CG22_SCHPO
ID CG22_SCHPO Reviewed; 411 AA.
AC P36630;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=G2/mitotic-specific cyclin cig2;
GN Name=cig2; Synonyms=cyc17; ORFNames=SPAPB2B4.03;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CDC2.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8455610; DOI=10.1128/mcb.13.4.2286-2297.1993;
RA Bueno A., Russell P.;
RT "Two fission yeast B-type cyclins, cig2 and Cdc13, have different functions
RT in mitosis.";
RL Mol. Cell. Biol. 13:2286-2297(1993).
RN [2]
RP ERRATUM OF PUBMED:8455610.
RA Bueno A., Russell P.;
RL Mol. Cell. Biol. 14:869-869(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RX PubMed=7909513; DOI=10.1002/j.1460-2075.1994.tb06455.x;
RA Obara-Ishihara T., Okayama H.;
RT "A B-type cyclin negatively regulates conjugation via interacting with cell
RT cycle 'start' genes in fission yeast.";
RL EMBO J. 13:1863-1872(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8264644; DOI=10.1128/mcb.14.1.768-776.1994;
RA Connolly T., Beach D.;
RT "Interaction between the Cig1 and Cig2 B-type cyclins in the fission yeast
RT cell cycle.";
RL Mol. Cell. Biol. 14:768-776(1994).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=8657126; DOI=10.1128/mcb.16.4.1527;
RA Mondesert O., McGowan C.H., Russell P.;
RT "Cig2, a B-type cyclin, promotes the onset of S in Schizosaccharomyces
RT pombe.";
RL Mol. Cell. Biol. 16:1527-1533(1996).
RN [7]
RP REVIEW ON ASSOCIATION WITH CDC2.
RX PubMed=8855663; DOI=10.1016/s0168-9525(96)80016-3;
RA Stern B., Nurse P.;
RT "A quantitative model for the cdc2 control of S phase and mitosis in
RT fission yeast.";
RL Trends Genet. 12:345-350(1996).
RN [8]
RP INTERACTION WITH RUM1.
RX PubMed=9614176; DOI=10.1091/mbc.9.6.1309;
RA Stern B., Nurse P.;
RT "Cyclin B proteolysis and the cyclin-dependent kinase inhibitor rum1p are
RT required for pheromone-induced G1 arrest in fission yeast.";
RL Mol. Biol. Cell 9:1309-1321(1998).
RN [9]
RP FUNCTION, INTERACTION WITH CDC2, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP DESTRUCTION BOX MOTIF, AND MUTAGENESIS OF ARG-51; LEU-54; ARG-169; GLU-170;
RP ILE-171; SER-268 AND THR-329.
RX PubMed=11163211; DOI=10.1016/s1097-2765(00)00135-0;
RA Yamano H., Kitamura K., Kominami K., Lehmann A., Hunt T., Toda T.;
RT "The spike of S phase cyclin Cig2 expression at the G1-S border in fission
RT yeast requires both APC and SCF ubiquitin ligases.";
RL Mol. Cell 6:1377-1387(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH RES2.
RX PubMed=11781565; DOI=10.1038/ncb1201-1043;
RA Ayte J., Schweitzer C., Zarzov P., Nurse P., DeCaprio J.A.;
RT "Feedback regulation of the MBF transcription factor by cyclin Cig2.";
RL Nat. Cell Biol. 3:1043-1050(2001).
RN [11]
RP FUNCTION, AND INTERACTION WITH POP1.
RX PubMed=14970237; DOI=10.1074/jbc.m311060200;
RA Yamano H., Kominami K., Harrison C., Kitamura K., Katayama S., Dhut S.,
RA Hunt T., Toda T.;
RT "Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the
RT fission yeast S phase cyclin Cig2.";
RL J. Biol. Chem. 279:18974-18980(2004).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M and
CC G1/S (mitosis) transition. Interacts with the cdc2 protein kinase to
CC form MPF. Interaction with res2 promotes the phosphorylation of res1
CC and inhibits MBF-dependent gene transcription. Forms an autoregulating
CC feedback-inhibition loop with MBF which is important for normal
CC regulation of the cell cycle. G2/M cyclins accumulate steadily during
CC G2 and are abruptly destroyed at mitosis. Negatively regulates
CC conjugation via interacting with cell cycle 'start' genes. Degraded by
CC skp1, pop1 and pop2 in the G2 and M phases of the cell cycle.
CC {ECO:0000269|PubMed:11163211, ECO:0000269|PubMed:11781565,
CC ECO:0000269|PubMed:14970237, ECO:0000269|PubMed:7909513,
CC ECO:0000269|PubMed:8264644, ECO:0000269|PubMed:8455610,
CC ECO:0000269|PubMed:8657126}.
CC -!- SUBUNIT: Associates with cdc2, res2 and rum1. Interacts with pop1 only
CC when phosphorylated. {ECO:0000269|PubMed:11163211,
CC ECO:0000269|PubMed:11781565, ECO:0000269|PubMed:14970237,
CC ECO:0000269|PubMed:8455610, ECO:0000269|PubMed:9614176}.
CC -!- INTERACTION:
CC P36630; P87060: pop1; NbExp=4; IntAct=EBI-1149212, EBI-1185389;
CC P36630; P33520: res1; NbExp=3; IntAct=EBI-1149212, EBI-1149288;
CC P36630; P41412: res2; NbExp=3; IntAct=EBI-1149212, EBI-1149177;
CC P36630; P40380: rum1; NbExp=2; IntAct=EBI-1149212, EBI-1187892;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body.
CC -!- INDUCTION: Highly induced upon nitrogen starvation and during
CC conjugation. {ECO:0000269|PubMed:7909513}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11163211}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X70046; CAA49640.1; -; mRNA.
DR EMBL; D28751; BAA05943.1; -; mRNA.
DR EMBL; S67490; AAB29297.2; ALT_SEQ; mRNA.
DR EMBL; CU329670; CAC21469.1; -; Genomic_DNA.
DR PIR; A48100; A48100.
DR PIR; S44344; S44344.
DR PIR; T52009; T52009.
DR RefSeq; NP_593889.1; NM_001019319.2.
DR AlphaFoldDB; P36630; -.
DR SMR; P36630; -.
DR BioGRID; 279901; 40.
DR IntAct; P36630; 5.
DR STRING; 4896.SPAPB2B4.03.1; -.
DR iPTMnet; P36630; -.
DR MaxQB; P36630; -.
DR PaxDb; P36630; -.
DR PRIDE; P36630; -.
DR EnsemblFungi; SPAPB2B4.03.1; SPAPB2B4.03.1:pep; SPAPB2B4.03.
DR GeneID; 2543481; -.
DR KEGG; spo:SPAPB2B4.03; -.
DR PomBase; SPAPB2B4.03; cig2.
DR VEuPathDB; FungiDB:SPAPB2B4.03; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_2_0_1; -.
DR InParanoid; P36630; -.
DR OMA; IQNFVYM; -.
DR PhylomeDB; P36630; -.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SPO-69231; Cyclin D associated events in G1.
DR Reactome; R-SPO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P36630; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; EXP:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IDA: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:0000082; P:G1/S transition of mitotic cell cycle; 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:0031568; P:mitotic G1 cell size control checkpoint signaling; IGI:PomBase.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0110044; P:regulation of cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IGI: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 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; Conjugation; Cyclin; Cytoplasm; Cytoskeleton;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..411
FT /note="G2/mitotic-specific cyclin cig2"
FT /id="PRO_0000080401"
FT DOMAIN 139..265
FT /note="Cyclin N-terminal"
FT REGION 57..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..273
FT /note="Interaction with pop1"
FT MOTIF 51..60
FT /note="Destruction box"
FT COMPBIAS 62..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 51
FT /note="R->A: Improves protein stability; when associated
FT with A-54."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 54
FT /note="L->A: Improves protein stability; when associated
FT with A-51."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 169
FT /note="R->A: Prevents binding to cdc2 and improves protein
FT stability; when associated with A-170 and A-171."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 170
FT /note="E->A: Prevents binding to cdc2 and improves protein
FT stability; when associated with A-169 and A-171."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 171
FT /note="I->A: Prevents binding to cdc2 and improves protein
FT stability; when associated with A-169 and A-170."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 268
FT /note="S->N: No effect on protein stability; when
FT associated with A-329."
FT /evidence="ECO:0000269|PubMed:11163211"
FT MUTAGEN 329
FT /note="T->A: No effect on protein stability; when
FT associated with N-268."
FT /evidence="ECO:0000269|PubMed:11163211"
FT CONFLICT 1..49
FT /note="MALYSISKPVGSKINKHSYQDENTLVGKQALSKGTEKTKLSTNFEINLP ->
FT MKTHLLANKLYQKGLRRQNYLQICKLICHA (in Ref. 1; CAA49640)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..124
FT /note="VSNVDD -> ALMLMN (in Ref. 1; CAA49640)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="Missing (in Ref. 1; CAA49640)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="P -> A (in Ref. 1; CAA49640)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="H -> QRTLL (in Ref. 1; CAA49640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 47477 MW; 6F255D2E26C6F8B3 CRC64;
MALYSISKPV GSKINKHSYQ DENTLVGKQA LSKGTEKTKL STNFEINLPR RTVLSDVSNV
GKNNADEKDT KKAKRSFDES NLSTNEEADK PVESKFVKKL KVYSKNADPS VETLQKDRVS
NVDDHLSSNP LMAEEYAPEI FEYIRKLDLK CLPNPKYMDQ QKELTWKMRE ILNEWLVEIH
SNFCLMPETL YLAVNIIDRF LSRRSCSLSK FQLTGITALL IASKYEEVMC PSIQNFVYMT
DGAFTVEDVC VAERYMLNVL NFDLSYPSPL NFLRKISQAE GYDAQTRTLG KYLTEIYLFD
HDLLRYPMSK IAAAAMYLSR RLLRRGPWTP KLVESSGGYE EHELKEIAYI MLHYHNKPLE
HKAFFQKYSS KRFLKASIFV HQLVRQRYSV NRTDDDDLQS EPSSSLTNDG H
