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GTT3_YEAST
ID   GTT3_YEAST              Reviewed;         337 AA.
AC   P39996; D3DLN3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Glutathione transferase 3;
GN   Name=GTT3; OrderedLocusNames=YEL017W;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-72; SER-99 AND
RP   SER-116, 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   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:14562095};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U18530; AAB64494.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07637.1; -; Genomic_DNA.
DR   PIR; S50442; S50442.
DR   RefSeq; NP_010899.3; NM_001178832.3.
DR   AlphaFoldDB; P39996; -.
DR   BioGRID; 36714; 38.
DR   DIP; DIP-2062N; -.
DR   IntAct; P39996; 9.
DR   MINT; P39996; -.
DR   STRING; 4932.YEL017W; -.
DR   iPTMnet; P39996; -.
DR   MaxQB; P39996; -.
DR   PaxDb; P39996; -.
DR   PRIDE; P39996; -.
DR   EnsemblFungi; YEL017W_mRNA; YEL017W; YEL017W.
DR   GeneID; 856698; -.
DR   KEGG; sce:YEL017W; -.
DR   SGD; S000000743; GTT3.
DR   VEuPathDB; FungiDB:YEL017W; -.
DR   eggNOG; ENOG502S2H3; Eukaryota.
DR   HOGENOM; CLU_052849_0_0_1; -.
DR   InParanoid; P39996; -.
DR   OMA; IRYDLPS; -.
DR   BioCyc; YEAST:G3O-30142-MON; -.
DR   PRO; PR:P39996; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P39996; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR   InterPro; IPR038872; Put_GTT3.
DR   PANTHER; PTHR41807; PTHR41807; 1.
PE   1: Evidence at protein level;
KW   Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..337
FT                   /note="Glutathione transferase 3"
FT                   /id="PRO_0000202611"
FT   TOPO_DOM        1..239
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..313
FT                   /note="Perinuclear space"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          66..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   337 AA;  38235 MW;  E9F07EFD2A522006 CRC64;
     MPTKSTFSRW KKADLIDLAN KLEIDGFPNY AKKSDMIDYL ESHLNHLEKP VDFKDDYPEL
     RSFYESMTVD QSKDERNEYG SGSGNGSGSG SCDTATNDSD LEKAYIKEDD DEKPQSGDET
     SATKPLSSRN ANSNAKTNFN LLDFSTDNDS STSAFTKFKF NFQEYLSDIR YQTQKLNENV
     QDYLSTISAV DTIFSLLEFS FLVRNILAAG QPTSSSSLAS SLEAAVAAHN KYQYTLDFCL
     PILTWLLFFR GIPTLVSYYI NFIRYDLNIE LDPMTFNLTK FLISLAIFKT CNNKNIDFHS
     FRCVNQLWTQ LCTVNRSLGM VPLVFSMVSC LLTLYVL
 
 
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