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CWC25_SCHPO
ID   CWC25_SCHPO             Reviewed;         376 AA.
AC   Q9Y805; Q9UU20;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Pre-mRNA-splicing factor cwf25;
DE   AltName: Full=Complexed with cdc5 protein 25;
GN   Name=cwf25; ORFNames=SPBC146.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 211-354.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   IDENTIFICATION IN THE CWF 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-268, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Involved in mRNA splicing.
CC   -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC       cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC       cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC       cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC       cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC       prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC       smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CWC25 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB46758.1; -; Genomic_DNA.
DR   EMBL; AB027864; BAA87168.1; -; Genomic_DNA.
DR   PIR; T39419; T39419.
DR   RefSeq; NP_595394.1; NM_001021301.2.
DR   AlphaFoldDB; Q9Y805; -.
DR   SMR; Q9Y805; -.
DR   BioGRID; 276238; 11.
DR   IntAct; Q9Y805; 6.
DR   STRING; 4896.SPBC146.05c.1; -.
DR   iPTMnet; Q9Y805; -.
DR   MaxQB; Q9Y805; -.
DR   PaxDb; Q9Y805; -.
DR   PRIDE; Q9Y805; -.
DR   EnsemblFungi; SPBC146.05c.1; SPBC146.05c.1:pep; SPBC146.05c.
DR   GeneID; 2539683; -.
DR   KEGG; spo:SPBC146.05c; -.
DR   PomBase; SPBC146.05c; cwf25.
DR   VEuPathDB; FungiDB:SPBC146.05c; -.
DR   eggNOG; KOG3869; Eukaryota.
DR   HOGENOM; CLU_025093_0_0_1; -.
DR   InParanoid; Q9Y805; -.
DR   OMA; VEWMYAV; -.
DR   PhylomeDB; Q9Y805; -.
DR   PRO; PR:Q9Y805; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:PomBase.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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   Coiled coil; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome.
FT   CHAIN           1..376
FT                   /note="Pre-mRNA-splicing factor cwf25"
FT                   /id="PRO_0000079593"
FT   REGION          153..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          25..60
FT                   /evidence="ECO:0000255"
FT   COILED          286..334
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        153..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        211..212
FT                   /note="NW -> FG (in Ref. 2; BAA87168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="S -> T (in Ref. 2; BAA87168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  46057 MW;  7CAD5F99CF165B15 CRC64;
     MGGGDLNMKK SWHPLLMRNQ EKVWKDEQAH KEEMKRVEQL RREIEEERQL LELHRLQEAA
     GGKKRKDRVE WMYAVPNTNG PNRDSSEMEE YLLGRRRLDD LLKDKIEDQN NSLEKTEFIA
     LQNANSLQDT QAKLRLDPLL AIKQQEQKQL QTLMEKRKYS LDSDRKSKER RHRDRHHRSN
     QDRSRERSDN EQHSSDKREH SRRSYRNDRN NWRERTHNDR YRHRDKYDSG YFKKHYDDDM
     RFDQGHFQDE RDLKKYVRTS RQYSRSPSPD FRTRNHQFHS RDSQPITQRH TDIESRLQKM
     QDNAKELDES RRKKIELLEK KERDEEQFLE KERRDTARKW DNQGDFIRNM RKEIYSGDSV
     SLADRVNSSR HNMLRP
 
 
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