| Tag | Content |
|---|
| EKPD ID | EKS-BOT-00065 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| CMGC/CDK | 371.7 | 2.3E-111 | 19 | 315 | 297 |
|
| Status | Reviewed |
| Ensembl Protein | ENSBTAP00000006162 |
| UniProt Accession | Q5EAB2; Q148K6; Q58CR5; |
| Protein Name | Cyclin-dependent kinase 9 |
| Protein Synonyms/Alias | Cell division protein kinase 9; |
| Gene Name | CDK9 |
| Gene Synonyms/Alias | CDK9; |
| Ensembl Information | |
| Organism | Bos taurus |
| Functional Description | Protein kinase involved in the regulation oftranscription. 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 productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single- stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement. RPB1/POLR2A phosphorylation on 'Ser-2' in CTD activates transcription. AR phosphorylation modulates AR transcription factor promoter selectivity and cell growth. DSIF and NELF phosphorylation promotes transcription by inhibiting their negative effect. The phosphorylation of MYOD1 enhances its transcriptional activity and thus promotes muscle differentiation (By similarity). |
| Protein Length | 372 |
Protein Sequence
(FASTA) | | MAKQYDSVEC PFCDEVTKYE KLAKIGQGTF GEVFKAKHRK TGQKVALKKV LMENEKEGFP 60 | | ITALREIKIL QLLKHENVVN LIEICRTKAS PYNRCKGSIY LVFDFCEHDL AGLLSNVLVK 120 | | FTLSEIKRVM QMLLNGLYYI HRNKILHRDM KAANVLITRD GVLKLADFGL ARAFSLAKNS 180 | | QPNRYTNRVV TLWYRPPELL LGERDYGPPI DLWGAGCIMA EMWTRSPIMQ GNTEQHQLAL 240 | | ISQLCGSITP EVWPNVDKYE LFEKVELVKG QKRKVKDRLK AYVRDPYALD LIDKLLVLDP 300 | | AQRIDSDDAL NHDFFWSDPM PSDLKGMLST HLTSMFEYLA PPRRKGSQIT QQSTNQSRNP 360 | | ATTNQTEFER VF 372 |
|
Nucleotide Sequence
(FASTA) | | ATGGCAAAGC AGTACGACTC GGTGGAGTGC CCTTTTTGTG ATGAGGTGAC CAAATATGAG 60 | | AAGCTCGCTA AAATCGGCCA AGGCACCTTC GGGGAGGTGT TTAAGGCAAA GCACCGCAAG 120 | | ACTGGCCAAA AGGTGGCCCT GAAGAAGGTA CTGATGGAGA ACGAGAAAGA GGGGTTCCCC 180 | | ATTACAGCAT TGCGGGAGAT CAAGATCCTC CAGCTTCTAA AACACGAGAA TGTGGTCAAC 240 | | TTGATTGAGA TCTGTCGAAC CAAAGCTTCC CCCTATAACC GCTGCAAAGG CAGTATATAC 300 | | CTGGTGTTTG ACTTCTGTGA GCATGATCTT GCTGGGCTGC TGAGCAACGT TTTAGTCAAG 360 | | TTCACACTAT CTGAGATCAA GAGGGTCATG CAGATGTTGC TTAACGGCCT CTACTACATC 420 | | CATAGGAACA AGATCCTGCA CCGGGACATG AAGGCGGCTA ACGTGCTCAT CACCCGCGAT 480 | | GGGGTTCTGA AGCTGGCGGA CTTTGGGCTG GCCCGGGCCT TCAGCCTGGC CAAGAACAGC 540 | | CAGCCCAACC GCTACACCAA CCGTGTGGTG ACCCTCTGGT ACCGGCCCCC AGAGCTGTTG 600 | | CTCGGGGAGC GGGACTACGG CCCCCCCATT GATCTGTGGG GTGCTGGGTG CATCATGGCG 660 | | GAGATGTGGA CCCGCAGCCC CATCATGCAG GGCAACACGG AGCAGCACCA ACTCGCCCTC 720 | | ATCAGCCAGC TCTGCGGCTC CATCACCCCC GAGGTGTGGC CAAATGTGGA CAAGTACGAG 780 | | CTGTTTGAGA AAGTGGAGCT GGTCAAGGGC CAGAAGCGGA AGGTGAAGGA CAGGCTGAAG 840 | | GCCTACGTGC GAGACCCCTA CGCACTGGAC CTCATCGACA AGCTGCTGGT GCTGGACCCC 900 | | GCCCAGCGCA TCGACAGTGA CGACGCCCTC AACCACGACT TCTTCTGGTC TGACCCCATG 960 | | CCCTCGGACC TCAAGGGCAT GCTGTCCACC CACCTGACAT CCATGTTCGA GTACCTGGCA 1020 | | CCTCCACGCC GGAAGGGCAG CCAGATCACC CAGCAGTCTA CCAACCAGAG CCGGAATCCC 1080 | | GCCACCACCA ACCAGACGGA GTTTGAGCGC GTCTTCTGA 1119 |
|
| Domain Profile | S: 1 yeklekigeGtygkvykakdketgevvAlKkirlekekegvpitalrEisllkelkhkni 60 | yekl+kig+Gt+g+v+kak+++tg++vAlKk+ +e+ekeg+pitalrEi++l+ lkh+n+ | Q: 19 YEKLAKIGQGTFGEVFKAKHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENV 78 | 99********************************************************** |
| S: 61 vkLlevva.......kdkkklyLvfefleqdLkkllkkkkkkklsleevkslllqllegl 113 | v+L+e++ + k ++yLvf+f+e+dL+ ll++ k++l+e+k+++++ll+gl | Q: 79 VNLIEICRtkaspynRCKGSIYLVFDFCEHDLAGLLSNVLV-KFTLSEIKRVMQMLLNGL 137 | ********99999988889*********************9.****************** |
| S: 114 aylHsnkilHRDlKpqNlLiskegklklaDfGlaraf....ssplktytkevvTlwYraP 169 | y+H+nkilHRD+K++N+Li+++g+lklaDfGlaraf +s+ ++yt++vvTlwYr+P | Q: 138 YYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFslakNSQPNRYTNRVVTLWYRPP 197 | *************************************7776555557************* |
| S: 170 elLlgakeYstavDiWsvgcilaelltrkplfqgkseidqlerifkllgtpsekvwpevs 229 | elLlg+++Y+ +D+W++gci+ae++tr+p++qg++e++ql i++l+g+++ +vwp+v | Q: 198 ELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVD 257 | ************************************************************ |
| S: 230 klpeyk.ksfpkkkkkklkekvkklkek..aldllekllaldpkkRisakealqhkyf 284 | k++ ++ ++ k +k+k+k+++k++ ++ aldl++kll ldp++Ri++++al+h++f | Q: 258 KYELFEkVELVKGQKRKVKDRLKAYVRDpyALDLIDKLLVLDPAQRIDSDDALNHDFF 315 | ******88999999999**999887755469*************************98 |
|
Domain Sequence
(FASTA) | | YEKLAKIGQG TFGEVFKAKH RKTGQKVALK KVLMENEKEG FPITALREIK ILQLLKHENV 60 | | VNLIEICRTK ASPYNRCKGS IYLVFDFCEH DLAGLLSNVL VKFTLSEIKR VMQMLLNGLY 120 | | YIHRNKILHR DMKAANVLIT RDGVLKLADF GLARAFSLAK NSQPNRYTNR VVTLWYRPPE 180 | | LLLGERDYGP PIDLWGAGCI MAEMWTRSPI MQGNTEQHQL ALISQLCGSI TPEVWPNVDK 240 | | YELFEKVELV KGQKRKVKDR LKAYVRDPYA LDLIDKLLVL DPAQRIDSDD ALNHDFF 297 |
|
| Keyword | Acetylation; ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Ubl conjugation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
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| Created Date | 20-Feb-2013 |