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P40380 (RUM1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase inhibitor rum1
Alternative name(s):
p25-rum1
Gene names
Name:rum1
ORF Names:SPBC32F12.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of cell cycle G1 phase progression. Ensures the correct sequence of S phase and mitosis in the cell by acting as an inhibitor of the cdc2 mitotic kinase. Probably interacts with cdc2 to inhibit its action until the cell mass for Start is reached. Determines the length of the pre-Start G1 period and prevents mitosis from happening in early G1 cells. Required for maintaining pheromone-induced G1 arrest. Acts as an adapter protein since interaction with cdc13 promotes cyclin proteolysis during G1. Becomes a target for degradation at the G1/S phase transition, following phosphorylation by cig1-associated cdc2 at the G1/S phase transition. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subunit structure

Interacts with cdc13, cig2 and pop1. Ref.4 Ref.6 Ref.7 Ref.10

Subcellular location

Nucleus Ref.11.

Induction

Expression increases in nitrogen deprived environment, which is important to cause delay of the G1 phase of the cell cycle in response to nitrogen starvation. Ref.9

Post-translational modification

Phosphorylated by cig1-associated cdc2 which leads to increased stability. Phosphorylation by MAPK reduces cdc2 kinase inhibitor ability. Ref.4 Ref.5 Ref.8

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Cyclin-dependent kinase inhibitor rum1
PRO_0000097531

Regions

Region67 – 14781CDK inhibitory and cyclin-binding
Region101 – 230130Required for activity as a cdc2 kinase inhibitor
Compositional bias151 – 1544Poly-Ser
Compositional bias192 – 1976Poly-Ser

Amino acid modifications

Modified residue131Phosphothreonine; by MAPK Ref.8
Modified residue191Phosphoserine; by MAPK Ref.8
Modified residue581Phosphothreonine; by cdc2 Ref.5
Modified residue621Phosphothreonine; by cdc2 Ref.5

Experimental info

Mutagenesis51T → A: No effect on phenotype and no reduction in 32-P incorporation mediated by MAPK. Ref.5 Ref.8
Mutagenesis131T → A: No effect on phenotype; when associated with A-16 and A-19. Reduced 32-P incorporation mediated by MAPK; when associated with A-19. Ref.5 Ref.8
Mutagenesis131T → E: Reduces activity as a cdc2 inhibitor; when associated with E-19. Ref.5 Ref.8
Mutagenesis161T → A: No effect on phenotype; when associated with A-13 and A-19. No reduction in 32-P incorporation mediated by MAPK. Ref.5 Ref.8
Mutagenesis191S → A: No effect on phenotype; when associated with A-13 and A-16. Reduced 32-P incorporation mediated by MAPK; when associated with A-13. Ref.5 Ref.8
Mutagenesis191S → E: Reduces activity as a cdc2 inhibitor; when associated with E-13. Ref.5 Ref.8
Mutagenesis581T → A: Reduces growth rate into small colonies containing many elongated cells. Phenotype enhances due to increased stability; when associated with A-62. No reduction in 32-P incorporation mediated by MAPK. Ref.5 Ref.8
Mutagenesis581T → S: Shift in mobility; when associated with S-62. Ref.5 Ref.8
Mutagenesis621T → A: Reduces growth rate into small colonies containing many elongated cells. Phenotype enhances due to increased stability; when associated with A-58. Ref.5
Mutagenesis621T → S: Shift in mobility; when associated with S-58. Ref.5
Mutagenesis1101T → A: No effect on phenotype. Ref.5
Mutagenesis2121S → A: No effect on phenotype. Ref.5
Sequence conflict72 – 732ML → IV in CAA54786. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40380 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: C5199FE345F7484A

FASTA23025,289
        10         20         30         40         50         60 
MEPSTPPMRG LCTPSTPESP GSFKGVIDAS LEGNSSIMID EIPESDLPAP QVSTFPPTPA 

        70         80         90        100        110        120 
KTPKKQLLPN LMLQDRSNSL ERCMEEDREH NPFLSSSDNQ LLSRKKRKPT PPPSDGLYYV 

       130        140        150        160        170        180 
FRGKRIKKSF RPGTDLSTFK PKLLFADSAP SSSSDNPTSS VDLNDYSQIG ILPPNLNSIG 

       190        200        210        220        230 
NKMFSLKSRV PSSSSGSFVA PPPQMRLPAY SSPQKSRSNT KDENRHNLLR 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of progression through the G1 phase of the cell cycle by the rum1+ gene."
Moreno S., Nurse P.
Nature 367:236-242(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"p25rum1 orders S phase and mitosis by acting as an inhibitor of the p34cdc2 mitotic kinase."
Correa-Bordes J., Nurse P.
Cell 83:1001-1009(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"p25rum1 promotes proteolysis of the mitotic B-cyclin p56cdc13 during G1 of the fission yeast cell cycle."
Correa-Bordes J., Gulli M.P., Nurse P.
EMBO J. 16:4657-4664(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC13, PHOSPHORYLATION.
[5]"Regulation of the G1 phase of the cell cycle by periodic stabilization and degradation of the p25rum1 CDK inhibitor."
Benito J., Martin-Castellanos C., Moreno S.
EMBO J. 17:482-497(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-58 AND THR-62, MUTAGENESIS OF THR-5; THR-13; THR-16; SER-19; THR-58; THR-62; THR-110 AND SER-212.
[6]"The Cdk inhibitors p25rum1 and p40SIC1 are functional homologues that play similar roles in the regulation of the cell cycle in fission and budding yeast."
Sanchez-Diaz A., Gonzalez I., Arellano M., Moreno S.
J. Cell Sci. 111:843-851(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC13, DOMAIN.
[7]"Cyclin B proteolysis and the cyclin-dependent kinase inhibitor rum1p are required for pheromone-induced G1 arrest in fission yeast."
Stern B., Nurse P.
Mol. Biol. Cell 9:1309-1321(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC13 AND CIG2.
[8]"Rum1, an inhibitor of cyclin-dependent kinase in fission yeast, is negatively regulated by mitogen-activated protein kinase-mediated phosphorylation at Ser and Thr residues."
Matsuoka K., Kiyokawa N., Taguchi T., Matsui J., Suzuki T., Mimori K., Nakajima H., Takenouchi H., Weiran T., Katagiri Y.U., Fujimoto J.
Eur. J. Biochem. 269:3511-3521(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-13 AND SER-19, MUTAGENESIS OF THR-5; THR-13; THR-16; SER-19 AND THR-58.
[9]"Regulated mRNA stability of the Cdk inhibitor Rum1 links nutrient status to cell cycle progression."
Daga R.R., Bolanos P., Moreno S.
Curr. Biol. 13:2015-2024(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[10]"Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the fission yeast S phase cyclin Cig2."
Yamano H., Kominami K., Harrison C., Kitamura K., Katayama S., Dhut S., Hunt T., Toda T.
J. Biol. Chem. 279:18974-18980(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POP1.
[11]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77730 mRNA. Translation: CAA54786.1.
CU329671 Genomic DNA. Translation: CAA19370.1.
PIRS41043.
T40233.
RefSeqNP_596152.1. NM_001022071.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276195. 31 interactions.
IntActP40380. 5 interactions.
MINTMINT-4689673.
STRING4896.SPBC32F12.09-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC32F12.09.1; SPBC32F12.09.1:pep; SPBC32F12.09.
GeneID2539640.
KEGGspo:SPBC32F12.09.

Organism-specific databases

PomBaseSPBC32F12.09.

Phylogenomic databases

OMADICIFRR.

Family and domain databases

ProtoNetSearch...

Other

NextBio20800794.

Entry information

Entry nameRUM1_SCHPO
AccessionPrimary (citable) accession number: P40380
Secondary accession number(s): O74373
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 11, 2001
Last modified: June 11, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names