CCNT1_HUMAN - dbPTM
CCNT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNT1_HUMAN
UniProt AC O60563
Protein Name Cyclin-T1
Gene Name CCNT1
Organism Homo sapiens (Human).
Sequence Length 726
Subcellular Localization Nucleus .
Protein 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).; (Microbial infection) 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..
Protein Sequence MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESSSNLTSVEMLPGKRWLSSQPSFKLEPTQGHRTSENLALTGVDHSLPQDGSNAFISQKQNSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHHDSHSSVILKMPIEGSENPERPFLEKADKTALKMRIPVAGGDKAASSKPEEIKMRIKVHAAADKHNSVEDSVTKSREHKEKHKTHPSNHHHHHNHHSHKHSHSQLPVGTGNKRPGDPKHSSQTSNLAHKTYSLSSSFSSSSSTRKRGPSEETGGAVFDHPAKIAKSTKSSSLNFSFPSLPTMGQMPGHSSDTSGLSFSQPSCKTRVPHSKLDKGPTGANGHNTTQTIDYQDTVNMLHSLLSAQGVQPTQPTAFEFVRPYSDYLNPRSGGISSRSGNTDKPRPPPLPSEPPPPLPPLPK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
22PhosphorylationTREQLENSPSRRFGV
EHHHHHCCCHHHCCC		18.1927067055
33UbiquitinationRFGVDPDKELSYRQQ
HCCCCCCCHHHHHHH		66.98-
33UbiquitinationRFGVDPDKELSYRQQ
HCCCCCCCHHHHHHH		66.98-
33AcetylationRFGVDPDKELSYRQQ
HCCCCCCCHHHHHHH		66.9825953088
99UbiquitinationAKVEEQPKKLEHVIK
HHHHHCCHHHHHHHH		70.46-
100UbiquitinationKVEEQPKKLEHVIKV
HHHHCCHHHHHHHHH		66.83-
100UbiquitinationKVEEQPKKLEHVIKV
HHHHCCHHHHHHHHH		66.83-
106UbiquitinationKKLEHVIKVAHTCLH
HHHHHHHHHHHHCCC		32.07-
110PhosphorylationHVIKVAHTCLHPQES
HHHHHHHHCCCCCCC		13.66-
117PhosphorylationTCLHPQESLPDTRSE
HCCCCCCCCCCCCCH		39.7022817900
168UbiquitinationTQLVRASKDLAQTSY
HHHHHHCCHHHHCCE		56.63-
278PhosphorylationDRGTDEKTSEQTILN
CCCCCCCCCHHHHHH		35.13-
279PhosphorylationRGTDEKTSEQTILNM
CCCCCCCCHHHHHHH		38.48-
282PhosphorylationDEKTSEQTILNMISQ
CCCCCHHHHHHHHHC		24.31-
290PhosphorylationILNMISQSSSDTTIA
HHHHHHCCCCCCCHH		25.64-
292PhosphorylationNMISQSSSDTTIAGL
HHHHCCCCCCCHHHH		44.20-
307PhosphorylationMSMSTSTTSAVPSLP
HCCCCCCCCCCCCCC		17.92-
336PhosphorylationLPGKRWLSSQPSFKL
CCCCCCCCCCCCCCC		21.7026434776
337PhosphorylationPGKRWLSSQPSFKLE
CCCCCCCCCCCCCCC		43.8928857561
340PhosphorylationRWLSSQPSFKLEPTQ
CCCCCCCCCCCCCCC		27.6323401153
342SumoylationLSSQPSFKLEPTQGH
CCCCCCCCCCCCCCC		57.1728112733
342SumoylationLSSQPSFKLEPTQGH
CCCCCCCCCCCCCCC		57.17-
346PhosphorylationPSFKLEPTQGHRTSE
CCCCCCCCCCCCCCC		37.5026434776
351PhosphorylationEPTQGHRTSENLALT
CCCCCCCCCCCEEEC		34.4218691976
352PhosphorylationPTQGHRTSENLALTG
CCCCCCCCCCEEECC		25.1728555341
363PhosphorylationALTGVDHSLPQDGSN
EECCCCCCCCCCCCC		36.9628555341
376MethylationSNAFISQKQNSKSVP
CCCCCCCCCCCCCCC		44.66-
376AcetylationSNAFISQKQNSKSVP
CCCCCCCCCCCCCCC		44.6625953088
376UbiquitinationSNAFISQKQNSKSVP
CCCCCCCCCCCCCCC		44.66-
380AcetylationISQKQNSKSVPSAKV
CCCCCCCCCCCCCCC		64.1219387490
386AcetylationSKSVPSAKVSLKEYR
CCCCCCCCCCHHHHH		36.3719387490
386UbiquitinationSKSVPSAKVSLKEYR
CCCCCCCCCCHHHHH		36.37-
388PhosphorylationSVPSAKVSLKEYRAK
CCCCCCCCHHHHHHH		32.7723186163
390AcetylationPSAKVSLKEYRAKHA
CCCCCCHHHHHHHHH		45.2319608861
390UbiquitinationPSAKVSLKEYRAKHA
CCCCCCHHHHHHHHH		45.2319608861
390MethylationPSAKVSLKEYRAKHA
CCCCCCHHHHHHHHH		45.2319608861
404AcetylationAEELAAQKRQLENME
HHHHHHHHHHHHHHH		37.0719387490
4042-HydroxyisobutyrylationAEELAAQKRQLENME
HHHHHHHHHHHHHHH		37.07-
404UbiquitinationAEELAAQKRQLENME
HHHHHHHHHHHHHHH		37.07-
415SumoylationENMEANVKSQYAYAA
HHHHHHHHHHHHHHH		31.4828112733
418PhosphorylationEANVKSQYAYAAQNL
HHHHHHHHHHHHHHH		14.5227642862
420PhosphorylationNVKSQYAYAAQNLLS
HHHHHHHHHHHHHHH		9.49-
431PhosphorylationNLLSHHDSHSSVILK
HHHHCCCCCCEEEEE		22.4027080861
433PhosphorylationLSHHDSHSSVILKMP
HHCCCCCCEEEEECC		30.1927080861
457AcetylationPFLEKADKTALKMRI
CCHHHHCCCEECCCC		40.3225953088
471AcetylationIPVAGGDKAASSKPE
CCCCCCCHHHCCCHH		49.4825953088
474PhosphorylationAGGDKAASSKPEEIK
CCCCHHHCCCHHHHH		43.6929083192
475PhosphorylationGGDKAASSKPEEIKM
CCCHHHCCCHHHHHH		47.7229083192
476AcetylationGDKAASSKPEEIKMR
CCHHHCCCHHHHHHH		54.6926051181
481UbiquitinationSSKPEEIKMRIKVHA
CCCHHHHHHHHHHHH		25.96-
481SumoylationSSKPEEIKMRIKVHA
CCCHHHHHHHHHHHH		25.9628112733
492AcetylationKVHAAADKHNSVEDS
HHHHCHHCCCCHHHH		39.7016916647
495PhosphorylationAAADKHNSVEDSVTK
HCHHCCCCHHHHHHC		26.9728355574
499PhosphorylationKHNSVEDSVTKSREH
CCCCHHHHHHCCHHH		20.4120068231
529PhosphorylationNHHSHKHSHSQLPVG
CCCCCCCCCCCCCCC		29.63-
531PhosphorylationHSHKHSHSQLPVGTG
CCCCCCCCCCCCCCC		36.1128555341
537PhosphorylationHSQLPVGTGNKRPGD
CCCCCCCCCCCCCCC		37.5028555341
546UbiquitinationNKRPGDPKHSSQTSN
CCCCCCCCCCCCCCC		61.94-
549PhosphorylationPGDPKHSSQTSNLAH
CCCCCCCCCCCCCCH		36.88-
560PhosphorylationNLAHKTYSLSSSFSS
CCCHHEEECCCCCCC		27.3222496350
562PhosphorylationAHKTYSLSSSFSSSS
CHHEEECCCCCCCCC		20.2828152594
563PhosphorylationHKTYSLSSSFSSSSS
HHEEECCCCCCCCCC		40.4728152594
564PhosphorylationKTYSLSSSFSSSSST
HEEECCCCCCCCCCC		26.2728152594
566PhosphorylationYSLSSSFSSSSSTRK
EECCCCCCCCCCCCC		31.1228152594
567PhosphorylationSLSSSFSSSSSTRKR
ECCCCCCCCCCCCCC		32.0328152594
568PhosphorylationLSSSFSSSSSTRKRG
CCCCCCCCCCCCCCC		27.4028152594
569PhosphorylationSSSFSSSSSTRKRGP
CCCCCCCCCCCCCCC		37.3628152594
570PhosphorylationSSFSSSSSTRKRGPS
CCCCCCCCCCCCCCC		33.8928152594
571PhosphorylationSFSSSSSTRKRGPSE
CCCCCCCCCCCCCCC		42.0028152594
577PhosphorylationSTRKRGPSEETGGAV
CCCCCCCCCCCCCCC		51.3821082442
580PhosphorylationKRGPSEETGGAVFDH
CCCCCCCCCCCCCCC		36.5423186163
590UbiquitinationAVFDHPAKIAKSTKS
CCCCCHHHHCCCCCC		47.88-
629PhosphorylationGLSFSQPSCKTRVPH
CCCCCCCCCCCCCCC		22.17-
638AcetylationKTRVPHSKLDKGPTG
CCCCCCHHCCCCCCC		58.6425953088
690PhosphorylationFVRPYSDYLNPRSGG
EECCHHHHCCCCCCC		11.48-
705PhosphorylationISSRSGNTDKPRPPP
CCCCCCCCCCCCCCC		49.2628555341
707AcetylationSRSGNTDKPRPPPLP
CCCCCCCCCCCCCCC		40.6726051181
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
564SPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNT1_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 CCNT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRN_HUMANGRNphysical
12588988
CDK9_HUMANCDK9physical
15107825
MYC_HUMANMYCphysical
12944920
CDK9_HUMANCDK9physical
12944466
MDFIC_HUMANMDFICphysical
12944466
AHR_HUMANAHRphysical
12917420
CDK9_HUMANCDK9physical
12832472
PML_HUMANPMLphysical
12727882
CDK9_HUMANCDK9physical
12588988
HTSF1_HUMANHTATSF1physical
11780068
PURA_HUMANPURAphysical
11730934
CDK9_HUMANCDK9physical
10574912
CDK9_HUMANCDK9physical
9499409
CDK9_HUMANCDK9physical
10958691
BRD4_HUMANBRD4physical
16109376
AFF1_HUMANAFF1physical
19956800
CDK9_HUMANCDK9physical
19818711
MAX_HUMANMAXphysical
17700062
CDK9_HUMANCDK9physical
17700062
KDM1B_HUMANKDM1Bphysical
20670891
NSD3_HUMANWHSC1L1physical
20670891
CDK9_HUMANCDK9physical
15546612
AFF1_HUMANAFF1physical
21030982
TAF7_HUMANTAF7physical
18391197
RPB1_HUMANPOLR2Aphysical
12591939
T2FA_HUMANGTF2F1physical
12591939
CDK9_HUMANCDK9physical
20305087
TAT_HV1H2tatgenetic
16615932
UBE2A_HUMANUBE2Aphysical
22592529
CDK9_HUMANCDK9physical
15528190
CDK9_HUMANCDK9physical
18566585
CDK9_HUMANCDK9physical
22939629
LEO1_HUMANLEO1physical
22939629
TAF1_HUMANTAF1physical
22939629
TBB4B_HUMANTUBB4Bphysical
22939629
GNAI3_HUMANGNAI3physical
22939629
RS9_HUMANRPS9physical
22939629
SMAP_HUMANC11orf58physical
22939629
TP53B_HUMANTP53BP1physical
22939629
CDK9_HUMANCDK9physical
11282025
TAT_HV1H2tatphysical
11282025
CDK9_HUMANCDK9physical
14627702
TAT_HV1H2tatphysical
12753906
CCNT1_HUMANCCNT1physical
12753906
ESR1_HUMANESR1physical
15940264
TAT_HV1H2tatphysical
9872325
CDK9_HUMANCDK9physical
12115727
CDK9_HUMANCDK9physical
9491887
HEXI1_HUMANHEXIM1physical
15201869
SPT5H_HUMANSUPT5Hphysical
15201869
LARP7_HUMANLARP7physical
18483487
HEXI1_HUMANHEXIM1physical
18483487
CDK9_HUMANCDK9physical
18483487
KAT2B_HUMANKAT2Bphysical
12486002
TAT_HV1H2tatphysical
12486002
P73_HUMANTP73physical
16135803
TAT_HV1H2tatphysical
12887902
HEXI1_HUMANHEXIM1physical
15855166
TAT_HV1H2tatphysical
15855166
Drug and Disease Associations
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.
Regulatory Network of CCNT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-390 AND LYS-492, AND MASSSPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-492, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-117 AND SER-340, 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 SER-495 AND SER-577, ANDMASS SPECTROMETRY.

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