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YL032_YEAST
ID   YL032_YEAST             Reviewed;         825 AA.
AC   Q07834; D6VXX3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=KH domain-containing protein YLL032C;
GN   OrderedLocusNames=YLL032C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, AND IDENTIFICATION BY
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z73137; CAA97481.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09289.1; -; Genomic_DNA.
DR   PIR; S64783; S64783.
DR   RefSeq; NP_013068.1; NM_001181852.1.
DR   AlphaFoldDB; Q07834; -.
DR   SMR; Q07834; -.
DR   BioGRID; 31221; 152.
DR   DIP; DIP-1956N; -.
DR   IntAct; Q07834; 4.
DR   MINT; Q07834; -.
DR   STRING; 4932.YLL032C; -.
DR   iPTMnet; Q07834; -.
DR   MaxQB; Q07834; -.
DR   PaxDb; Q07834; -.
DR   PRIDE; Q07834; -.
DR   EnsemblFungi; YLL032C_mRNA; YLL032C; YLL032C.
DR   GeneID; 850627; -.
DR   KEGG; sce:YLL032C; -.
DR   SGD; S000003955; YLL032C.
DR   VEuPathDB; FungiDB:YLL032C; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   GeneTree; ENSGT00940000169857; -.
DR   HOGENOM; CLU_020231_0_0_1; -.
DR   InParanoid; Q07834; -.
DR   OMA; IFEIHPD; -.
DR   BioCyc; YEAST:G3O-32135-MON; -.
DR   PRO; PR:Q07834; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07834; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..825
FT                   /note="KH domain-containing protein YLL032C"
FT                   /id="PRO_0000247115"
FT   DOMAIN          482..556
FT                   /note="KH"
FT   REGION          727..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         762
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   825 AA;  94597 MW;  00ADD65FBF1FA9FA CRC64;
     MDNFKIYSTV ITTAFLQVPH LYTTNRLWKP IEAPFLVEFL QKRISSKELK NTKAICHIDP
     SWVNLNASFI RDDMISIKAT TDDMDLDAIC RISLPLPMNT NDLTAELEKM KRILLDLSEK
     FNLELIITKE PAYFTPEQTG ESKELCIYVH ALGFRSNLME CEPQLLAFVD LIKKNGMTLP
     PQHYIIEPME LNSYSVLPLY MGVDMENFKH ISRAFKTSIY APSLITLSRD LKANPQIFFS
     GAVHSLSLLA RKTLRESISV NSKSFFYRRL TNITPGKLLF IRKYYQQKVN QLILKYQSLI
     RVTNEYIEFQ SISTNLLEMV IKNFTIQVLH EIVEVQISLN ENCAMSPELI IDSFFGHTGN
     QIVVITPKED SFNQLIVVGN QSSTDEASDT SILHYLSDFI MGSNQVINPN LRQIKAIFEI
     HPDFEDFISG KKNGKLTRIM ELSACLIQLE MEEEDDNLYL NLVSDSFPDF KESFKNVINE
     FPAEESFFIP EVCHRPIIGT GGSLIQATMR KHNVFIQFSN SFNLPQNKIS MIRYDNVIIR
     CPRKNKANIC LAKNDLKQIV QEYDSLQSKT LIRFSSGQYR HILHVNGQKN IIGQIEKNEN
     VYIMIPLKEP LDGTSQLSIQ GNDENASRAA NELVNSAFGY EYEFKIDQEI DPNKEYEFYN
     LIVVPFLQIM NIIVTFEKDL ITFTFEKDTN ENTLTKAIEL LSNYLETQKT KIIFKKIIKK
     FVLGSASSKS NTSNSNTNGN FRSMNNAKSR TTIDNTSQSG ASPQRHKMPV ITTVGGAQAI
     KGYIPNTYYN GYGYGYGYTY EYDYNYANSN KAQTNNRHKY QNGRK
 
 
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