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SRL2_YEAST
ID   SRL2_YEAST              Reviewed;         392 AA.
AC   Q12020; D6VY82;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Protein SRL2;
DE   AltName: Full=Suppressor of RAD53 null lethality protein 2;
GN   Name=SRL2; OrderedLocusNames=YLR082C;
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-11 AND SER-139, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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   -!- INTERACTION:
CC       Q12020; P39014: MET30; NbExp=3; IntAct=EBI-38714, EBI-11507;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z73254; CAA97641.1; -; Genomic_DNA.
DR   EMBL; U53880; AAB67586.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09398.1; -; Genomic_DNA.
DR   PIR; S64914; S64914.
DR   RefSeq; NP_013183.1; NM_001181969.1.
DR   AlphaFoldDB; Q12020; -.
DR   BioGRID; 31355; 108.
DR   DIP; DIP-1442N; -.
DR   IntAct; Q12020; 9.
DR   MINT; Q12020; -.
DR   STRING; 4932.YLR082C; -.
DR   iPTMnet; Q12020; -.
DR   MaxQB; Q12020; -.
DR   PaxDb; Q12020; -.
DR   PRIDE; Q12020; -.
DR   EnsemblFungi; YLR082C_mRNA; YLR082C; YLR082C.
DR   GeneID; 850771; -.
DR   KEGG; sce:YLR082C; -.
DR   SGD; S000004072; SRL2.
DR   VEuPathDB; FungiDB:YLR082C; -.
DR   HOGENOM; CLU_071668_0_0_1; -.
DR   OMA; STHTICF; -.
DR   BioCyc; YEAST:G3O-32233-MON; -.
DR   PRO; PR:Q12020; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12020; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Protein SRL2"
FT                   /id="PRO_0000270577"
FT   REGION          18..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   392 AA;  45140 MW;  A39CD3D2E0F9BBF3 CRC64;
     MSNFKNFTLN SFEDYYGKPS ETPKMEEEKL EVTNVNASSS KKVHKSKKST SKYDQKNVFR
     NSMTGIAQIL PTKPVKIIEQ NIDFANPKSF DLLQSTHTIC FNKRINTTNT KLNVETHTSS
     DIDNDILHVG APTDLGGNSN DEAETRQLRK FRWSNNKEKS LCEKLTVIYW ALLLHTTKRA
     SKRRPILCHQ MIAEFFNRVY KEKSRVPITS RYIRDNLVAW VTQGKELHEK GWVGDAKTGD
     LQEQFNIATV KLYESAEDGR LSIGKDKPFR EENTGSDSLV RAEEDSTAVT NENGHISSEK
     NLKKDRRESI RNQILTLDLN DEDFFQNVMK VLSAIDEPEL RQYVIVISEL VSMEMDDGKT
     VREKLRDVEL NINRLQVDIK EIKEMLVTLI NK
 
 
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