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WHI4_YEAST
ID   WHI4_YEAST              Reviewed;         649 AA.
AC   Q07655; D6VRD1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Protein WHI4;
GN   Name=WHI4; OrderedLocusNames=YDL224C; ORFNames=D0839;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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=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   [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   PHOSPHORYLATION.
RX   PubMed=16172400; DOI=10.1073/pnas.0501046102;
RA   Budovskaya Y.V., Stephan J.S., Deminoff S.J., Herman P.K.;
RT   "An evolutionary proteomics approach identifies substrates of the cAMP-
RT   dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13933-13938(2005).
RN   [6]
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-206; SER-258 AND
RP   SER-283, AND 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: Has a partially redundant function to WHI3, a dosage-
CC       dependent modulator of cell size. {ECO:0000269|PubMed:11290704}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Cell cycle-regulated. Expression peaks during S/G2 phase.
CC       {ECO:0000269|PubMed:16278933}.
CC   -!- PTM: Phosphorylated by PKA in vitro. {ECO:0000269|PubMed:16172400}.
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DR   EMBL; Z74272; CAA98803.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11641.1; -; Genomic_DNA.
DR   PIR; S67787; S67787.
DR   RefSeq; NP_010057.1; NM_001180284.1.
DR   AlphaFoldDB; Q07655; -.
DR   SMR; Q07655; -.
DR   BioGRID; 31822; 93.
DR   DIP; DIP-4321N; -.
DR   IntAct; Q07655; 8.
DR   MINT; Q07655; -.
DR   STRING; 4932.YDL224C; -.
DR   iPTMnet; Q07655; -.
DR   MaxQB; Q07655; -.
DR   PaxDb; Q07655; -.
DR   PRIDE; Q07655; -.
DR   EnsemblFungi; YDL224C_mRNA; YDL224C; YDL224C.
DR   GeneID; 851302; -.
DR   KEGG; sce:YDL224C; -.
DR   SGD; S000002383; WHI4.
DR   VEuPathDB; FungiDB:YDL224C; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   GeneTree; ENSGT00940000176750; -.
DR   HOGENOM; CLU_018359_0_0_1; -.
DR   InParanoid; Q07655; -.
DR   OMA; THYANIL; -.
DR   BioCyc; YEAST:G3O-29604-MON; -.
DR   PRO; PR:Q07655; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q07655; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; ISS:SGD.
DR   GO; GO:0061157; P:mRNA destabilization; IGI:SGD.
DR   GO; GO:0008361; P:regulation of cell size; IGI: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   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..649
FT                   /note="Protein WHI4"
FT                   /id="PRO_0000262756"
FT   DOMAIN          533..625
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          196..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   649 AA;  70690 MW;  8A1E7DDED388B73C CRC64;
     MSLVHNQTNL NESKFLIERA FSSSSETVPL SKEATYPMPT AYSFSAVRSN SETNIKRENP
     QGFAKEPIMT SMLHNLTMST GKGNGNDVNS LAPHDVDVGP YCLLLRNLPK DITLRECYCI
     FSLATGVSSI ELKRDDREPF NDNEKVVVVK FGSLSLVTHY ANILNSKSEI FGPSFPFRSH
     IDVVNEQTQL PVSFQEHVSS GTTNSSPKNY QLSSSAQNEI QNQSFNTISY GKTSSSPLGP
     SAAKPRPSLL SERSLRFSFN DPFGLETISQ RKESVPFLRN SISQHDLSNV TTTPVPAGMP
     PQKDAGKSLL LLEKDEINES IWNGDELVND VGNSSFGASL QEPPMSSTPV MEWNASSTAN
     IPLFQLSSQE NHQSNLLPPS HHSISQDVPH IQSQPNLNNS GVIHSATSLP HYHLLNQINA
     STKTQSIQQS VSNVPSNLDL NLQTENGHPQ SSAPNGSSIF NNQKVNQGFL VSEQDTSTIS
     RQKECSSTAS ASAFSKNNET NVAGSTTISQ ADLSLLAKVP PPANPADQNP PCNTLYVGNL
     PPDATEQELR QLFSNQQGFR RLSFRNKMNS HGHGNGHGHG PICFVEFEDV SFATRALAEL
     YGSQLPHPRP SLNNKGGIRL SFSKNPLGVR GSNSRSKSGY SFNGSYGKS
 
 
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