Q12126 (CRK1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase crk1
EC=2.7.11.23

Alternative name(s):
Mitotic catastrophe suppressor 6

Gene names

Name:	crk1
Synonyms:	mcs6, mop1
ORF Names:	SPBC19F8.07

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	335 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein kinase essential for cell proliferation, where it is required for completion of cytokinesis. Phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II. Ref.1 Ref.2
Catalytic activity	ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Subunit structure	One of the nine subunits forming the core-TFIIH basal transcription factor. Interacts with mcs2 and tfb3. Ref.1 Ref.2 Ref.5 Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.7.
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	Cell cycle Cell division Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	P-TEFb-cap methyltransferase complex localization Inferred from mutant phenotype PubMed 19328067. Source: PomBase cell division Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation of RNA polymerase II C-terminal domain Inferred from mutant phenotype PubMed 19328067. Source: PomBase positive regulation of transcription from RNA polymerase II promoter Inferred from sequence orthology. Source: PomBase regulation of mitotic cell cycle Inferred from genetic interaction Ref.2. Source: PomBase regulation of transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype PubMed 19328067. Source: PomBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.7. Source: PomBase holo TFIIH complex Inferred from sequence orthology. Source: PomBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from direct assay PubMed 19328067. Source: PomBase cyclin-dependent protein kinase activating kinase activity Inferred from genetic interaction Ref.2. Source: PomBase cyclin-dependent protein serine/threonine kinase activity Non-traceable author statement. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 335	335	Serine/threonine-protein kinase crk1		PRO_0000085879
Regions
	Domain	11 – 292	282	Protein kinase
	Nucleotide binding	17 – 25	9	ATP By similarity
Sites
	Active site	133	1	Proton acceptor By similarity
	Binding site	40	1	ATP By similarity
Amino acid modifications
	Modified residue	162	1	Phosphoserine Ref.8
	Modified residue	165	1	Phosphoserine; by CAK Ref.4 Ref.8
	Modified residue	318	1	Phosphoserine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q12126 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8AD88A491ACB1671	FASTA	335	38,538
	10 20 30 40 50 60 MDIEKSDKWT YVKERKVGEG TYAVVFLGRQ KETNRRVAIK KIKVGQFKDG IDISALREIK 70 80 90 100 110 120 FLRESRHDNV IELVDVFSTK SNLNIILEFL DSDLEMLIKD KFIVFQPAHI KSWMVMLLRG 130 140 150 160 170 180 LHHIHSRFIL HRDLKPNNLL ISSDGVLKLA DFGLSRDFGT PSHMSHQVIT RWYRPPELFM 190 200 210 220 230 240 GCRSYGTGVD MWSVGCIFAE LMLRTPYLPG ESDLDQLNVI FRALGTPEPE VIKSMQQLPN 250 260 270 280 290 300 YVEMKHIPPP NGGMEALFSA AGHEEIDLLK MMLDYNPYRR PTAQQALEHH YFSALPKPTH 310 320 330 PSLLPRKGGE EGIKHVSSDL QRQNNFPMRA NIKFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Schizosaccharomyces pombe Mop1-Mcs2 is related to mammalian CAK." Damagnez V., Makela T.P., Cottarel G. EMBO J. 14:6164-6172(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MCS2.
[2]	"Identification of a cdk-activating kinase in fission yeast." Buck V., Russell P., Millar J.B.A. EMBO J. 14:6173-6183(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MCS2. Strain: 972 / ATCC 24843.
[3]	"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.
[4]	"Fission yeast Csk1 is a CAK-activating kinase (CAKAK)." Hermand D., Pihlak A., Westerling T., Damagnez V., Vandenhaute J., Cottarel G., Makela T.P. EMBO J. 17:7230-7238(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-165.
[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: SUBUNIT.
[6]	"Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast." Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J., Maekelae T.P., Hermand D. Biochem. Biophys. Res. Commun. 325:1424-1432(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MCS2 AND TFB3.
[7]	"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].
[8]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-165 AND SER-318, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L47353 mRNA. Translation: AAB00356.1. X91239 Genomic DNA. Translation: CAA62621.1. CU329671 Genomic DNA. Translation: CAA19127.1.
PIR	S66145.
RefSeq	NP_596349.1. NM_001022269.2.
3D structure databases
ProteinModelPortal	Q12126.
SMR	Q12126. Positions 14-307.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12126. 2 interactions.
STRING	4896.SPBC19F8.07-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC19F8.07.1; SPBC19F8.07.1:pep; SPBC19F8.07.
GeneID	2540471.
KEGG	spo:SPBC19F8.07.
Organism-specific databases
PomBase	SPBC19F8.07.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
KO	K02202.
OMA	PRPNCPA.
OrthoDB	EOG4DV8W4.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. 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. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801598.

Entry information

Entry name

CRK1_SCHPO

Accession

Primary (citable) accession number: Q12126

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program