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Reviewed, UniProtKB/Swiss-Prot Q99J95 (CDK9_MOUSE)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell division protein kinase 9
    EC=2.7.11.22
    EC=2.7.11.23
Alternative name(s):
    Cyclin-dependent kinase 9
Gene names
Name: Cdk9
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to production elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II), SUPT5H and RDBP. The CDK9/cyclin-K complex has also a kinase activity toward CTD of RNAP II and can substitute for P-TEFb in vitro By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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

Subunit structure

Associates with CCNT1/cyclin-T1 to form P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31. Also associates with CCNK/cyclin-K. Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed at high levels in brain and kidney. Ref.1

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 BAE25966.1 differs from that shown. Reason: Frameshift at position 46.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99J95-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99J95-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q99J95-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Cell division protein kinase 9
PRO_0000085801

Regions

Domain19 – 315297Protein kinase
Nucleotide binding25 – 339ATP By similarity

Sites

Active site1491Proton acceptor By similarity
Binding site481ATP By similarity

Amino acid modifications

Modified residue1861Phosphothreonine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3531Phosphoserine By similarity

Natural variations

Alternative sequence1 – 129129Missing in isoform 3.
VSP_016290
Alternative sequence1 – 5151Missing in isoform 2.
VSP_016289

Experimental info

Sequence conflict1221T → R in BAE34054. Ref.3
Sequence conflict1541N → S in BAE25055. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 973B18869F9963E3

FASTA37242,762
        10         20         30         40         50         60 
MAKQYDSVEC PFCDEVTKYE KLAKIGQGTF GEVFKAKHRQ TGQKVALKKV LMENEKEGFP 

        70         80         90        100        110        120 
ITALREIKIL QLLKHENVVN LIEICRTKAS PYNRCKGSIY LVFDFCEHDL AGLLSNVLVK 

       130        140        150        160        170        180 
FTLSEIKRVM QMLLNGLYYI HRNKILHRDM KAANVLITRD GVLKLADFGL ARAFSLAKNS 

       190        200        210        220        230        240 
QPNRYTNRVV TLWYRPPELL LGERDYGPPI DLWGAGCIMA EMWTRSPIMQ GNTEQHQLAL 

       250        260        270        280        290        300 
ISQLCGSITP EVWPNVDKYE LFEKLELVKG QKRKVKDRLK AYVRDPYALD LIDKLLVLDP 

       310        320        330        340        350        360 
AQRIDSDDAL NHDFFWSDPM PSDLKGMLST HLTSMFEYLA PPRRKGSQIT QQSTNQSRNP 

       370 
ATTNQTEFER VF 

« Hide

Isoform 2.

Checksum: 4E7C2E2B4DB2042A
Show »

FASTA32137,002
Isoform 3.

Checksum: 99DBB3953EB6971A
Show »

FASTA24328,026

References

« Hide 'large scale' references
[1]"Cloning of murine CDK9/PITALRE and its tissue-specific expression in development."
Bagella L., MacLachlan T.K., Buono R.J., Pisano M.M., Giordano A., De Luca A.
J. Cell. Physiol. 177:206-213(1998) [PubMed: 9766517] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Genomic organization, promoter analysis, and chromosomal mapping of the mouse gene encoding Cdk9."
Bagella L., Stiegler P., De Luca A., Siracusa L.D., Giordano A.
J. Cell. Biochem. 78:170-178(2000) [PubMed: 10797576] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Eye, Lung and Spleen.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF327431 mRNA. Translation: AAK15699.1.
AF327569 Genomic DNA. Translation: AAK15706.1.
AK089276 mRNA. Translation: BAC40824.1.
AK142397 mRNA. Translation: BAE25055.1.
AK143217 mRNA. Translation: BAE25312.1.
AK144607 mRNA. Translation: BAE25966.1. Frameshift.
AK157340 mRNA. Translation: BAE34054.1.
AL772271 Genomic DNA. Translation: CAQ13017.1.
BC003901 mRNA. Translation: AAH03901.1.
IPIIPI00114953.
IPI00656169.
IPI00656171.
RefSeqNP_570930.1.
UniGeneMm.27557

3D structure databases

HSSPHSSP built from PDB template 1H4L based on UniProtKB Q00535.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99J95.

PTM databases

PhosphoSiteQ99J95.

Proteomic databases

PRIDEQ99J95.

Genome annotation databases

EnsemblENSMUST00000009699; ENSMUSP00000009699; ENSMUSG00000009555; Mus musculus. [Genome view]
GeneID107951.
KEGGmmu:107951.
UCSCuc008jgn.1. mouse.
uc008jgo.1. mouse.

Organism-specific databases

CTD107951.
MGIMGI:1328368. Cdk9.

Phylogenomic databases

HOGENOMQ99J95.
HOVERGENQ99J95.
OMATEQHQLT.

Enzyme and pathway databases

BRENDA2.7.11.22. 244.
2.7.11.23. 244.

Gene expression databases

ArrayExpressQ99J95.
BgeeQ99J95.
CleanExMM_CDK9.
GenevestigatorQ99J95.
GermOnlineENSMUSG00000009555. Mus musculus.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio359767.
SOURCESearch...

Entry information

Entry nameCDK9_MOUSE
AccessionPrimary (citable) accession number: Q99J95
Secondary accession number(s): B0R020 expand/collapse secondary AC list , Q3U002, Q3UMY2, Q3UPT3, Q3UQI6, Q8BTN0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents