G3O-33207-MON; -.
DR   PRO; PR:P34761; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P34761; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071554; P:cell wall organization or biogenesis; IMP:CACAO.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0061157; P:mRNA destabilization; IMP:SGD.
DR   GO; GO:0045793; P:positive regulation of cell size; IMP:CACAO.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CACAO.
DR   GO; GO:0032106; P:positive regulation of response to extracellular stimulus; IMP:CACAO.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:CACAO.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IMP:CACAO.
DR   GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   GO; GO:0061013; P:regulation of mRNA catabolic process; IMP:SGD.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..661
FT                   /note="Protein WHI3"
FT                   /id="PRO_0000082005"
FT   DOMAIN          538..625
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          14..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   661 AA;  71253 MW;  47A6B9716CF96043 CRC64;
     MQSSVYFDQT GSFASSSDNV VSSTTNTHNI SPSHRSSLNL NTTSHPHEAS GRGSASGELY
     LNDTNSPLAI SSMLNTLALG SMPQDIASSN ISNHDNNIKG SYSLKLSNVA KDITLRECYA
     IFALAEGVKS IELQKKNSSS SITSASLEDE NDIFIIARFE LLNLAINYAV ILNSKNELFG
     PSFPNKTTVE IIDDTTKNLV SFPSSAIFND TSRLNKSNSG MKRPSLLSQR SRFSFSDPFS
     NDSPLSQQQS QQQQQQPQQP QQHSTQKHSP QQCNQQQVNS SIPLSSQGQV IGLHSNHSHQ
     DLSVESTIQT SDIGKSFLLR DNTEINEKIW GTSGIPSSIN GYMSTPQPST PTLEWGNTSA
     SQHGSSFFLP SAASTAIAPT NSNTSANANA SSNNGASNNG ANQALSASSQ QPMMQIGNTI
     NTSLTSSNSL PPYGLMSSQS QHISNMVNTS DMNITPQKQN RFMQQPQPEH MYPVNQSNTP
     QKVPPARLSS SRNSHKNNST TSLSSNITGS ASISQADLSL LARIPPPANP ADQNPPCNTL
     YVGNLPSDAT EQELRQLFSG QEGFRRLSFR NKNTTSNGHS HGPMCFVEFD DVSFATRALA
     ELYGRQLPRS TVSSKGGIRL SFSKNPLGVR GPNSRRGGSG NPNPNVNMLS SYNSNVGHIK
     N
 
 
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