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JJJ2_YEAST
ID   JJJ2_YEAST              Reviewed;         583 AA.
AC   P46997; D6VW25;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=J protein JJJ2;
GN   Name=JJJ2; OrderedLocusNames=YJL162C; ORFNames=J0549;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 433 AND 483.
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   IDENTIFICATION OF PROBABLE SEQUENCE ERRORS.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
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   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   GENE NAME.
RX   PubMed=15170475; DOI=10.1038/sj.embor.7400172;
RA   Walsh P., Bursac D., Law Y.C., Cyr D., Lithgow T.;
RT   "The J-protein family: modulating protein assembly, disassembly and
RT   translocation.";
RL   EMBO Rep. 5:567-571(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, 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   [8]
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 184 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA89457.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z49437; CAA89457.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006943; DAA08641.1; -; Genomic_DNA.
DR   PIR; S56945; S56945.
DR   RefSeq; NP_012373.2; NM_001181595.1.
DR   AlphaFoldDB; P46997; -.
DR   SMR; P46997; -.
DR   BioGRID; 33597; 42.
DR   DIP; DIP-4033N; -.
DR   IntAct; P46997; 1.
DR   MINT; P46997; -.
DR   STRING; 4932.YJL162C; -.
DR   iPTMnet; P46997; -.
DR   MaxQB; P46997; -.
DR   PaxDb; P46997; -.
DR   PRIDE; P46997; -.
DR   EnsemblFungi; YJL162C_mRNA; YJL162C; YJL162C.
DR   GeneID; 853277; -.
DR   KEGG; sce:YJL162C; -.
DR   SGD; S000003698; JJJ2.
DR   VEuPathDB; FungiDB:YJL162C; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_490950_0_0_1; -.
DR   InParanoid; P46997; -.
DR   OMA; ARSKFEC; -.
DR   BioCyc; YEAST:G3O-31602-MON; -.
DR   PRO; PR:P46997; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P46997; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..583
FT                   /note="J protein JJJ2"
FT                   /id="PRO_0000071142"
FT   DOMAIN          11..79
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          215..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   583 AA;  67389 MW;  6CBB8ED37F5F340B CRC64;
     MSQVIEPQLD RTTYYSILGL TSNATSSEVH KSYLKLARLL HPDKTKSDKS EELFKAVVHA
     HSILTDEDQK LRYDRDLKIK GLHTYQPKKN CHIFKTKAKE SQGASPTLGQ SEAYHRQNKP
     YEQQPYGFGV GKKMTSSSKS KVPIFKSFNL KSYQRNHYYS SKKERKHGSP DIDSLFHETN
     GASKVRMTDA GKMDTNSQFQ EIWEILGKNA YTHKSYSEDP NSCLGSALSD HEEEEEAGKQ
     QQQQQQQQQQ QQHYGMTSKS SSPDEEKKNN KEPKRESRVS PEENGEEETG HKQFKLPKTS
     TFSSGSHDSN LQSPFYNHEY RHYARSKFEC KNQFRKSVSP IKEIPATTSA NEGWNILRDI
     IEKLNISNVD DRNKDLLFRR DEIGDKNHSD SIDIENLSIK EPKGMKRRKK DDISLEELFQ
     SLPREKDYFM MDAINDSLES INLFKKPKTT QSHEQGGTFA QAESNRAKFK PLLEQCGITP
     EILDLEIPEI PEFDAVADLE TLKLNVQLFN NQCNKLKETI HQVSLQRLRA DTQFSDMLTQ
     KQSIMVWKTY LEFDKSLMDK LNILQERQMQ VIKIFSERCD GKV
 
 
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