ID CGM2_SCHPO Reviewed; 322 AA.
AC P36613;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 27-MAR-2024, entry version 177.
DE RecName: Full=Cyclin mcs2;
DE AltName: Full=Mitotic catastrophe suppressor 2;
GN Name=mcs2; ORFNames=SPBP16F5.02;
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 SUBCELLULAR LOCATION.
RX PubMed=8467814; DOI=10.1002/j.1460-2075.1993.tb05817.x;
RA Molz L., Beach D.;
RT "Characterization of the fission yeast mcs2 cyclin and its associated
RT protein kinase activity.";
RL EMBO J. 12:1723-1732(1993).
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 INTERACTION WITH CRK1/MCS6.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8557037; DOI=10.1002/j.1460-2075.1995.tb00308.x;
RA Buck V., Russell P., Millar J.B.A.;
RT "Identification of a cdk-activating kinase in fission yeast.";
RL EMBO J. 14:6173-6183(1995).
RN [4]
RP INTERACTION WITH CRK1/MCS6.
RX PubMed=8557036; DOI=10.1002/j.1460-2075.1995.tb00307.x;
RA Damagnez V., Makela T.P., Cottarel G.;
RT "Schizosaccharomyces pombe Mop1-Mcs2 is related to mammalian CAK.";
RL EMBO J. 14:6164-6172(1995).
RN [5]
RP SUBUNIT.
RX PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT transcription in vitro.";
RL J. Biol. Chem. 278:51301-51306(2003).
RN [6]
RP INTERACTION WITH SKP1 AND CRK1/MCS6.
RC STRAIN=972 / ATCC 24843;
RX PubMed=15555586; DOI=10.1016/j.bbrc.2004.10.190;
RA Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J.,
RA Maekelae T.P., Hermand D.;
RT "Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast.";
RL Biochem. Biophys. Res. Commun. 325:1424-1432(2004).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, 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: Essential for progression through the cell cycle. Posseses
CC kinase activity that can be detected when myelin basic protein (MBP) is
CC provided as an exogenous substrate. {ECO:0000269|PubMed:8467814}.
CC -!- SUBUNIT: One of the nine subunits forming the core-TFIIH basal
CC transcription factor. Interacts with crk1 and skp1.
CC {ECO:0000269|PubMed:14534314, ECO:0000269|PubMed:15555586,
CC ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037}.
CC -!- INTERACTION:
CC P36613; Q9Y709: skp1; NbExp=3; IntAct=EBI-1168694, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:8467814}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; S59895; AAB26193.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC08541.1; -; Genomic_DNA.
DR PIR; S35380; S35380.
DR RefSeq; NP_595776.1; NM_001021676.2.
DR AlphaFoldDB; P36613; -.
DR SMR; P36613; -.
DR BioGRID; 277082; 170.
DR IntAct; P36613; 3.
DR STRING; 284812.P36613; -.
DR iPTMnet; P36613; -.
DR MaxQB; P36613; -.
DR PaxDb; 4896-SPBP16F5-02-1; -.
DR EnsemblFungi; SPBP16F5.02.1; SPBP16F5.02.1:pep; SPBP16F5.02.
DR GeneID; 2540555; -.
DR KEGG; spo:SPBP16F5.02; -.
DR PomBase; SPBP16F5.02; mcs2.
DR VEuPathDB; FungiDB:SPBP16F5.02; -.
DR eggNOG; KOG2496; Eukaryota.
DR HOGENOM; CLU_022620_4_0_1; -.
DR InParanoid; P36613; -.
DR OMA; KTTNHPI; -.
DR PhylomeDB; P36613; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
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-72086; mRNA Capping.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P36613; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA: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:0043539; F:protein serine/threonine kinase activator activity; EXP:PomBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; EXP:PomBase.
DR CDD; cd20524; CYCLIN_CCNH_rpt1; 1.
DR CDD; cd20525; CYCLIN_CCNH_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR027081; CyclinH/Ccl1.
DR NCBIfam; TIGR00569; ccl1; 1.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF8; CYCLIN-H; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..322
FT /note="Cyclin mcs2"
FT /id="PRO_0000080505"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 322 AA; 37674 MW; 09B8DDB46563727C CRC64;
MSADKFRDST HYRDWIFTEE DLSKTRAKVN EKFTNIVRER MLEELSLQNK EASLEVLPPT
LTVEEELELV NYYSFQLNAL SSALSLPTHI RSTAILFFKR FYLINSVMEY SPKIISFTSL
FLATKCNDHY ISIEQFCKNM PKTTPEEVLE YEFNVCQSLK WDLYVWLPFR PLQGFLLDCQ
TVLPKVAVEK FYECHDLSKK FLIETLHSDI YFLHSPSIIA LGAIYHTNPT ICLQYIEAKK
IPELQPLIIS ISANLKATKK FKIEKKKAQD YGRKLYFCMN PLRNKSSALY LKRKAEEEST
NNNKWAKKFS TSSNVLDKNP FE
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