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CG13_YEAST
ID   CG13_YEAST              Reviewed;         580 AA.
AC   P13365; D6VPH6; E9P940;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=G1/S-specific cyclin CLN3;
GN   Name=CLN3; Synonyms=DAF1, WHI1; OrderedLocusNames=YAL040C; ORFNames=FUN10;
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 [GENOMIC DNA].
RC   STRAIN=S673A;
RX   PubMed=2907481; DOI=10.1002/j.1460-2075.1988.tb03332.x;
RA   Nash R., Tokiwa G., Anand S., Erickson C., Futcher A.B.;
RT   "The WHI1+ gene of Saccharomyces cerevisiae tethers cell division to cell
RT   size and is a cyclin homolog.";
RL   EMBO J. 7:4335-4346(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3062366; DOI=10.1128/mcb.8.11.4675-4684.1988;
RA   Cross F.R.;
RT   "DAF1, a mutant gene affecting size control, pheromone arrest, and cell
RT   cycle kinetics of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 8:4675-4684(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [4]
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   [5]
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).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition. CLN3 may be an upstream activator of the G1 cyclins
CC       which directly catalyze start.
CC   -!- INTERACTION:
CC       P13365; P00546: CDC28; NbExp=6; IntAct=EBI-4490, EBI-4253;
CC       P13365; P09959: SWI6; NbExp=2; IntAct=EBI-4490, EBI-18641;
CC   -!- INDUCTION: Not significantly cell cycle regulated.
CC   -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR   EMBL; X13964; CAA32143.1; -; Genomic_DNA.
DR   EMBL; M23359; AAA34552.1; -; Genomic_DNA.
DR   EMBL; M23359; AAA34551.1; ALT_TERM; Genomic_DNA.
DR   EMBL; U12980; AAC04991.1; -; Genomic_DNA.
DR   EMBL; AY723756; AAU09673.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06946.1; -; Genomic_DNA.
DR   PIR; S14054; S14054.
DR   RefSeq; NP_009360.1; NM_001178185.1.
DR   AlphaFoldDB; P13365; -.
DR   SMR; P13365; -.
DR   BioGRID; 31725; 288.
DR   ComplexPortal; CPX-1700; CLN3-CDC28 kinase complex.
DR   DIP; DIP-1267N; -.
DR   IntAct; P13365; 15.
DR   MINT; P13365; -.
DR   STRING; 4932.YAL040C; -.
DR   iPTMnet; P13365; -.
DR   PaxDb; P13365; -.
DR   PRIDE; P13365; -.
DR   EnsemblFungi; YAL040C_mRNA; YAL040C; YAL040C.
DR   GeneID; 851191; -.
DR   KEGG; sce:YAL040C; -.
DR   SGD; S000000038; CLN3.
DR   VEuPathDB; FungiDB:YAL040C; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_033561_1_0_1; -.
DR   InParanoid; P13365; -.
DR   OMA; FIMYCHT; -.
DR   BioCyc; YEAST:G3O-28848-MON; -.
DR   Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR   Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR   Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR   Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-SCE-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P13365; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P13365; protein.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IC:ComplexPortal.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:SGD.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR   GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR028857; CCNF_metazoan.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF252; PTHR10177:SF252; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Reference proteome.
FT   CHAIN           1..580
FT                   /note="G1/S-specific cyclin CLN3"
FT                   /id="PRO_0000080413"
FT   REGION          454..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        23
FT                   /note="S -> P (in Ref. 5; AAU09673)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  64991 MW;  AF6950A7E68DB295 CRC64;
     MAILKDTIIR YANARYATAS GTSTATAASV SAASCPNLPL LLQKRRAIAS AKSKNPNLVK
     RELQAHHSAI SEYNNDQLDH YFRLSHTERP LYNLTNFNSQ PQVNPKMRFL IFDFIMYCHT
     RLNLSTSTLF LTFTILDKYS SRFIIKSYNY QLLSLTALWI SSKFWDSKNR MATLKVLQNL
     CCNQYSIKQF TTMEMHLFKS LDWSICQSAT FDSYIDIFLF QSTSPLSPGV VLSAPLEAFI
     QQKLALLNNA AGTAINKSSS SQGPSLNINE IKLGAIMLCE LASFNLELSF KYDRSLIALG
     AINLIKLSLN YYNSNLWENI NLALEENCQD LDIKLSEISN TLLDIAMDQN SFPSSFKSKY
     LNSNKTSLAK SLLDALQNYC IQLKLEEFYR SQELETMYNT IFAQSFDSDS LTCVYSNATT
     PKSATVSSAA TDYFSDHTHL RRLTKDSISP PFAFTPTSSS SSPSPFNSPY KTSSSMTTPD
     SASHHSHSGS FSSTQNSFKR SLSIPQNSSI FWPSPLTPTT PSLMSNRKLL QNLSVRSKRL
     FPVRPMATAH PCSAPTQLKK RSTSSVDCDF NDSSNLKKTR
 
 
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