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CWC25_YEAST
ID   CWC25_YEAST             Reviewed;         179 AA.
AC   P53854; D6W0U8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Pre-mRNA-splicing factor CWC25;
DE   AltName: Full=Complexed with CEF1 protein 25;
GN   Name=CWC25; OrderedLocusNames=YNL245C; ORFNames=N0901;
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 96604 / S288c / FY1679;
RX   PubMed=9234673;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA   Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT   "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT   left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL   Yeast 13:849-860(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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
RN   [6]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, 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   -!- FUNCTION: Involved in pre-mRNA splicing.
CC   -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC       CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC       CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC       PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC       SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
CC       {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:14690591}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14690591}.
CC   -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CWC25 family. {ECO:0000305}.
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DR   EMBL; X96722; CAA65498.1; -; Genomic_DNA.
DR   EMBL; Z71522; CAA96153.1; -; Genomic_DNA.
DR   EMBL; AY693108; AAT93127.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10314.1; -; Genomic_DNA.
DR   PIR; S63213; S63213.
DR   RefSeq; NP_014154.1; NM_001183083.1.
DR   PDB; 5GMK; EM; 3.40 A; G=1-179.
DR   PDB; 5LJ3; EM; 3.80 A; F=1-179.
DR   PDB; 5LJ5; EM; 3.80 A; F=1-179.
DR   PDBsum; 5GMK; -.
DR   PDBsum; 5LJ3; -.
DR   PDBsum; 5LJ5; -.
DR   AlphaFoldDB; P53854; -.
DR   SMR; P53854; -.
DR   BioGRID; 35594; 392.
DR   ComplexPortal; CPX-1651; PRP19-associated complex.
DR   DIP; DIP-2781N; -.
DR   IntAct; P53854; 20.
DR   MINT; P53854; -.
DR   STRING; 4932.YNL245C; -.
DR   iPTMnet; P53854; -.
DR   MaxQB; P53854; -.
DR   PaxDb; P53854; -.
DR   PRIDE; P53854; -.
DR   TopDownProteomics; P53854; -.
DR   EnsemblFungi; YNL245C_mRNA; YNL245C; YNL245C.
DR   GeneID; 855476; -.
DR   KEGG; sce:YNL245C; -.
DR   SGD; S000005189; CWC25.
DR   VEuPathDB; FungiDB:YNL245C; -.
DR   eggNOG; KOG3869; Eukaryota.
DR   GeneTree; ENSGT00440000039055; -.
DR   HOGENOM; CLU_025093_3_1_1; -.
DR   InParanoid; P53854; -.
DR   OMA; IEKERQF; -.
DR   BioCyc; YEAST:G3O-33242-MON; -.
DR   PRO; PR:P53854; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53854; protein.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IDA:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR   InterPro; IPR019339; CIR_N_dom.
DR   InterPro; IPR022209; CWC25.
DR   Pfam; PF10197; Cir_N; 1.
DR   Pfam; PF12542; CWC25; 1.
DR   SMART; SM01083; Cir_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Spliceosome.
FT   CHAIN           1..179
FT                   /note="Pre-mRNA-splicing factor CWC25"
FT                   /id="PRO_0000079596"
FT   REGION          99..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          25..57
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        102..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:5GMK"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:5GMK"
FT   HELIX           19..41
FT                   /evidence="ECO:0007829|PDB:5GMK"
SQ   SEQUENCE   179 AA;  20374 MW;  C6146E12248E48E8 CRC64;
     MGSGDLNLLK SWNPKLMKNR KKVWETEQDL ITEQQKLNTR LKEIEKEREL NELLNESSKD
     KPETLKNDLA LKKSGLEWMY QDAKLSDEKE DYLLGKKKLD SSILNQPATP PVRAATTISA
     SGAATSISSQ KKKSKLLKDD PMSKFKVTKQ QRRTPDSTKK RAMSQRGKPL SKPAPDLDY
 
 
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