CCNK_HUMAN - dbPTM
CCNK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCNK_HUMAN
UniProt AC O75909
Protein Name Cyclin-K
Gene Name CCNK
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Nucleus .
Protein Description Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A)..
Protein Sequence MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQVQQSQPSQSSEPSQPQQKDPQQPAQQQQPAQQPKKPSPQPSSPRQVKRAVVVSPKEENKAAEPPPPKIPKIETTHPPLPPAHPPPDRKPPLAAALGEAEPPGPVDATDLPKVQIPPPAHPAPVHQPPPLPHRPPPPPPSSYMTGMSTTSSYMSGEGYQSLQSMMKTEGPSYGALPPAYGPPAHLPYHPHVYPPNPPPPPVPPPPASFPPPAIPPPTPGYPPPPPTYNPNFPPPPPRLPPTHAVPPHPPPGLGLPPASYPPPAVPPGGQPPVPPPIPPPGMPPVGGLGRAAWMR
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
8PhosphorylationMKENKENSSPSVTSA
CCCCCCCCCCCCCCC		44.7223401153
9PhosphorylationKENKENSSPSVTSAN
CCCCCCCCCCCCCCC		32.5423401153
11PhosphorylationNKENSSPSVTSANLD
CCCCCCCCCCCCCCC		39.7222167270
13PhosphorylationENSSPSVTSANLDHT
CCCCCCCCCCCCCCC		26.8522167270
14PhosphorylationNSSPSVTSANLDHTK
CCCCCCCCCCCCCCC		17.0122167270
20PhosphorylationTSANLDHTKPCWYWD
CCCCCCCCCCCCCCC		36.0323403867
25PhosphorylationDHTKPCWYWDKKDLA
CCCCCCCCCCHHHHC		15.5023403867
34PhosphorylationDKKDLAHTPSQLEGL
CHHHHCCCHHHHCCC		21.0126074081
36PhosphorylationKDLAHTPSQLEGLDP
HHHCCCHHHHCCCCH		48.8626074081
166 (in isoform 3)Ubiquitination-45.3621890473
166 (in isoform 2)Ubiquitination-45.3621890473
166 (in isoform 1)Ubiquitination-45.3621890473
166UbiquitinationHPYQFLLKYAKQLKG
CHHHHHHHHHHHHCC		45.36-
166 (in isoform 4)Ubiquitination-45.3621890473
226PhosphorylationKFEIQEWTSKPMYRR
HHHHHHHCCCHHHHH		26.5625690035
227PhosphorylationFEIQEWTSKPMYRRW
HHHHHHCCCHHHHHH		35.5225690035
231PhosphorylationEWTSKPMYRRWWEQF
HHCCCHHHHHHHHHH		12.9328509920
324PhosphorylationAQQPKKPSPQPSSPR
CCCCCCCCCCCCCHH		45.0829255136
328PhosphorylationKKPSPQPSSPRQVKR
CCCCCCCCCHHHCEE		47.9629255136
329PhosphorylationKPSPQPSSPRQVKRA
CCCCCCCCHHHCEEE		30.6829255136
340O-linked_GlycosylationVKRAVVVSPKEENKA
CEEEEECCHHHHCCC		20.7430379171
340 (in isoform 1)Phosphorylation-20.7427107777
340PhosphorylationVKRAVVVSPKEENKA
CEEEEECCHHHHCCC		20.7429255136
426PhosphorylationRPPPPPPSSYMTGMS
CCCCCCCHHHCCCCC		39.6224043423
427PhosphorylationPPPPPPSSYMTGMST
CCCCCCHHHCCCCCC		25.3824043423
428PhosphorylationPPPPPSSYMTGMSTT
CCCCCHHHCCCCCCC		11.7524043423
430PhosphorylationPPPSSYMTGMSTTSS
CCCHHHCCCCCCCCC		22.8424043423
433PhosphorylationSSYMTGMSTTSSYMS
HHHCCCCCCCCCCCC		29.8524043423
434PhosphorylationSYMTGMSTTSSYMSG
HHCCCCCCCCCCCCC		23.0824043423
435PhosphorylationYMTGMSTTSSYMSGE
HCCCCCCCCCCCCCC		14.3624043423
436PhosphorylationMTGMSTTSSYMSGEG
CCCCCCCCCCCCCCC		21.4024043423
437PhosphorylationTGMSTTSSYMSGEGY
CCCCCCCCCCCCCCH		23.8224043423
438PhosphorylationGMSTTSSYMSGEGYQ
CCCCCCCCCCCCCHH		8.6224043423
440PhosphorylationSTTSSYMSGEGYQSL
CCCCCCCCCCCHHHH		26.0124043423
444PhosphorylationSYMSGEGYQSLQSMM
CCCCCCCHHHHHHHH		7.2224043423
446PhosphorylationMSGEGYQSLQSMMKT
CCCCCHHHHHHHHHC		21.6424043423
449PhosphorylationEGYQSLQSMMKTEGP
CCHHHHHHHHHCCCC		26.5724043423
580MethylationLGRAAWMR-------
CCCCHHCC-------		32.46-
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
-KUbiquitinationE3 ubiquitin ligaseDDB1Q16531
PMID:32494016
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCNK_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 CCNK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
T22D4_HUMANTSC22D4physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
NECA2_HUMANNECAB2physical
16189514
USBP1_HUMANUSHBP1physical
16189514
FBLN4_HUMANEFEMP2physical
16189514
KCNRG_HUMANKCNRGphysical
16189514
RFX6_HUMANRFX6physical
16189514
RBPMS_HUMANRBPMSphysical
16189514
CEP76_HUMANCEP76physical
16189514
RHXF2_HUMANRHOXF2physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
HM20A_HUMANHMG20Aphysical
16189514
RPB1_HUMANPOLR2Aphysical
9632813
CDK9_HUMANCDK9physical
10574912
CDK12_HUMANCDK12physical
22939629
NDC80_HUMANNDC80physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
LZTS2_HUMANLZTS2physical
25416956
CDK1_HUMANCDK1physical
26344197
CDK12_HUMANCDK12physical
26344197
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 CCNK_HUMAN

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Related Literatures of Post-Translational Modification
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-324; SER-328 ANDSER-340, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, 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-9; SER-324; SER-329 ANDSER-340, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND MASSSPECTROMETRY.
"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-324 AND SER-329, ANDMASS SPECTROMETRY.

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