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SWD3_SCHPO
ID   SWD3_SCHPO              Reviewed;         380 AA.
AC   O43017;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Set1 complex component swd3;
DE            Short=Set1C component swd3;
DE   AltName: Full=COMPASS component swd3;
DE   AltName: Full=Complex proteins associated with set1 protein swd3;
GN   Name=swd3 {ECO:0000312|EMBL:CAA17803.1}; ORFNames=SPBC354.03;
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] {ECO:0000312|EMBL:CAA17803.1}
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] {ECO:0000305}
RP   FUNCTION, AND IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=12488447; DOI=10.1074/jbc.m209562200;
RA   Roguev A., Schaft D., Shevchenko A., Aasland R., Shevchenko A.,
RA   Stewart A.F.;
RT   "High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation
RT   in budding and fission yeasts.";
RL   J. Biol. Chem. 278:8487-8493(2003).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=14617822; DOI=10.1074/mcp.m300081-mcp200;
RA   Roguev A., Shevchenko A., Schaft D., Thomas H., Stewart A.F.,
RA   Shevchenko A.;
RT   "A comparative analysis of an orthologous proteomic environment in the
RT   yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.";
RL   Mol. Cell. Proteomics 3:125-132(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP   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: The Set1 complex specifically methylates 'Lys-4' of histone
CC       H3. {ECO:0000269|PubMed:12488447}.
CC   -!- SUBUNIT: Component of the Set1 complex composed of ash2, sdc1, set1,
CC       shg1, spp1, swd1, swd2 and swd3. {ECO:0000269|PubMed:12488447,
CC       ECO:0000269|PubMed:14617822}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; CU329671; CAA17803.1; -; Genomic_DNA.
DR   PIR; T40283; T40283.
DR   RefSeq; NP_595227.1; NM_001021133.2.
DR   AlphaFoldDB; O43017; -.
DR   SMR; O43017; -.
DR   BioGRID; 277445; 234.
DR   IntAct; O43017; 3.
DR   STRING; 4896.SPBC354.03.1; -.
DR   iPTMnet; O43017; -.
DR   MaxQB; O43017; -.
DR   PaxDb; O43017; -.
DR   PRIDE; O43017; -.
DR   EnsemblFungi; SPBC354.03.1; SPBC354.03.1:pep; SPBC354.03.
DR   GeneID; 2540929; -.
DR   KEGG; spo:SPBC354.03; -.
DR   PomBase; SPBC354.03; swd3.
DR   VEuPathDB; FungiDB:SPBC354.03; -.
DR   eggNOG; KOG0266; Eukaryota.
DR   HOGENOM; CLU_000288_57_1_1; -.
DR   InParanoid; O43017; -.
DR   OMA; YDGMARI; -.
DR   PhylomeDB; O43017; -.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   PRO; PR:O43017; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IC:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:PomBase.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031507; P:heterochromatin assembly; IC:PomBase.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..380
FT                   /note="Set1 complex component swd3"
FT                   /id="PRO_0000051254"
FT   REPEAT          52..91
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          94..133
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          136..177
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          179..219
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          221..262
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          291..330
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          335..374
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   380 AA;  42980 MW;  B5A962506B0C0D7A CRC64;
     MDSTAQQFPL NHDLQVQKDQ KGVVEEDEEQ IHKRIRNYES HSGFSEYCTL FGHEKSVTCV
     SVSPNKRWIA TSSSDGTIKI WSALTFRLEC TLFGHYRGIS QVKWATGSKY LASASDDKTI
     RIWDFEKRCS VRCLKGHTNY VSSIDFNPLG TLLVSGSWDE TVRIWNLQDG TCLRMLPAHS
     EPIISVSISA DGTLCATASY DGMARIWDVL SGQCLKTLVE PINVPLSNLQ FTENRKYLLV
     SNLNSQIRLW DYRRNRVVRI FDSHVNTRYS MSWDCYSSKN IPKNTEALPN NDSSYPDDAE
     SFMHDAYLLI PSEDGTIQIT DPSTKIIIDD SIRHSDDPET SLLNVTSLGP FIITSGTDPY
     VRVWAPSLLL SKHEKDGFSP
 
 
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