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Q96WV9 (CDK9_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:pi014, SPBC32H8.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Probable cyclin-dependent kinase 9
PRO_0000085808

Regions

Domain36 – 339304Protein kinase
Nucleotide binding42 – 509ATP By similarity
Region1 – 385385Interacts with pch1
Region442 – 52382Binds to pct1

Sites

Active site1661Proton acceptor By similarity
Binding site651ATP By similarity

Amino acid modifications

Modified residue2111Phosphotyrosine Ref.5
Modified residue2121Phosphothreonine Ref.5
Modified residue5651Phosphothreonine Ref.5
Modified residue5771Phosphoserine Ref.5

Experimental info

Mutagenesis651K → A: Abolishes activity. Ref.3
Mutagenesis831E → A: Defective kinase activity. Ref.3
Mutagenesis1841D → N: Abolishes activity. Ref.3
Mutagenesis2121T → A: Abolishes activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q96WV9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 28DFF6032388E16A

FASTA59168,029
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. 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]"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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565 AND SER-577, IDENTIFICATION BY 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.
RefSeqNP_595616.1. NM_001021511.2.

3D structure databases

ProteinModelPortalQ96WV9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276771. 18 interactions.
IntActQ96WV9. 2 interactions.
MINTMINT-253408.
STRING4896.SPBC32H8.10-1.

Proteomic databases

PRIDEQ96WV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC32H8.10.1; SPBC32H8.10.1:pep; SPBC32H8.10.
GeneID2540239.
KEGGspo:SPBC32H8.10.

Organism-specific databases

PomBaseSPBC32H8.10.

Phylogenomic databases

eggNOGCOG0515.
KOK15562.
OMACHSNERM.
OrthoDBEOG7K3TWD.
PhylomeDBQ96WV9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801370.

Entry information

Entry nameCDK9_SCHPO
AccessionPrimary (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: April 16, 2014
This is version 102 of the entry and version 1 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