CDC10_SCHPO
ID CDC10_SCHPO Reviewed; 767 AA.
AC P01129; Q9UU04;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 184.
DE RecName: Full=Start control protein cdc10;
GN Name=cdc10; ORFNames=SPBC336.12c;
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].
RX PubMed=4018034; DOI=10.1002/j.1460-2075.1985.tb03651.x;
RA Aves S.J., Durkacz B.W., Carr A., Nurse P.;
RT "Cloning, sequencing and transcriptional control of the Schizosaccharomyces
RT pombe cdc10 'start' gene.";
RL EMBO J. 4:457-463(1985).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 76-310, 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 [4]
RP FUNCTION.
RX PubMed=8532516; DOI=10.1093/nar/23.23.4761;
RA McInerny C.J., Kersey P.J., Creanor J., Fantes P.A.;
RT "Positive and negative roles for cdc10 in cell cycle gene expression.";
RL Nucleic Acids Res. 23:4761-4768(1995).
RN [5]
RP FUNCTION, AND INTERACTION WITH POL5.
RX PubMed=16816948; DOI=10.1007/s00438-006-0144-6;
RA Nadeem F.K., Blair D., McInerny C.J.;
RT "Pol5p, a novel binding partner to Cdc10p in fission yeast involved in rRNA
RT production.";
RL Mol. Genet. Genomics 276:391-401(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, 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: Major component of the cell cycle transcription factor
CC complex MBF (MCB binding factor, also known as DSC1), that controls G1-
CC S phase specific gene expression. Involved in the control of rRNA
CC production, via interaction with pol5. May be involved in the
CC transcriptional regulation of the cdc22 and cdt1 genes. In fission
CC yeast, two genes, cdc10 and cdc2, are required for the cell cycle
CC control called start, the point early in the G1 phase at which cells
CC become committed to the mitotic cycle. {ECO:0000269|PubMed:16816948,
CC ECO:0000269|PubMed:8532516}.
CC -!- SUBUNIT: DSC1 contains cdc10 and sct1/res1. Interacts with pol5.
CC {ECO:0000269|PubMed:16816948}.
CC -!- INTERACTION:
CC P01129; O60094: pol5; NbExp=2; IntAct=EBI-1009350, EBI-1009362;
CC P01129; P41412: res2; NbExp=3; IntAct=EBI-1009350, EBI-1149177;
CC P01129; P40923: yox1; NbExp=4; IntAct=EBI-1009350, EBI-8530485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630,
CC ECO:0000269|PubMed:10759889}.
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DR EMBL; X02175; CAA26116.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB58164.1; -; Genomic_DNA.
DR EMBL; AB027889; BAA87193.1; -; Genomic_DNA.
DR PIR; A01382; COZPCD.
DR RefSeq; NP_596132.1; NM_001022050.2.
DR AlphaFoldDB; P01129; -.
DR SMR; P01129; -.
DR BioGRID; 276766; 71.
DR DIP; DIP-353N; -.
DR IntAct; P01129; 5.
DR MINT; P01129; -.
DR STRING; 4896.SPBC336.12c.1; -.
DR iPTMnet; P01129; -.
DR MaxQB; P01129; -.
DR PaxDb; P01129; -.
DR PRIDE; P01129; -.
DR EnsemblFungi; SPBC336.12c.1; SPBC336.12c.1:pep; SPBC336.12c.
DR GeneID; 2540234; -.
DR KEGG; spo:SPBC336.12c; -.
DR PomBase; SPBC336.12c; cdc10.
DR VEuPathDB; FungiDB:SPBC336.12c; -.
DR eggNOG; ENOG502QPWC; Eukaryota.
DR HOGENOM; CLU_009666_1_1_1; -.
DR InParanoid; P01129; -.
DR OMA; WIPYDKA; -.
DR PhylomeDB; P01129; -.
DR PRO; PR:P01129; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0030907; C:MBF transcription complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; EXP:PomBase.
DR GO; GO:0033309; C:SBF transcription complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0009303; P:rRNA transcription; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR Pfam; PF00023; Ank; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..767
FT /note="Start control protein cdc10"
FT /id="PRO_0000067060"
FT DOMAIN 66..173
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REPEAT 356..385
FT /note="ANK 1"
FT REPEAT 483..512
FT /note="ANK 2"
FT DNA_BIND 98..119
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..264
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 767 AA; 85513 MW; 0E514EE1BE218EFA CRC64;
MASANFIRQF ELGNDSFSYQ KRPEDEPSQP LSNRNINKLN DSSTLKDSSS RIFINSQVLR
DGRPVELYAV ECSGMKYMEL SCGDNVALRR CPDSYFNISQ ILRLAGTSSS ENAKELDDII
ESGDYENVDS KHPQIDGVWV PYDRAISIAK RYGVYEILQP LISFNLDLFP KFSKQQQIES
SSISKNLNTS SFNTRSPLRN HNFSNPSKSS KNGVHTINNM QSSPSPSSSF LLPLTQIDSQ
NVKRSNNYLS TSPPILEQRL KRHRIDVSDE DLHPSSQLND NEASSLFPDT PRLNHSLSFV
SLVSSLPPLD QNIMQDYHTS KDILTSIFLD VNFADSSALE AKLSDSLDLD VPIDELGHAA
LHWAAAVAKM PLLQALIHKG ANPLRGNLTG ETALMRSVLV TNHLNQNSFG DLLDLLYASL
PCTDRAGRTV VHHICLTAGI KGRGSASRYY LETLLNWAKK HASGNNGYML KDFINYLNHQ
DKNGDTALNI AARIGNKNIV EVLMQAGASA YIPNRAGLSV ANFGIFVENA LKQPEDSKQT
KVSLMSENLS SKEKTAVPPR QKSRDIIASV TDVISSLDKD FQDEMAAKQS MIDSAYTQLR
ESTKKLSDLR EQLHVSETQR TLFLELRQRC KNLMTSIEEQ KSELSNLYES FDPNGIHDSL
SLDADAPFTV NENNNKNLSI AELKFQVAAY ERNEARLNEL ANKLWQRNSN IKSKCRRVVS
LCTGVDESRV DSLLESLLQA VESDGQQGEV DMGRVAGFLR VVKEHQA
