Q96WV9 (CDK9_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable cyclin-dependent kinase 9
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
Cell division protein kinase 9

Gene names

Name:	cdk9
ORF Names:	SPBC32H8.10, pi014

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the positive transcription elongation factor b (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the C-terminal domain (CTD) of RNA polymerase II and spt5. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	May be activated by autophosphorylation or phosphorylation by a separate activating kinase.
Subunit structure	Interacts with pch1 cyclin via its N-terminal domain. Via its C-terminal domain, interacts with RNA triphosphatase pct1 which is involved in mRNA capping. Interacts also with pcm1. Ref.3 Ref.4
Subcellular location	Nucleus.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA21391.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	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	phosphorylation of RNA polymerase II C-terminal domain Inferred from mutant phenotype. Source: GeneDB_Spombe regulation of transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype. Source: GeneDB_Spombe transcription from RNA polymerase I promoter Inferred from genetic interaction. Source: GeneDB_Spombe
Cellular component	P-TEFb-cap methyltransferase complex Inferred from direct assay. Source: GeneDB_Spombe positive transcription elongation factor complex b Non-traceable author statement. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from direct assay Ref.3. Source: UniProtKB RNA polymerase II carboxy-terminal domain kinase activity Inferred from direct assay. Source: GeneDB_Spombe cyclin-dependent protein kinase activity Inferred from direct assay Ref.3. Source: UniProtKB protein binding Inferred from physical interaction Ref.3. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pct1	Q9P6Q6	2	EBI-443557,EBI-443547

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 591	591	Probable cyclin-dependent kinase 9		PRO_0000085808
Regions
	Domain	36 – 339	304	Protein kinase
	Nucleotide binding	42 – 50	9	ATP By similarity
	Region	1 – 385	385	Interacts with pch1
	Region	442 – 523	82	Binds to pct1
Sites
	Active site	166	1	Proton acceptor By similarity
	Binding site	65	1	ATP By similarity
Amino acid modifications
	Modified residue	211	1	Phosphotyrosine Ref.5
	Modified residue	212	1	Phosphothreonine Ref.5
	Modified residue	565	1	Phosphothreonine Ref.5
	Modified residue	577	1	Phosphoserine Ref.5
Experimental info
	Mutagenesis	65	1	K → A: Abolishes activity. Ref.3
	Mutagenesis	83	1	E → A: Defective kinase activity. Ref.3
	Mutagenesis	184	1	D → N: Abolishes activity. Ref.3
	Mutagenesis	212	1	T → A: Abolishes activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96WV9 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 28DFF6032388E16A	FASTA	591	68,029
	10 20 30 40 50 60 MKRSSSVSVE DEKSARRKLD VVPKLHFVGC SHLTDYHLME KLGEGTFGEV YKSQRRKDGK 70 80 90 100 110 120 VYALKRILMH TEKEGFPITA IREIKILKSI KHENIIPLSD MTVVRADKKH RRRGSIYMVT 130 140 150 160 170 180 PYMDHDLSGL LENPSVKFTE PQIKCYMKQL FAGTKYLHDQ LILHRDLKAA NLLIDNHGIL 190 200 210 220 230 240 KIADFGLARV ITEESYANKN PGLPPPNRRE YTGCVVTRWY RSPELLLGER RYTTAIDMWS 250 260 270 280 290 300 VGCIMAEMYK GRPILQGSSD LDQLDKIFRL CGSPTQATMP NWEKLPGCEG VRSFPSHPRT 310 320 330 340 350 360 LETAFFTFGK EMTSLCGAIL TLNPDERLSA SMALEHEYFT TPPYPANPSE LQSYSASHEY 370 380 390 400 410 420 DKRRKREQRD ANSHAFEQTA NGKRQFRFMT RGPSDPWYGI RRPNYNSQPQ YQRGSYNREG 430 440 450 460 470 480 GNMDRSRNVN YQPKRQQNFK PLTSDLPQKN SEFSETNAMN QTSNHSHADG QRYYRPEQDR 490 500 510 520 530 540 SQRLRNPSDY GRQGRQSSQS QQPAWNVSSR YQNNSKVQTT SRASENADTN KTQHNIKYID 550 560 570 580 590 SYVPEYSIAR QSANQKTNEQ HPSSTSLHQQ STSDLKSPSF HENSNVDDTP K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment." Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M. Yeast 16:71-80(2000) [PubMed: 10620777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[3]	"Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control." Pei Y., Schwer B., Shuman S. J. Biol. Chem. 278:7180-7188(2003) [PubMed: 12475973] [Abstract] Cited for: FUNCTION, INTERACTION WITH PCH1 AND PCT1, MUTAGENESIS OF LYS-65; GLU-83; ASP-184 AND THR-212.
[4]	"Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo." Pei Y., Du H., Singer J., Saint Amour C., Granitto S., Shuman S., Fisher R.P. Mol. Cell. Biol. 26:777-788(2006) [PubMed: 16428435] [Abstract] Cited for: INTERACTION WITH PCM1.
[5]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565 AND SER-577, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004534 Genomic DNA. Translation: BAA21391.2. Different initiation. CU329671 Genomic DNA. Translation: CAC37500.1.
RefSeq	NP_595616.1. NM_001021511.1.
3D structure databases
ProteinModelPortal	Q96WV9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96WV9. 2 interactions.
MINT	MINT-253408.
STRING	Q96WV9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
GeneID	2540239.
GenomeReviews	Gene locus cdk9 in contig CU329671_GR.
KEGG	spo:SPBC32H8.10.
NMPDR	fig|4896.1.peg.1482.
Organism-specific databases
GeneDB_Spombe	SPBC32H8.10.
Phylogenomic databases
eggNOG	fuNOG04620.
GeneTree	EFGT00050000000591.
OMA	LGERRYT.
OrthoDB	EOG41K2MW.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003650-MONOMER.
Gene expression databases
ArrayExpress	Q96WV9.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K15562.
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...

Entry information

Entry name

CDK9_SCHPO

Accession

Primary (citable) accession number: Q96WV9
Secondary accession number(s): O13607

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	December 1, 2001
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program