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CG21_SCHPO
ID   CG21_SCHPO              Reviewed;         415 AA.
AC   P24865; Q9USI7; Q9USI9;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=G2/mitotic-specific cyclin cig1;
GN   Name=cig1; ORFNames=SPCC4E9.02, SPCC645.01;
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 [GENOMIC DNA].
RX   PubMed=1829983; DOI=10.1016/0092-8674(91)90147-q;
RA   Bueno A., Richardson H.E., Reed S.I., Russell P.;
RT   "A fission yeast B-type cyclin functioning early in the cell cycle.";
RL   Cell 66:149-159(1991).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, 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: Required for efficient passage of the G1/S transition.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin G subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M68881; AAA35288.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB57300.1; -; Genomic_DNA.
DR   PIR; T41518; T41518.
DR   RefSeq; NP_588110.2; NM_001023100.2.
DR   AlphaFoldDB; P24865; -.
DR   SMR; P24865; -.
DR   BioGRID; 275996; 10.
DR   STRING; 4896.SPCC4E9.02.1; -.
DR   iPTMnet; P24865; -.
DR   MaxQB; P24865; -.
DR   PaxDb; P24865; -.
DR   PRIDE; P24865; -.
DR   EnsemblFungi; SPCC4E9.02.1; SPCC4E9.02.1:pep; SPCC4E9.02.
DR   GeneID; 2539433; -.
DR   KEGG; spo:SPCC4E9.02; -.
DR   PomBase; SPCC4E9.02; cig1.
DR   VEuPathDB; FungiDB:SPCC4E9.02; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_10_6_1; -.
DR   InParanoid; P24865; -.
DR   OMA; HKYHENI; -.
DR   PhylomeDB; P24865; -.
DR   PRO; PR:P24865; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; EXP:PomBase.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IMP:PomBase.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..415
FT                   /note="G2/mitotic-specific cyclin cig1"
FT                   /id="PRO_0000080400"
FT   REGION          54..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        39
FT                   /note="R -> P (in Ref. 1; AAA35288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="D -> H (in Ref. 1; AAA35288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        375
FT                   /note="I -> N (in Ref. 1; AAA35288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="M -> W (in Ref. 1; AAA35288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   415 AA;  47808 MW;  352A6E48D309D06B CRC64;
     MDVSTQTRHA TYFQDENQLQ KDHIYVKKKS HIKLNTGVRA PFKAVDNINQ QDEPTLIEGN
     NESSISSSTG DTFEEDFAYQ DKVEIEERSI RSTPKSIGDD DLENREGSFD APEGILTHGK
     HRLPTIPEWT KEDLAALSEA AARLQANPSP EDIETDPSMV PDYDPEIFHY MQSLERKLAP
     PPNYMSVQQE IDWVTRHMLV DWIVQVQIHF RLLPETLFLA VNLIDRFLSI KVVSLQKVQL
     VGLSALLIAC KYEEIHPPSI YNFAHVVQGI FTVDEIIRAE RYMLMLLDFD ISWPGPMSFL
     RRISRADSYD HDIRMLAKYL QEVTLMDEIF IGAHISFIAA TAYYLSMQML GHLDWTPCHV
     YYSGYTARQL KPCAIIIMEC LVDAPNHHNA IYRKYSENRM KRVSAFAHNW VLSVI
 
 
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