O13958 (SSN3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Activator Kinase Repressor Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of bipolar cell growth Inferred from mutant phenotype PubMed 20501954. Source: PomBase negative regulation of cell-cell adhesion by negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 18310102. Source: PomBase phosphorylation of RNA polymerase II C-terminal domain Non-traceable author statement. Source: PomBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mediator complex Inferred from direct assay Ref.4. Source: PomBase
Molecular_function	ATP binding Inferred from sequence model. Source: PomBase RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from sequence orthology. Source: PomBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Serine/threonine-protein kinase srb10		PRO_0000086580
Regions
	Domain	5 – 319	315	Protein kinase
	Nucleotide binding	11 – 19	9	ATP By similarity
Sites
	Active site	140	1	Proton acceptor By similarity
	Binding site	36	1	ATP By similarity
Experimental info
	Mutagenesis	158	1	D → A: Abrogates kinase activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O13958 [UniParc]. Last modified April 18, 2012. Version 2. Checksum: C7F9AC9F73FFD30E	FASTA	369	42,585
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	T38311.
RefSeq	NP_593389.2. NM_001018821.2.
3D structure databases
ProteinModelPortal	O13958.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC23H4.17c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC23H4.17c.1; SPAC23H4.17c.1:pep; SPAC23H4.17c.
GeneID	2541900.
KEGG	spo:SPAC23H4.17c.
Organism-specific databases
PomBase	SPAC23H4.17c.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
KO	K02208.
OrthoDB	EOG470XRW.
Enzyme and pathway databases
BRENDA	2.7.11.22. 5615.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802987.

Entry information

Entry name

SSN3_SCHPO

Accession

Primary (citable) accession number: O13958

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	April 18, 2012
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program