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EDC2_YEAST
ID   EDC2_YEAST              Reviewed;         145 AA.
AC   P40023; D3DLT4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Enhancer of mRNA-decapping protein 2;
GN   Name=EDC2; OrderedLocusNames=YER035W;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=11139489; DOI=10.1093/genetics/157.1.27;
RA   Dunckley T., Tucker M., Parker R.;
RT   "Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in
RT   Saccharomyces cerevisiae.";
RL   Genetics 157:27-37(2001).
RN   [5]
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   [6]
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   [7]
RP   FUNCTION.
RX   PubMed=12554866; DOI=10.1261/rna.2151403;
RA   Steiger M., Carr-Schmid A., Schwartz D.C., Kiledjian M., Parker R.;
RT   "Analysis of recombinant yeast decapping enzyme.";
RL   RNA 9:231-238(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=12554867; DOI=10.1261/rna.2171203;
RA   Schwartz D., Decker C.J., Parker R.;
RT   "The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and
RT   stimulate the activity of the decapping enzyme.";
RL   RNA 9:239-251(2003).
CC   -!- FUNCTION: mRNA-binding protein which stimulates mRNA decapping by DCP1
CC       and DCP2. {ECO:0000269|PubMed:11139489, ECO:0000269|PubMed:12554866,
CC       ECO:0000269|PubMed:12554867}.
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}.
CC   -!- SIMILARITY: Belongs to the EDC family. {ECO:0000305}.
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DR   EMBL; U18796; AAB64570.1; -; Genomic_DNA.
DR   EMBL; AY558451; AAS56777.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07688.1; -; Genomic_DNA.
DR   PIR; S50538; S50538.
DR   RefSeq; NP_010952.3; NM_001178926.3.
DR   AlphaFoldDB; P40023; -.
DR   BioGRID; 36770; 62.
DR   DIP; DIP-5234N; -.
DR   IntAct; P40023; 5.
DR   MINT; P40023; -.
DR   STRING; 4932.YER035W; -.
DR   iPTMnet; P40023; -.
DR   PaxDb; P40023; -.
DR   PRIDE; P40023; -.
DR   EnsemblFungi; YER035W_mRNA; YER035W; YER035W.
DR   GeneID; 856757; -.
DR   KEGG; sce:YER035W; -.
DR   SGD; S000000837; EDC2.
DR   VEuPathDB; FungiDB:YER035W; -.
DR   HOGENOM; CLU_1797570_0_0_1; -.
DR   InParanoid; P40023; -.
DR   OMA; PSAKEHM; -.
DR   BioCyc; YEAST:G3O-30216-MON; -.
DR   PRO; PR:P40023; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40023; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:SGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0032056; P:positive regulation of translation in response to stress; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..145
FT                   /note="Enhancer of mRNA-decapping protein 2"
FT                   /id="PRO_0000202626"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  16071 MW;  4D8A461EFD78BFA9 CRC64;
     MGSETKHSAK VKIVTRESPP SAKEHMRPTK TQILVPPTQS LPNGKKPNFG KSTKQRREPR
     ERTSKTGHED DKATMVTVNI DAFLHDKAPK KKSCKYKKKK TRQYQDRAAA SIDSKPHVAG
     HTAFAGASFT TDIPHEAALP KPSFV
 
 
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