CG23_SCHPO
ID CG23_SCHPO Reviewed; 482 AA.
AC P10815; Q9UU16;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=G2/mitotic-specific cyclin cdc13 {ECO:0000303|PubMed:2847913};
GN Name=cdc13 {ECO:0000303|PubMed:2847913};
GN ORFNames=SPBC582.03 {ECO:0000312|PomBase:SPBC582.03};
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 [GENOMIC DNA], FUNCTION, AND ASSOCIATION WITH
RP MICROTUBULES.
RX PubMed=2847913; DOI=10.1002/j.1460-2075.1988.tb03075.x;
RA Booher R., Beach D.;
RT "Involvement of cdc13+ in mitotic control in Schizosaccharomyces pombe:
RT possible interaction of the gene product with microtubules.";
RL EMBO J. 7:2321-2327(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2908246; DOI=10.1242/jcs.91.4.587;
RA Hagan I., Hayles J., Nurse P.;
RT "Cloning and sequencing of the cyclin-related cdc13+ gene and a cytological
RT study of its role in fission yeast mitosis.";
RL J. Cell Sci. 91:587-595(1988).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 22-226, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [5]
RP SIMILARITY TO THE CYCLIN FAMILY.
RX PubMed=2900688; DOI=10.1016/s0092-8674(88)90933-6;
RA Solomon M., Booher R., Kirschner M., Beach B.;
RT "Cyclin in fission yeast.";
RL Cell 54:738-739(1988).
RN [6]
RP SIMILARITY TO THE CYCLIN FAMILY.
RA Goebl M., Bryers B.;
RT "Cyclin in fission yeast.";
RL Cell 54:739-740(1988).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2534559; DOI=10.1242/jcs.1989.supplement_12.2;
RA Alfa C.E., Booher R., Beach D., Hyams J.S.;
RT "Fission yeast cyclin: subcellular localisation and cell cycle
RT regulation.";
RL J. Cell Sci. Suppl. 12:9-19(1989).
RN [8]
RP 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 [9]
RP FUNCTION.
RX PubMed=7498766; DOI=10.1093/genetics/140.4.1235;
RA Iino Y., Hiramine Y., Yamamoto M.;
RT "The role of cdc2 and other genes in meiosis in Schizosaccharomyces
RT pombe.";
RL Genetics 140:1235-1245(1995).
RN [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH RUM1.
RX PubMed=9303310; DOI=10.1093/emboj/16.15.4657;
RA Correa-Bordes J., Gulli M.P., Nurse P.;
RT "p25rum1 promotes proteolysis of the mitotic B-cyclin p56cdc13 during G1 of
RT the fission yeast cell cycle.";
RL EMBO J. 16:4657-4664(1997).
RN [12]
RP INTERACTION WITH RUM1.
RX PubMed=9472012; DOI=10.1242/jcs.111.6.843;
RA Sanchez-Diaz A., Gonzalez I., Arellano M., Moreno S.;
RT "The Cdk inhibitors p25rum1 and p40SIC1 are functional homologues that play
RT similar roles in the regulation of the cell cycle in fission and budding
RT yeast.";
RL J. Cell Sci. 111:843-851(1998).
RN [13]
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 [14]
RP INTERACTION WITH CDC11.
RX PubMed=15062098; DOI=10.1016/j.cub.2004.03.036;
RA Morrell J.L., Tomlin G.C., Rajagopalan S., Venkatram S., Feoktistova A.S.,
RA Tasto J.J., Mehta S., Jennings J.L., Link A., Balasubramanian M.K.,
RA Gould K.L.;
RT "Sid4p-Cdc11p assembles the septation initiation network and its regulators
RT at the S. pombe SPB.";
RL Curr. Biol. 14:579-584(2004).
RN [15]
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
CC (mitosis) transition (PubMed:2847913, PubMed:2908246). Interacts with
CC the cdc2 protein kinase to form MPF (PubMed:8455610). G2/M cyclins
CC accumulate steadily during G2 and are abruptly destroyed at mitosis
CC (PubMed:2534559). Involved in the reorganization of the cytoskeleton on
CC transition from G2 to mitosis (PubMed:2908246). Association with rum1
CC promotes its proteolysis during G1 (PubMed:9303310). Also essential for
CC initiation of meiosis II (PubMed:7498766). {ECO:0000269|PubMed:2534559,
CC ECO:0000269|PubMed:2847913, ECO:0000269|PubMed:2908246,
CC ECO:0000269|PubMed:7498766, ECO:0000269|PubMed:8455610,
CC ECO:0000269|PubMed:9303310}.
CC -!- SUBUNIT: Interacts with cdc2 (PubMed:8455610). Interacts with rum1
CC (PubMed:9303310, PubMed:9472012, PubMed:9614176). Associates with
CC microtubules (PubMed:2847913). Also interacts with cdc11
CC (PubMed:15062098). {ECO:0000269|PubMed:15062098,
CC ECO:0000269|PubMed:2847913, ECO:0000269|PubMed:8455610,
CC ECO:0000269|PubMed:9303310, ECO:0000269|PubMed:9472012,
CC ECO:0000269|PubMed:9614176}.
CC -!- INTERACTION:
CC P10815; P40380: rum1; NbExp=5; IntAct=EBI-1187843, EBI-1187892;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:2534559}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X12557; CAA31070.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB46666.1; -; Genomic_DNA.
DR EMBL; AB027869; BAA87173.1; -; Genomic_DNA.
DR PIR; A34948; A34948.
DR PIR; S01153; S01153.
DR RefSeq; NP_595171.1; NM_001021079.2.
DR AlphaFoldDB; P10815; -.
DR SMR; P10815; -.
DR BioGRID; 277397; 59.
DR DIP; DIP-620N; -.
DR IntAct; P10815; 15.
DR STRING; 4896.SPBC582.03.1; -.
DR iPTMnet; P10815; -.
DR MaxQB; P10815; -.
DR PaxDb; P10815; -.
DR EnsemblFungi; SPBC582.03.1; SPBC582.03.1:pep; SPBC582.03.
DR PomBase; SPBC582.03; cdc13.
DR VEuPathDB; FungiDB:SPBC582.03; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_10_6_1; -.
DR InParanoid; P10815; -.
DR OMA; EDWADPL; -.
DR PhylomeDB; P10815; -.
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:P10815; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; EXP:PomBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; EXP:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IMP: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:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0140013; P:meiotic nuclear division; IMP:PomBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0075297; P:negative regulation of ascospore formation; IMP:PomBase.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:PomBase.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IGI:PomBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0007165; P:signal transduction; NAS: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; Cyclin; Cytoplasm; Cytoskeleton; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..482
FT /note="G2/mitotic-specific cyclin cdc13"
FT /id="PRO_0000080402"
FT DOMAIN 206..332
FT /note="Cyclin N-terminal"
FT REGION 35..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 479
FT /note="D -> H (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 55609 MW; B2C267CF57F5FD36 CRC64;
MTTRRLTRQH LLANTLGNND ENHPSNHIAR AKSSLHSSEN SLVNGKKATV SSTNVPKKRH
ALDDVSNFHN KEGVPLASKN TNVRHTTASV STRRALEEKS IIPATDDEPA SKKRRQPSVF
NSSVPSLPQH LSTKSHSVST HGVDAFHKDQ ATIPKKLKKD VDERVVSKDI PKLHRDSVES
PESQDWDDLD AEDWADPLMV SEYVVDIFEY LNELEIETMP SPTYMDRQKE LAWKMRGILT
DWLIEVHSRF RLLPETLFLA VNIIDRFLSL RVCSLNKLQL VGIAALFIAS KYEEVMCPSV
QNFVYMADGG YDEEEILQAE RYILRVLEFN LAYPNPMNFL RRISKADFYD IQTRTVAKYL
VEIGLLDHKL LPYPPSQQCA AAMYLAREML GRGPWNRNLV HYSGYEEYQL ISVVKKMINY
LQKPVQHEAF FKKYASKKFM KASLFVRDWI KKNSIPLGDD ADEDYTFHKQ KRIQHDMKDE
EW
