RUM1_SCHPO
ID RUM1_SCHPO Reviewed; 230 AA.
AC P40380; O74373;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cyclin-dependent kinase inhibitor rum1;
DE AltName: Full=p25-rum1;
GN Name=rum1; ORFNames=SPBC32F12.09;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8121488; DOI=10.1038/367236a0;
RA Moreno S., Nurse P.;
RT "Regulation of progression through the G1 phase of the cell cycle by the
RT rum1+ gene.";
RL Nature 367:236-242(1994).
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 FUNCTION.
RX PubMed=8521500; DOI=10.1016/0092-8674(95)90215-5;
RA Correa-Bordes J., Nurse P.;
RT "p25rum1 orders S phase and mitosis by acting as an inhibitor of the
RT p34cdc2 mitotic kinase.";
RL Cell 83:1001-1009(1995).
RN [4]
RP FUNCTION, INTERACTION WITH CDC13, AND PHOSPHORYLATION.
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 [5]
RP FUNCTION, PHOSPHORYLATION AT THR-58 AND THR-62, AND MUTAGENESIS OF THR-5;
RP THR-13; THR-16; SER-19; THR-58; THR-62; THR-110 AND SER-212.
RX PubMed=9430640; DOI=10.1093/emboj/17.2.482;
RA Benito J., Martin-Castellanos C., Moreno S.;
RT "Regulation of the G1 phase of the cell cycle by periodic stabilization and
RT degradation of the p25rum1 CDK inhibitor.";
RL EMBO J. 17:482-497(1998).
RN [6]
RP FUNCTION, INTERACTION WITH CDC13, AND DOMAIN.
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 [7]
RP FUNCTION, AND INTERACTION WITH CDC13 AND CIG2.
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 [8]
RP FUNCTION, PHOSPHORYLATION AT THR-13 AND SER-19, AND MUTAGENESIS OF THR-5;
RP THR-13; THR-16; SER-19 AND THR-58.
RX PubMed=12135491; DOI=10.1046/j.1432-1033.2002.03033.x;
RA Matsuoka K., Kiyokawa N., Taguchi T., Matsui J., Suzuki T., Mimori K.,
RA Nakajima H., Takenouchi H., Weiran T., Katagiri Y.U., Fujimoto J.;
RT "Rum1, an inhibitor of cyclin-dependent kinase in fission yeast, is
RT negatively regulated by mitogen-activated protein kinase-mediated
RT phosphorylation at Ser and Thr residues.";
RL Eur. J. Biochem. 269:3511-3521(2002).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=14653990; DOI=10.1016/j.cub.2003.10.061;
RA Daga R.R., Bolanos P., Moreno S.;
RT "Regulated mRNA stability of the Cdk inhibitor Rum1 links nutrient status
RT to cell cycle progression.";
RL Curr. Biol. 13:2015-2024(2003).
RN [10]
RP 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 [11]
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: Regulator of cell cycle G1 phase progression. Ensures the
CC correct sequence of S phase and mitosis in the cell by acting as an
CC inhibitor of the cdc2 mitotic kinase. Probably interacts with cdc2 to
CC inhibit its action until the cell mass for Start is reached. Determines
CC the length of the pre-Start G1 period and prevents mitosis from
CC happening in early G1 cells. Required for maintaining pheromone-induced
CC G1 arrest. Acts as an adapter protein since interaction with cdc13
CC promotes cyclin proteolysis during G1. Becomes a target for degradation
CC at the G1/S phase transition, following phosphorylation by cig1-
CC associated cdc2 at the G1/S phase transition.
CC {ECO:0000269|PubMed:12135491, ECO:0000269|PubMed:14653990,
CC ECO:0000269|PubMed:8121488, ECO:0000269|PubMed:8521500,
CC ECO:0000269|PubMed:9303310, ECO:0000269|PubMed:9430640,
CC ECO:0000269|PubMed:9472012, ECO:0000269|PubMed:9614176}.
CC -!- SUBUNIT: Interacts with cdc13, cig2 and pop1.
CC {ECO:0000269|PubMed:14970237, ECO:0000269|PubMed:9303310,
CC ECO:0000269|PubMed:9472012, ECO:0000269|PubMed:9614176}.
CC -!- INTERACTION:
CC P40380; P10815: cdc13; NbExp=5; IntAct=EBI-1187892, EBI-1187843;
CC P40380; P04551: cdc2; NbExp=2; IntAct=EBI-1187892, EBI-1187862;
CC P40380; P36630: cig2; NbExp=2; IntAct=EBI-1187892, EBI-1149212;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Expression increases in nitrogen deprived environment, which
CC is important to cause delay of the G1 phase of the cell cycle in
CC response to nitrogen starvation. {ECO:0000269|PubMed:14653990}.
CC -!- PTM: Phosphorylated by cig1-associated cdc2 which leads to increased
CC stability. Phosphorylation by MAPK reduces cdc2 kinase inhibitor
CC ability. {ECO:0000269|PubMed:12135491, ECO:0000269|PubMed:9303310,
CC ECO:0000269|PubMed:9430640}.
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DR EMBL; X77730; CAA54786.1; -; mRNA.
DR EMBL; CU329671; CAA19370.1; -; Genomic_DNA.
DR PIR; S41043; S41043.
DR PIR; T40233; T40233.
DR RefSeq; NP_596152.1; NM_001022071.2.
DR AlphaFoldDB; P40380; -.
DR BioGRID; 276195; 34.
DR IntAct; P40380; 5.
DR STRING; 4896.SPBC32F12.09.1; -.
DR iPTMnet; P40380; -.
DR PaxDb; P40380; -.
DR PRIDE; P40380; -.
DR EnsemblFungi; SPBC32F12.09.1; SPBC32F12.09.1:pep; SPBC32F12.09.
DR GeneID; 2539640; -.
DR KEGG; spo:SPBC32F12.09; -.
DR PomBase; SPBC32F12.09; rum1.
DR VEuPathDB; FungiDB:SPBC32F12.09; -.
DR HOGENOM; CLU_1246003_0_0_1; -.
DR OMA; ERCMEED; -.
DR PRO; PR:P40380; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IDA:PomBase.
DR GO; GO:0031568; P:mitotic G1 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:PomBase.
DR GO; GO:1903464; P:negative regulation of mitotic cell cycle DNA replication; IMP:PomBase.
DR GO; GO:1903467; P:negative regulation of mitotic DNA replication initiation; IDA:PomBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; EXP:PomBase.
DR GO; GO:0031647; P:regulation of protein stability; IDA:PomBase.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..230
FT /note="Cyclin-dependent kinase inhibitor rum1"
FT /id="PRO_0000097531"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..147
FT /note="CDK inhibitory and cyclin-binding"
FT REGION 101..230
FT /note="Required for activity as a cdc2 kinase inhibitor"
FT REGION 187..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000269|PubMed:12135491"
FT MOD_RES 19
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:12135491"
FT MOD_RES 58
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:9430640"
FT MOD_RES 62
FT /note="Phosphothreonine; by cdc2"
FT /evidence="ECO:0000269|PubMed:9430640"
FT MUTAGEN 5
FT /note="T->A: No effect on phenotype and no reduction in 32-
FT P incorporation mediated by MAPK."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 13
FT /note="T->A: No effect on phenotype; when associated with
FT A-16 and A-19. Reduced 32-P incorporation mediated by MAPK;
FT when associated with A-19."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 13
FT /note="T->E: Reduces activity as a cdc2 inhibitor; when
FT associated with E-19."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 16
FT /note="T->A: No effect on phenotype; when associated with
FT A-13 and A-19. No reduction in 32-P incorporation mediated
FT by MAPK."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 19
FT /note="S->A: No effect on phenotype; when associated with
FT A-13 and A-16. Reduced 32-P incorporation mediated by MAPK;
FT when associated with A-13."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 19
FT /note="S->E: Reduces activity as a cdc2 inhibitor; when
FT associated with E-13."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 58
FT /note="T->A: Reduces growth rate into small colonies
FT containing many elongated cells. Phenotype enhances due to
FT increased stability; when associated with A-62. No
FT reduction in 32-P incorporation mediated by MAPK."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 58
FT /note="T->S: Shift in mobility; when associated with S-62."
FT /evidence="ECO:0000269|PubMed:12135491,
FT ECO:0000269|PubMed:9430640"
FT MUTAGEN 62
FT /note="T->A: Reduces growth rate into small colonies
FT containing many elongated cells. Phenotype enhances due to
FT increased stability; when associated with A-58."
FT /evidence="ECO:0000269|PubMed:9430640"
FT MUTAGEN 62
FT /note="T->S: Shift in mobility; when associated with S-58."
FT /evidence="ECO:0000269|PubMed:9430640"
FT MUTAGEN 110
FT /note="T->A: No effect on phenotype."
FT /evidence="ECO:0000269|PubMed:9430640"
FT MUTAGEN 212
FT /note="S->A: No effect on phenotype."
FT /evidence="ECO:0000269|PubMed:9430640"
FT CONFLICT 72..73
FT /note="ML -> IV (in Ref. 1; CAA54786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 25289 MW; C5199FE345F7484A CRC64;
MEPSTPPMRG LCTPSTPESP GSFKGVIDAS LEGNSSIMID EIPESDLPAP QVSTFPPTPA
KTPKKQLLPN LMLQDRSNSL ERCMEEDREH NPFLSSSDNQ LLSRKKRKPT PPPSDGLYYV
FRGKRIKKSF RPGTDLSTFK PKLLFADSAP SSSSDNPTSS VDLNDYSQIG ILPPNLNSIG
NKMFSLKSRV PSSSSGSFVA PPPQMRLPAY SSPQKSRSNT KDENRHNLLR
