CCNT2_HUMAN - dbPTM
CCNT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNT2_HUMAN
UniProt AC O60583
Protein Name Cyclin-T2 {ECO:0000250|UniProtKB:Q7TQK0}
Gene Name CCNT2 {ECO:0000312|HGNC:HGNC:1600}
Organism Homo sapiens (Human).
Sequence Length 730
Subcellular Localization Cytoplasm, perinuclear region . Nucleus . Nucleus in differentiating cells.
Protein Description Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II). [PubMed: 9499409]
Protein Sequence MASGRGASSRWFFTREQLENTPSRRCGVEADKELSCRQQAANLIQEMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNKNIISSTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVILETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPNRLKKIRNWRANQAARKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPTNPSFQKPSTSAFPAPVPLNSGNISVQDSHTSDNLSMLATGMPSTSYGLSSHQEWPQHQDSARTEQLYSQKQETSLSGSQYNINFQQGPSISLHSGLHHRPDKISDHSSVKQEYTHKAGSSKHHGPISTTPGIIPQKMSLDKYREKRKLETLDLDVRDHYIAAQVEQQHKQGQSQAASSSSVTSPIKMKIPIANTEKYMADKKEKSGSLKLRIPIPPTDKSASKEELKMKIKVSSSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPSSRHHTSSHKHSHSHSGSSSGGSKHSADGIPPTVLRSPVGLSSDGISSSSSSSRKRLHVNDASHNHHSKMSKSSKSSGSSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVETNGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM
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
3Phosphorylation-----MASGRGASSR
-----CCCCCCCCHH		27.9423403867
8PhosphorylationMASGRGASSRWFFTR
CCCCCCCCHHCCCCH		24.22-
9PhosphorylationASGRGASSRWFFTRE
CCCCCCCHHCCCCHH		32.75-
14PhosphorylationASSRWFFTREQLENT
CCHHCCCCHHHHCCC		24.67-
32UbiquitinationRCGVEADKELSCRQQ
CCCCHHCHHHHHHHH		68.55-
73PhosphorylationHRFYMHHSFTKFNKN
HHHHHHCCCCCCCHH		21.6724719451
99UbiquitinationKVEEQARKLEHVIKV
HHHHHHHHHHHHHHH		62.33-
286PhosphorylationGSSLVQNSILVDSVT
CCHHHCCCEEEECCC		10.5422210691
300PhosphorylationTGVPTNPSFQKPSTS
CCCCCCCCCCCCCCC		42.2422210691
407SumoylationISDHSSVKQEYTHKA
CCCCHHCCHHHCCCC		39.08-
407SumoylationISDHSSVKQEYTHKA
CCCCHHCCHHHCCCC		39.0828112733
424PhosphorylationSKHHGPISTTPGIIP
CCCCCCCCCCCCCCC		29.3923403867
425PhosphorylationKHHGPISTTPGIIPQ
CCCCCCCCCCCCCCC		37.4223403867
426PhosphorylationHHGPISTTPGIIPQK
CCCCCCCCCCCCCCC		16.8423403867
456PhosphorylationDLDVRDHYIAAQVEQ
CCCHHHHHHHHHHHH		9.1327642862
470PhosphorylationQQHKQGQSQAASSSS
HHHHHCCCHHCCCCC		28.7223403867
474PhosphorylationQGQSQAASSSSVTSP
HCCCHHCCCCCCCCC		33.4922167270
475PhosphorylationGQSQAASSSSVTSPI
CCCHHCCCCCCCCCC		23.1622167270
476PhosphorylationQSQAASSSSVTSPIK
CCHHCCCCCCCCCCE		26.7422167270
477PhosphorylationSQAASSSSVTSPIKM
CHHCCCCCCCCCCEE		31.2129255136
479PhosphorylationAASSSSVTSPIKMKI
HCCCCCCCCCCEEEE		30.6329255136
480PhosphorylationASSSSVTSPIKMKIP
CCCCCCCCCCEEEEC		23.6019664994
485UbiquitinationVTSPIKMKIPIANTE
CCCCCEEEECCCCCH		40.09-
493AcetylationIPIANTEKYMADKKE
ECCCCCHHHCCCCCC		37.9825953088
502PhosphorylationMADKKEKSGSLKLRI
CCCCCCCCCCCEEEC		34.40-
504PhosphorylationDKKEKSGSLKLRIPI
CCCCCCCCCEEECCC		29.4424719451
514PhosphorylationLRIPIPPTDKSASKE
EECCCCCCCCCCCHH		51.1820068231
517PhosphorylationPIPPTDKSASKEELK
CCCCCCCCCCHHHHC		40.3526437602
519PhosphorylationPPTDKSASKEELKMK
CCCCCCCCHHHHCCE		47.9224719451
520AcetylationPTDKSASKEELKMKI
CCCCCCCHHHHCCEE		55.7322970799
530PhosphorylationLKMKIKVSSSERHSS
HCCEEEECCCCCCCC		24.1221406692
531PhosphorylationKMKIKVSSSERHSSS
CCEEEECCCCCCCCC		38.9221406692
532PhosphorylationMKIKVSSSERHSSSD
CEEEECCCCCCCCCC		31.0129514088
536PhosphorylationVSSSERHSSSDEGSG
ECCCCCCCCCCCCCC		37.4525884760
537PhosphorylationSSSERHSSSDEGSGK
CCCCCCCCCCCCCCC		35.3730576142
538PhosphorylationSSERHSSSDEGSGKS
CCCCCCCCCCCCCCC		42.5730576142
542PhosphorylationHSSSDEGSGKSKHSS
CCCCCCCCCCCCCCC		40.7928985074
545PhosphorylationSDEGSGKSKHSSPHI
CCCCCCCCCCCCCCC		38.8421406692
548PhosphorylationGSGKSKHSSPHISRD
CCCCCCCCCCCCCCC		49.6730266825
549PhosphorylationSGKSKHSSPHISRDH
CCCCCCCCCCCCCCH		21.8830266825
553PhosphorylationKHSSPHISRDHKEKH
CCCCCCCCCCHHHHH		28.7330266825
580PhosphorylationHKHSHSHSGSSSGGS
CCCCCCCCCCCCCCC		43.3030576142
582PhosphorylationHSHSHSGSSSGGSKH
CCCCCCCCCCCCCCC		25.0930576142
584PhosphorylationHSHSGSSSGGSKHSA
CCCCCCCCCCCCCCC		49.2030576142
590PhosphorylationSSGGSKHSADGIPPT
CCCCCCCCCCCCCCC		31.6219664994
597PhosphorylationSADGIPPTVLRSPVG
CCCCCCCCEECCCCC		27.1519664994
601PhosphorylationIPPTVLRSPVGLSSD
CCCCEECCCCCCCCC		21.5619664994
606PhosphorylationLRSPVGLSSDGISSS
ECCCCCCCCCCCCCC		22.0623927012
607PhosphorylationRSPVGLSSDGISSSS
CCCCCCCCCCCCCCC		44.9223927012
611PhosphorylationGLSSDGISSSSSSSR
CCCCCCCCCCCCCCC		29.6925002506
612PhosphorylationLSSDGISSSSSSSRK
CCCCCCCCCCCCCCC		32.1125002506
613PhosphorylationSSDGISSSSSSSRKR
CCCCCCCCCCCCCCC		27.7025002506
614PhosphorylationSDGISSSSSSSRKRL
CCCCCCCCCCCCCCE		35.8725002506
615PhosphorylationDGISSSSSSSRKRLH
CCCCCCCCCCCCCEE		33.9926434776
616PhosphorylationGISSSSSSSRKRLHV
CCCCCCCCCCCCEEC		35.7926434776
617PhosphorylationISSSSSSSRKRLHVN
CCCCCCCCCCCEECC		43.7126434776
635 (in isoform 2)Phosphorylation-32.8720068231
637 (in isoform 2)Phosphorylation-35.3720068231
637PhosphorylationHHSKMSKSSKSSGSS
CCCCCCCCCCCCCCC		35.3729396449
638PhosphorylationHSKMSKSSKSSGSSS
CCCCCCCCCCCCCCC		40.0520068231
638 (in isoform 2)Phosphorylation-40.0520068231
640PhosphorylationKMSKSSKSSGSSSSS
CCCCCCCCCCCCCCC		41.7120068231
640 (in isoform 2)Phosphorylation-41.7120068231
641 (in isoform 2)Phosphorylation-46.5620068231
641PhosphorylationMSKSSKSSGSSSSSS
CCCCCCCCCCCCCCC		46.5629396449
643PhosphorylationKSSKSSGSSSSSSSS
CCCCCCCCCCCCCHH		29.0629396449
644PhosphorylationSSKSSGSSSSSSSSV
CCCCCCCCCCCCHHH		37.4529396449
645PhosphorylationSKSSGSSSSSSSSVK
CCCCCCCCCCCHHHH		35.6229396449
646PhosphorylationKSSGSSSSSSSSVKQ
CCCCCCCCCCHHHHH		35.8729396449
647PhosphorylationSSGSSSSSSSSVKQY
CCCCCCCCCHHHHHH		35.8729396449
663 (in isoform 2)Phosphorylation-33.4417192257
707PhosphorylationNHEYSTSSQHMDYKD
CCCCCCCCCCCCHHH		24.9728555341
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

Oops, there are no upstream regulatory protein records of CCNT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNT2_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 CCNT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
12037672
CDK9_HUMANCDK9physical
9499409
PKN1_HUMANPKN1physical
16331689
CDK9_HUMANCDK9physical
16331689
SPT5H_HUMANSUPT5Hphysical
15201869
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 CCNT2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND MASSSPECTROMETRY.
"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-475; SER-476; SER-477;THR-479; SER-480; SER-536; SER-537; SER-538; SER-542; SER-549;SER-590; THR-597 AND SER-601, PHOSPHORYLATION [LARGE SCALE ANALYSIS]AT SER-663 (ISOFORM 2), AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND MASSSPECTROMETRY.
"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-480; SER-549 ANDSER-601, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 (ISOFORM2), AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND MASSSPECTROMETRY.

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