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CGS5_YEAST
ID   CGS5_YEAST              Reviewed;         435 AA.
AC   P30283; D6W4B9;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=S-phase entry cyclin-5;
GN   Name=CLB5; OrderedLocusNames=YPR120C; ORFNames=P9642.8;
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=BF264-15D;
RX   PubMed=1387626; DOI=10.1101/gad.6.9.1695;
RA   Epstein C.B., Cross F.R.;
RT   "CLB5: a novel B cyclin from budding yeast with a role in S phase.";
RL   Genes Dev. 6:1695-1706(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204510 / AB320;
RX   PubMed=8319908; DOI=10.1101/gad.7.7a.1160;
RA   Schwob E., Nasmyth K.;
RT   "CLB5 and CLB6, a new pair of B cyclins involved in DNA replication in
RT   Saccharomyces cerevisiae.";
RL   Genes Dev. 7:1160-1175(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8253070; DOI=10.1002/j.1460-2075.1993.tb06018.x;
RA   Kuehne C., Linder P.;
RT   "A new pair of B-type cyclins from Saccharomyces cerevisiae that function
RT   early in the cell cycle.";
RL   EMBO J. 12:3437-3447(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [5]
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   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Required for efficient progression through S phase and
CC       possibly for the normal progression through meiosis. Interacts with
CC       CDC28.
CC   -!- INTERACTION:
CC       P30283; P00546: CDC28; NbExp=5; IntAct=EBI-4538, EBI-4253;
CC   -!- DEVELOPMENTAL STAGE: Maximally expressed just before cell cycle start.
CC   -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M91209; AAA34503.1; -; Genomic_DNA.
DR   EMBL; X70435; CAA49893.1; -; Genomic_DNA.
DR   EMBL; U40828; AAB68061.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11535.1; -; Genomic_DNA.
DR   PIR; S31290; S31290.
DR   RefSeq; NP_015445.1; NM_001184217.1.
DR   AlphaFoldDB; P30283; -.
DR   SMR; P30283; -.
DR   BioGRID; 36288; 323.
DR   ComplexPortal; CPX-1702; CLB5-CDC28 kinase complex.
DR   DIP; DIP-2710N; -.
DR   ELM; P30283; -.
DR   IntAct; P30283; 24.
DR   MINT; P30283; -.
DR   STRING; 4932.YPR120C; -.
DR   iPTMnet; P30283; -.
DR   PaxDb; P30283; -.
DR   PRIDE; P30283; -.
DR   EnsemblFungi; YPR120C_mRNA; YPR120C; YPR120C.
DR   GeneID; 856237; -.
DR   KEGG; sce:YPR120C; -.
DR   SGD; S000006324; CLB5.
DR   VEuPathDB; FungiDB:YPR120C; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   GeneTree; ENSGT00940000176489; -.
DR   HOGENOM; CLU_020695_12_4_1; -.
DR   InParanoid; P30283; -.
DR   OMA; MCCPKFV; -.
DR   BioCyc; YEAST:G3O-34259-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:P30283; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P30283; 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:0006974; P:cellular response to DNA damage stimulus; IDA:ComplexPortal.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IMP:SGD.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IGI:SGD.
DR   GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IGI:SGD.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:ComplexPortal.
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   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 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; Reference proteome.
FT   CHAIN           1..435
FT                   /note="S-phase entry cyclin-5"
FT                   /id="PRO_0000080408"
FT   REGION          36..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  50431 MW;  5AD67EB841BA5759 CRC64;
     MGENHDHEQS IKRNSMIYNE NERQLCNSNL KILQNKRALS KNDSSSKQQV QDSKPRRALT
     DVPVNNNPLS QNKRIVAGSK AAKVRREENI RPIVSAVQKR QIYNDRTAAE QEEEEEEEGE
     DDDAASIVNK KRRIDAEGVS EIVGWQDLDY VEKDDTAMVA EYSAEIFAFL YRRELETLPS
     HNYLLDKTSK YYLRPSMRTI LVDWLVEVHE KFQCYPETLF LSINLMDRFL AKNKVTMNKL
     QLLAVTSLFI AAKFEEVNLP KLAEYAYITD GAASKNDIKN AEMFMLTSLE FNIGWPNPLN
     FLRRISKADD YDPVNRNIGK FILEYAYCCH QFIHLPPSTV SAMAMYIARR MTNRNKNELW
     NGTLQHYSGG IDPIHDEAFQ SLCIDLVKDI ASSKTHLDSL ILKYKKPRYG SVYFQTFKWC
     TSEMHSNFQN LFNLK
 
 
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