| UniProt ID | CDK9_HUMAN | |
|---|---|---|
| UniProt AC | P50750 | |
| Protein Name | Cyclin-dependent kinase 9 | |
| Gene Name | CDK9 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 372 | |
| Subcellular Localization | Nucleus. Cytoplasm. Nucleus, PML body. Accumulates on chromatin in response to replication stress. Complexed with CCNT1 in nuclear speckles, but uncomplexed form in the cytoplasm. The translocation from nucleus to cytoplasm is XPO1/CRM1-dependent. As | |
| Protein Description | Protein kinase involved in the regulation of transcription. 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.. | |
| Protein Sequence | MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Acetylation | -----MAKQYDSVEC -----CCCCCCCCCC | 48.36 | 23749302 | |
| 3 | Ubiquitination | -----MAKQYDSVEC -----CCCCCCCCCC | 48.36 | - | |
| 7 | Phosphorylation | -MAKQYDSVECPFCD -CCCCCCCCCCCCCC | 18.19 | - | |
| 18 | Ubiquitination | PFCDEVSKYEKLAKI CCCCHHHHHHHHHHH | 63.71 | - | |
| 21 | Acetylation | DEVSKYEKLAKIGQG CHHHHHHHHHHHCCC | 51.13 | 26051181 | |
| 21 | Methylation | DEVSKYEKLAKIGQG CHHHHHHHHHHHCCC | 51.13 | - | |
| 21 | Ubiquitination | DEVSKYEKLAKIGQG CHHHHHHHHHHHCCC | 51.13 | - | |
| 24 | Sumoylation | SKYEKLAKIGQGTFG HHHHHHHHHCCCCHH | 58.78 | - | |
| 24 | Sumoylation | SKYEKLAKIGQGTFG HHHHHHHHHCCCCHH | 58.78 | - | |
| 24 | Ubiquitination | SKYEKLAKIGQGTFG HHHHHHHHHCCCCHH | 58.78 | 21906983 | |
| 24 (in isoform 1) | Ubiquitination | - | 58.78 | 21890473 | |
| 26 (in isoform 2) | Phosphorylation | - | 21.11 | 18691976 | |
| 27 (in isoform 2) | Phosphorylation | - | 51.75 | 17192257 | |
| 29 | Phosphorylation | LAKIGQGTFGEVFKA HHHHCCCCHHHHHHH | 22.15 | 19060867 | |
| 35 | Acetylation | GTFGEVFKARHRKTG CCHHHHHHHHHCHHC | 50.08 | 25953088 | |
| 35 | Methylation | GTFGEVFKARHRKTG CCHHHHHHHHHCHHC | 50.08 | - | |
| 35 | Ubiquitination | GTFGEVFKARHRKTG CCHHHHHHHHHCHHC | 50.08 | 21906983 | |
| 35 (in isoform 1) | Ubiquitination | - | 50.08 | 21890473 | |
| 35 (in isoform 2) | Phosphorylation | - | 50.08 | 17192257 | |
| 43 (in isoform 2) | Phosphorylation | - | 42.13 | 19369195 | |
| 44 | Acetylation | RHRKTGQKVALKKVL HHCHHCCCHHHHHHH | 30.71 | 18250157 | |
| 44 | Ubiquitination | RHRKTGQKVALKKVL HHCHHCCCHHHHHHH | 30.71 | 18250157 | |
| 48 | Acetylation | TGQKVALKKVLMENE HCCCHHHHHHHHHCC | 30.97 | 18250157 | |
| 49 | Sumoylation | GQKVALKKVLMENEK CCCHHHHHHHHHCCC | 41.26 | - | |
| 49 | Acetylation | GQKVALKKVLMENEK CCCHHHHHHHHHCCC | 41.26 | 26051181 | |
| 49 | Malonylation | GQKVALKKVLMENEK CCCHHHHHHHHHCCC | 41.26 | 26320211 | |
| 49 | Sumoylation | GQKVALKKVLMENEK CCCHHHHHHHHHCCC | 41.26 | - | |
| 49 | Ubiquitination | GQKVALKKVLMENEK CCCHHHHHHHHHCCC | 41.26 | - | |
| 52 (in isoform 2) | Phosphorylation | - | 6.10 | 30266825 | |
| 54 (in isoform 2) | Phosphorylation | - | 52.23 | 30266825 | |
| 55 (in isoform 2) | Phosphorylation | - | 38.90 | 30266825 | |
| 56 | Acetylation | KVLMENEKEGFPITA HHHHHCCCCCCCCHH | 74.78 | 56117427 | |
| 56 | Ubiquitination | KVLMENEKEGFPITA HHHHHCCCCCCCCHH | 74.78 | 21906983 | |
| 56 (in isoform 1) | Ubiquitination | - | 74.78 | 21890473 | |
| 56 (in isoform 2) | Phosphorylation | - | 74.78 | 30266825 | |
| 62 | Phosphorylation | EKEGFPITALREIKI CCCCCCCHHHHHHHH | 21.63 | 24719451 | |
| 68 | Acetylation | ITALREIKILQLLKH CHHHHHHHHHHHHCC | 32.39 | 56117425 | |
| 68 | Ubiquitination | ITALREIKILQLLKH CHHHHHHHHHHHHCC | 32.39 | 21890473 | |
| 68 (in isoform 1) | Ubiquitination | - | 32.39 | 21890473 | |
| 74 | Acetylation | IKILQLLKHENVVNL HHHHHHHCCCCHHCH | 58.42 | 56117429 | |
| 74 | Ubiquitination | IKILQLLKHENVVNL HHHHHHHCCCCHHCH | 58.42 | - | |
| 85 | Glutathionylation | VVNLIEICRTKASPY HHCHHHHHCCCCCCC | 2.68 | 22555962 | |
| 86 | Methylation | VNLIEICRTKASPYN HCHHHHHCCCCCCCC | 44.94 | - | |
| 88 | Ubiquitination | LIEICRTKASPYNRC HHHHHCCCCCCCCCC | 27.75 | 21906983 | |
| 88 (in isoform 1) | Ubiquitination | - | 27.75 | 21890473 | |
| 90 | Phosphorylation | EICRTKASPYNRCKG HHHCCCCCCCCCCCC | 29.49 | - | |
| 120 (in isoform 2) | Ubiquitination | - | 28.59 | - | |
| 127 | Acetylation | KFTLSEIKRVMQMLL HCCHHHHHHHHHHHH | 34.58 | 56117433 | |
| 127 | Methylation | KFTLSEIKRVMQMLL HCCHHHHHHHHHHHH | 34.58 | - | |
| 135 (in isoform 2) | Ubiquitination | - | 34.17 | - | |
| 138 | Phosphorylation | QMLLNGLYYIHRNKI HHHHHHHHHHHHCCC | 11.19 | 24043423 | |
| 139 | Phosphorylation | MLLNGLYYIHRNKIL HHHHHHHHHHHCCCC | 8.69 | 24043423 | |
| 141 (in isoform 2) | Ubiquitination | - | 15.90 | 21890473 | |
| 151 | Sumoylation | KILHRDMKAANVLIT CCCCCCHHHHCEEEE | 48.95 | - | |
| 151 | Sumoylation | KILHRDMKAANVLIT CCCCCCHHHHCEEEE | 48.95 | - | |
| 151 | Ubiquitination | KILHRDMKAANVLIT CCCCCCHHHHCEEEE | 48.95 | 21906983 | |
| 151 (in isoform 1) | Ubiquitination | - | 48.95 | 21890473 | |
| 152 (in isoform 2) | Ubiquitination | - | 9.53 | 21890473 | |
| 164 | Acetylation | ITRDGVLKLADFGLA EECCCHHHHHHHHHH | 38.94 | 56117411 | |
| 164 | Ubiquitination | ITRDGVLKLADFGLA EECCCHHHHHHHHHH | 38.94 | 21890473 | |
| 164 (in isoform 1) | Ubiquitination | - | 38.94 | 21890473 | |
| 173 (in isoform 2) | Ubiquitination | - | 7.86 | 21890473 | |
| 175 | Phosphorylation | FGLARAFSLAKNSQP HHHHHHHHHHHCCCC | 26.82 | 21533037 | |
| 178 | Acetylation | ARAFSLAKNSQPNRY HHHHHHHHCCCCCCC | 63.53 | 25953088 | |
| 178 | Ubiquitination | ARAFSLAKNSQPNRY HHHHHHHHCCCCCCC | 63.53 | 21906983 | |
| 178 (in isoform 1) | Ubiquitination | - | 63.53 | 21890473 | |
| 180 | Phosphorylation | AFSLAKNSQPNRYTN HHHHHHCCCCCCCCC | 46.43 | 18691976 | |
| 185 | Phosphorylation | KNSQPNRYTNRVVTL HCCCCCCCCCCEEEE | 18.27 | 20363803 | |
| 185 (in isoform 2) | Ubiquitination | - | 18.27 | 21890473 | |
| 186 | Phosphorylation | NSQPNRYTNRVVTLW CCCCCCCCCCEEEEE | 17.20 | 26846344 | |
| 194 | Phosphorylation | NRVVTLWYRPPELLL CCEEEEEECCHHHHC | 19.16 | 18083107 | |
| 205 (in isoform 2) | Ubiquitination | - | 48.73 | 21890473 | |
| 268 (in isoform 2) | Ubiquitination | - | 4.83 | 21890473 | |
| 269 | Acetylation | YEKLELVKGQKRKVK HHHHHHHHCCCHHHH | 69.15 | 56117437 | |
| 269 | Ubiquitination | YEKLELVKGQKRKVK HHHHHHHHCCCHHHH | 69.15 | 21906983 | |
| 269 (in isoform 1) | Ubiquitination | - | 69.15 | 21890473 | |
| 274 | Acetylation | LVKGQKRKVKDRLKA HHHCCCHHHHHHHHH | 61.75 | 7705799 | |
| 276 | Acetylation | KGQKRKVKDRLKAYV HCCCHHHHHHHHHHH | 39.92 | 7705813 | |
| 280 | Ubiquitination | RKVKDRLKAYVRDPY HHHHHHHHHHHCCHH | 38.27 | - | |
| 281 (in isoform 2) | Ubiquitination | - | 16.79 | 21890473 | |
| 282 | Phosphorylation | VKDRLKAYVRDPYAL HHHHHHHHHCCHHHH | 8.40 | 29496907 | |
| 287 | Phosphorylation | KAYVRDPYALDLIDK HHHHCCHHHHHHHHH | 24.88 | 29496907 | |
| 294 | Ubiquitination | YALDLIDKLLVLDPA HHHHHHHHHCCCCHH | 36.41 | - | |
| 295 (in isoform 2) | Ubiquitination | - | 3.38 | 21890473 | |
| 317 | Phosphorylation | LNHDFFWSDPMPSDL CCCCCCCCCCCCHHH | 27.04 | - | |
| 329 | Phosphorylation | SDLKGMLSTHLTSMF HHHHHHHHHHHHHHH | 12.61 | 17081983 | |
| 330 | Phosphorylation | DLKGMLSTHLTSMFE HHHHHHHHHHHHHHH | 19.55 | 17081983 | |
| 333 | Phosphorylation | GMLSTHLTSMFEYLA HHHHHHHHHHHHHHC | 15.56 | 17081983 | |
| 334 | Phosphorylation | MLSTHLTSMFEYLAP HHHHHHHHHHHHHCC | 28.03 | 22496350 | |
| 338 | Phosphorylation | HLTSMFEYLAPPRRK HHHHHHHHHCCCCCC | 9.26 | - | |
| 345 | Sumoylation | YLAPPRRKGSQITQQ HHCCCCCCCCCCCCC | 65.28 | - | |
| 345 | Acetylation | YLAPPRRKGSQITQQ HHCCCCCCCCCCCCC | 65.28 | 56117421 | |
| 345 | Sumoylation | YLAPPRRKGSQITQQ HHCCCCCCCCCCCCC | 65.28 | - | |
| 345 | Ubiquitination | YLAPPRRKGSQITQQ HHCCCCCCCCCCCCC | 65.28 | 2190698 | |
| 345 (in isoform 1) | Ubiquitination | - | 65.28 | 21890473 | |
| 347 | Phosphorylation | APPRRKGSQITQQST CCCCCCCCCCCCCCC | 22.80 | 25159151 | |
| 350 | Phosphorylation | RRKGSQITQQSTNQS CCCCCCCCCCCCCCC | 16.96 | 30266825 | |
| 353 | Phosphorylation | GSQITQQSTNQSRNP CCCCCCCCCCCCCCC | 21.36 | 21955146 | |
| 354 | Phosphorylation | SQITQQSTNQSRNPA CCCCCCCCCCCCCCC | 32.70 | 21955146 | |
| 357 | Phosphorylation | TQQSTNQSRNPATTN CCCCCCCCCCCCCCC | 35.77 | 21082442 | |
| 362 | Phosphorylation | NQSRNPATTNQTEFE CCCCCCCCCCCCHHH | 27.77 | 19060867 | |
| 363 | Phosphorylation | QSRNPATTNQTEFER CCCCCCCCCCCHHHH | 27.69 | 7695608 | |
| 366 | Phosphorylation | NPATTNQTEFERVF- CCCCCCCCHHHHCC- | 44.72 | - | |
| 370 | Methylation | TNQTEFERVF----- CCCCHHHHCC----- | 40.23 | - | |
| 386 (in isoform 2) | Ubiquitination | - | 21890473 | ||
| 397 (in isoform 2) | Ubiquitination | - | - | ||
| 411 (in isoform 2) | Ubiquitination | - | - | ||
| 462 (in isoform 2) | Ubiquitination | - | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 90 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 175 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
| 186 | T | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
| 186 | T | Phosphorylation | Kinase | CAMK1D | Q8IU85 | Uniprot |
| 347 | S | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 347 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
| 347 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 347 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 350 | T | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 353 | S | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 354 | T | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 357 | S | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 362 | T | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| 363 | T | Phosphorylation | Kinase | CDK9 | P50750 | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | UBR5 | O95071 | PMID:21127351 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:11689688 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 2 | S | Acetylation |
| 28426094 |
| 2 | S | Phosphorylation |
| 28426094 |
| 2 | S | Phosphorylation |
| 21127351 |
| 2 | S | ubiquitylation |
| 21127351 |
| 29 | T | Phosphorylation |
| 21448926 |
| 29 | T | Phosphorylation |
| 21448926 |
| 44 | K | Acetylation |
| 17452463 |
| 48 | K | Acetylation |
| 18250157 |
| 175 | S | Phosphorylation |
| 21533037 |
| 186 | T | Phosphorylation |
| 11145967 |
| 186 | T | Phosphorylation |
| 11145967 |
| 186 | T | Phosphorylation |
| 11145967 |
| 186 | T | Phosphorylation |
| 11145967 |
| 347 | S | Phosphorylation |
| 10958691 |
| 350 | T | Phosphorylation |
| 10958691 |
| 353 | S | Phosphorylation |
| 10958691 |
| 354 | T | Phosphorylation |
| 10958691 |
| 357 | S | Phosphorylation |
| 10958691 |
| 362 | T | Phosphorylation |
| 18566585 |
| 363 | T | Phosphorylation |
| 18566585 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CDK9_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulatestranscription."; Sabo A., Lusic M., Cereseto A., Giacca M.; Mol. Cell. Biol. 28:2201-2212(2008). Cited for: ACETYLATION AT LYS-44 AND LYS-48 BY PCAF/KAT2B AND GCN5/KAT2A, ENZYMEREGULATION BY ACETYLATION, AND SUBCELLULAR LOCATION. | |
| "Regulation of P-TEFb elongation complex activity by CDK9acetylation."; Fu J., Yoon H.-G., Qin J., Wong J.; Mol. Cell. Biol. 27:4641-4651(2007). Cited for: ACETYLATION AT LYS-44 BY P300/CBP, IDENTIFICATION IN COMPLEX WITHNCOR1; HEXIM1 AND HDAC3, AND MUTAGENESIS OF LYS-44. | |
| Phosphorylation | |
| Reference | PubMed |
| "Protein phosphatase-1 activates CDK9 by dephosphorylating Ser175."; Ammosova T., Obukhov Y., Kotelkin A., Breuer D., Beullens M.,Gordeuk V.R., Bollen M., Nekhai S.; PLoS ONE 6:E18985-E18985(2011). Cited for: DEPHOSPHORYLATION AT SER-175 BY PP1, AND MUTAGENESIS OF SER-175. | |
| "Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185; THR-186; SER-347;THR-350 AND SER-353, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27;SER-35; SER-43; SER-52; THR-54; THR-55 AND SER-56; (ISOFORM 2), ANDMASS SPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186; SER-347 ANDSER-353, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35;SER-52 AND SER-56 (ISOFORM 2), AND MASS SPECTROMETRY. | |
| "CDK9 autophosphorylation regulates high-affinity binding of the humanimmunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA."; Garber M.E., Mayall T.P., Suess E.M., Meisenhelder J., Thompson N.E.,Jones K.A.; Mol. Cell. Biol. 20:6958-6969(2000). Cited for: PHOSPHORYLATION BY PKA, AUTOPHOSPHORYLATION, PHOSPHORYLATION ATSER-347; THR-350; SER-353; THR-354 AND SER-357, INTERACTION WITH HIVTAT, AND MUTAGENESIS OF 347-SER--SER-357 AND ASP-167. | |
| "CDK inhibitors roscovitine and CR8 trigger Mcl-1 down-regulation andapoptotic cell death in neuroblastoma cells."; Bettayeb K., Baunbaek D., Delehouze C., Loaec N., Hole A.J.,Baumli S., Endicott J.A., Douc-Rasy S., Benard J., Oumata N.,Galons H., Meijer L.; Genes Cancer 1:369-380(2010). Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-330 IN COMPLEX WITH CCNT1;INHIBITORS ROSCOVITINE AND CR8, PHOSPHORYLATION AT THR-186, AND ENZYMEREGULATION. | |
| "Halogen bonds form the basis for selective P-TEFb inhibition byDRB."; Baumli S., Endicott J.A., Johnson L.N.; Chem. Biol. 17:931-936(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-330 IN COMPLEX WITHINHIBITOR DRB, AND PHOSPHORYLATION AT THR-186. | |
| "The structure of P-TEFb (CDK9/cyclin T1), its complex withflavopiridol and regulation by phosphorylation."; Baumli S., Lolli G., Lowe E.D., Troiani S., Rusconi L., Bullock A.N.,Debreczeni J.E., Knapp S., Johnson L.N.; EMBO J. 27:1907-1918(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 2-330 IN COMPLEX WITHINHIBITOR FLAVOPIRIDOL; ATP AND CCNT1, PHOSPHORYLATION AT THR-186SER347; THR362 AND THR363, AUTOPHOSPHORYLATION, AND MUTAGENESIS OFTHR-186. | |
| "Crystal structure of HIV-1 Tat complexed with human P-TEFb."; Tahirov T.H., Babayeva N.D., Varzavand K., Cooper J.J., Sedore S.C.,Price D.H.; Nature 465:747-751(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-345 IN COMPLEX WITH HIV-1TAT AND CCNT1, AND PHOSPHORYLATION AT THR-186. | |
| "Cdk9 T-loop phosphorylation is regulated by the calcium signalingpathway."; Ramakrishnan R., Rice A.P.; J. Cell. Physiol. 227:609-617(2012). Cited for: PHOSPHORYLATION AT THR-186, ENZYME REGULATION, DEGRADATION BYPROTEASOME, AND MUTAGENESIS OF THR-186. | |
| "Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop."; Wang Y., Dow E.C., Liang Y.Y., Ramakrishnan R., Liu H., Sung T.L.,Lin X., Rice A.P.; J. Biol. Chem. 283:33578-33584(2008). Cited for: PHOSPHORYLATION AT THR-186, AND DEPHOSPHORYLATION BY PPM1A AND PPM1B. | |
| "PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFbfor transcription in response to Ca2+ signaling."; Chen R., Liu M., Li H., Xue Y., Ramey W.N., He N., Ai N., Luo H.,Zhu Y., Zhou N., Zhou Q.; Genes Dev. 22:1356-1368(2008). Cited for: PHOSPHORYLATION AT THR-186, DEPHOSPHORYLATION BY PPP1CA, P-TEFB/7SKSNRNP COMPLEX, SUBUNIT, INTERACTION WITH BRD4, AND ENZYME REGULATION. | |
| "Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, AND MASSSPECTROMETRY. | |
| "Analysis of the large inactive P-TEFb complex indicates that itcontains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two P-TEFbmolecules containing Cdk9 phosphorylated at threonine 186."; Li Q., Price J.P., Byers S.A., Cheng D., Peng J., Price D.H.; J. Biol. Chem. 280:28819-28826(2005). Cited for: IDENTIFICATION IN INACTIVE 7SK SNRNP COMPLEX, AND PHOSPHORYLATION ATTHR-186. | |
