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O13958 (SSN3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase srb10

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cyclin-dependent kinase 8
Suppressor of RNA polymerase B srb10
Gene names
Name:srb10
Synonyms:cdk8, prk1
ORF Names:SPAC23H4.17c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of the Cdk8 module/Srb8-11 module which is a regulatory module of the Mediator complex that regulates basal RNA polymerase II transcription. The Cdk8 module may sterically hinder the interaction between Mediator and RNA polymerase II leading to transcriptional repression of a subset of genes regulated by Mediator. Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Subunit structure

Component of the Cdk8 module of the Mediator complex. The Cdk8 module is composed of srb8, srb9, srb10 and srb11. Interacts with med17 and med18. Ref.4 Ref.6

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Serine/threonine-protein kinase srb10
PRO_0000086580

Regions

Domain5 – 319315Protein kinase
Nucleotide binding11 – 199ATP By similarity

Sites

Active site1401Proton acceptor By similarity
Binding site361ATP By similarity

Experimental info

Mutagenesis1581D → A: Abrogates kinase activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O13958 [UniParc].

Last modified April 18, 2012. Version 2.
Checksum: C7F9AC9F73FFD30E

FASTA36942,585
        10         20         30         40         50         60 
MKDGYKIIGF ISSGTYGKVY KAVSSNSNDK RLFAIKKFKA ESKQVSSNAQ QTGVSQSAIR 

        70         80         90        100        110        120 
EMMLCREIQH ENIVSLVQVL LKDGTISMVF EYAEHDLLQI IHFHSRSRTR QIPPSILKSI 

       130        140        150        160        170        180 
LWQIINGVAY LHENWIMHRD LKPANIMITA TGKVKIGDLG LGRLIRDPIL PFYSSDRVVV 

       190        200        210        220        230        240 
TIWYRAPELL LGAHDYTPAI DVWAIGCIYG EMLALSPLFK GDEIKMEDKK VVPFQSTQML 

       250        260        270        280        290        300 
RIMELLGTPT EERWPGLKNY PEYYQLSSFE VRYWNNLLPQ WYQTVKNRDP QGLDLLMKML 

       310        320        330        340        350        360 
QYDPKSRITA KQALEHVFFT SDKLWTTSPF LNQPIHYPER RISEDDSEVS SKRVLSTSLR 


SESKRFKGN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the prk1 protein kinase from Schizosaccharomyces pombe."
Watson P., Davey J.
Yeast 14:485-492(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[4]"TRAP230/ARC240 and TRAP240/ARC250 Mediator subunits are functionally conserved through evolution."
Samuelsen C.O., Baraznenok V., Khorosjutina O., Spaehr H., Kieselbach T., Holmberg S., Gustafsson C.M.
Proc. Natl. Acad. Sci. U.S.A. 100:6422-6427(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN MEDIATOR COMPLEX.
[5]"Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent transcription in vitro."
Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O., Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.
J. Biol. Chem. 278:51301-51306(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II."
Elmlund H., Baraznenok V., Lindahl M., Samuelsen C.O., Koeck P.J.B., Holmberg S., Hebert H., Gustafsson C.M.
Proc. Natl. Acad. Sci. U.S.A. 103:15788-15793(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II, INTERACTION WITH MED17 AND MED18, MUTAGENESIS OF ASP-158.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB11671.2.
PIRT38311.
RefSeqNP_593389.2. NM_001018821.2.

3D structure databases

ProteinModelPortalO13958.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278390. 246 interactions.
STRING4896.SPAC23H4.17c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC23H4.17c.1; SPAC23H4.17c.1:pep; SPAC23H4.17c.
GeneID2541900.
KEGGspo:SPAC23H4.17c.

Organism-specific databases

PomBaseSPAC23H4.17c.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK02208.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BRENDA2.7.11.22. 5615.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802987.

Entry information

Entry nameSSN3_SCHPO
AccessionPrimary (citable) accession number: O13958
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 18, 2012
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names