CG1C_SCHPO
ID CG1C_SCHPO Reviewed; 342 AA.
AC O74627; P87075;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cyclin pch1;
DE AltName: Full=Pombe cyclin C homolog 1;
GN Name=pch1; ORFNames=SPBC32F12.06;
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 INTERACTION WITH CDC2.
RX PubMed=9115279; DOI=10.1074/jbc.272.18.12100;
RA Furnari B.A., Russell P., Leatherwood J.;
RT "pch1(+), a second essential C-type cyclin gene in Schizosaccharomyces
RT pombe.";
RL J. Biol. Chem. 272:12100-12106(1997).
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 CDK9.
RX PubMed=12475973; DOI=10.1074/jbc.m211713200;
RA Pei Y., Schwer B., Shuman S.;
RT "Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA
RT capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality
RT control.";
RL J. Biol. Chem. 278:7180-7188(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-300 AND SER-302, AND
RP IDENTIFICATION BY 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 whole cell cycle.
CC {ECO:0000269|PubMed:9115279}.
CC -!- SUBUNIT: Interacts with cdc2 protein kinase and with the N-terminal
CC domain of cdk9. {ECO:0000269|PubMed:12475973,
CC ECO:0000269|PubMed:9115279}.
CC -!- INTERACTION:
CC O74627; P04551: cdc2; NbExp=2; IntAct=EBI-443575, EBI-1187862;
CC O74627; Q96WV9: cdk9; NbExp=2; IntAct=EBI-443575, EBI-443557;
CC O74627; O74880: pcm1; NbExp=2; IntAct=EBI-443575, EBI-7296037;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; U92879; AAB53219.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19367.1; -; Genomic_DNA.
DR PIR; T40230; T40230.
DR RefSeq; NP_596149.1; NM_001022068.2.
DR AlphaFoldDB; O74627; -.
DR SMR; O74627; -.
DR BioGRID; 276769; 10.
DR IntAct; O74627; 3.
DR MINT; O74627; -.
DR STRING; 4896.SPBC32F12.06.1; -.
DR iPTMnet; O74627; -.
DR MaxQB; O74627; -.
DR PaxDb; O74627; -.
DR PRIDE; O74627; -.
DR EnsemblFungi; SPBC32F12.06.1; SPBC32F12.06.1:pep; SPBC32F12.06.
DR PomBase; SPBC32F12.06; pch1.
DR VEuPathDB; FungiDB:SPBC32F12.06; -.
DR eggNOG; KOG0834; Eukaryota.
DR HOGENOM; CLU_022000_7_0_1; -.
DR InParanoid; O74627; -.
DR OMA; YQIAATA; -.
DR PhylomeDB; O74627; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O74627; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:PomBase.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070691; C:P-TEFb complex; IPI:PomBase.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; EXP:PomBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..342
FT /note="Cyclin pch1"
FT /id="PRO_0000080426"
FT REGION 261..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 157
FT /note="V -> G (in Ref. 1; AAB53219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38286 MW; 751C28BAE0EA18AC CRC64;
MSEVIKSVPP GSQNTSQWII SKDQLVFTPS ALDGIPLDQE EIQRSKGCNF IINVGLRLKL
PQTALATANI YFHRFYLRFS LKNYHYYEVA ATCIFLATKV EDSVRKLRDI VINCAKVAQK
NSNVLVDEQT KEYWRWRDVI LYTEEVLLEA LCFDFTVEHP YPYVLSFIKK FVADDKNVTK
VAWTYINDST RSIACLLYSP KTIAAAAFQF ALEKNEINLS TTTDGLPVWM EESQVSYEDV
KGVLTLIDSL YKKINPSKQA LPIDQKNGSH ASSVAPGTPS SLASVSTQAT PQHQNSSGRT
DSFHSLNTET PSKSTVDDQI LSTAAQPKKS SDTDKEMETE AS
