CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000960
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-T1 
Protein Synonyms/Alias
 CycT1; Cyclin-T 
Gene Name
 CCNT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
380ISQKQNSKSVPSAKVacetylation[1]
386SKSVPSAKVSLKEYRacetylation[1]
390PSAKVSLKEYRAKHAacetylation[1, 2]
404AEELAAQKRQLENMEacetylation[1]
476GDKAASSKPEEIKMRacetylation[3]
492KVHAAADKHNSVEDSacetylation[2, 4, 5, 6]
Reference
 [1] Acetylation of cyclin T1 regulates the equilibrium between active and inactive P-TEFb in cells.
 Cho S, Schroeder S, Kaehlcke K, Kwon HS, Pedal A, Herker E, Schnoelzer M, Ott M.
 EMBO J. 2009 May 20;28(10):1407-17. [PMID: 19387490]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [5] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which is proposed to facilitate the transition from abortive to productive elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). In case of HIV or SIV infections, binds to the transactivation domain of the viral nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA). Serves as an essential cofactor for Tat, by promoting RNA Pol II activation, allowing transcription of viral genes. 
Sequence Annotation
 MOTIF 253 270 Nuclear localization signal, and
 MOD_RES 117 117 Phosphoserine.
 MOD_RES 340 340 Phosphoserine.
 MOD_RES 390 390 N6-acetyllysine.
 MOD_RES 495 495 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 MOD_RES 577 577 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil; Complete proteome; Cyclin; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 726 AA 
Protein Sequence
MEGERKNNNK RWYFTREQLE NSPSRRFGVD PDKELSYRQQ AANLLQDMGQ RLNVSQLTIN 60
TAIVYMHRFY MIQSFTQFPG NSVAPAALFL AAKVEEQPKK LEHVIKVAHT CLHPQESLPD 120
TRSEAYLQQV QDLVILESII LQTLGFELTI DHPHTHVVKC TQLVRASKDL AQTSYFMATN 180
SLHLTTFSLQ YTPPVVACVC IHLACKWSNW EIPVSTDGKH WWEYVDATVT LELLDELTHE 240
FLQILEKTPN RLKRIWNWRA CEAAKKTKAD DRGTDEKTSE QTILNMISQS SSDTTIAGLM 300
SMSTSTTSAV PSLPVSEESS SNLTSVEMLP GKRWLSSQPS FKLEPTQGHR TSENLALTGV 360
DHSLPQDGSN AFISQKQNSK SVPSAKVSLK EYRAKHAEEL AAQKRQLENM EANVKSQYAY 420
AAQNLLSHHD SHSSVILKMP IEGSENPERP FLEKADKTAL KMRIPVAGGD KAASSKPEEI 480
KMRIKVHAAA DKHNSVEDSV TKSREHKEKH KTHPSNHHHH HNHHSHKHSH SQLPVGTGNK 540
RPGDPKHSSQ TSNLAHKTYS LSSSFSSSSS TRKRGPSEET GGAVFDHPAK IAKSTKSSSL 600
NFSFPSLPTM GQMPGHSSDT SGLSFSQPSC KTRVPHSKLD KGPTGANGHN TTQTIDYQDT 660
VNMLHSLLSA QGVQPTQPTA FEFVRPYSDY LNPRSGGISS RSGNTDKPRP PPLPSEPPPP 720
LPPLPK 726 
Gene Ontology
 GO:0008024; C:positive transcription elongation factor complex b; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IDA:MGI.
 GO:0017069; F:snRNA binding; IEA:Compara.
 GO:0044212; F:transcription regulatory region DNA binding; IEA:Compara.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006468; P:protein phosphorylation; IPI:MGI.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR013763; Cyclin-like.
 IPR015429; Cyclin_C/H/T/L.
 IPR006671; Cyclin_N. 
Pfam
 PF00134; Cyclin_N 
SMART
 SM00385; CYCLIN 
PROSITE
 PS00292; CYCLINS 
PRINTS