CDK3_HUMAN - dbPTM
CDK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK3_HUMAN
UniProt AC Q00526
Protein Name Cyclin-dependent kinase 3
Gene Name CDK3
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization
Protein Description Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S cell cycle transitions. Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1-independent manner..
Protein Sequence MDMFQKVEKIGEGTYGVVYKAKNRETGQLVALKKIRLDLEMEGVPSTAIREISLLKELKHPNIVRLLDVVHNERKLYLVFEFLSQDLKKYMDSTPGSELPLHLIKSYLFQLLQGVSFCHSHRVIHRDLKPQNLLINELGAIKLADFGLARAFGVPLRTYTHEVVTLWYRAPEILLGSKFYTTAVDIWSIGCIFAEMVTRKALFPGDSEIDQLFRIFRMLGTPSEDTWPGVTQLPDYKGSFPKWTRKGLEEIVPNLEPEGRDLLMQLLQYDPSQRITAKTALAHPYFSSPEPSPAARQYVLQRFRH
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
6Ubiquitination--MDMFQKVEKIGEG
--CCCHHHHEECCCC		40.8922817900
9UbiquitinationDMFQKVEKIGEGTYG
CCHHHHEECCCCCCE		60.0221890473
14PhosphorylationVEKIGEGTYGVVYKA
HEECCCCCCEEEEEE		16.8919664994
15PhosphorylationEKIGEGTYGVVYKAK
EECCCCCCEEEEEEE		20.8419664994
19PhosphorylationEGTYGVVYKAKNRET
CCCCEEEEEEECCCC		11.6522167270
33UbiquitinationTGQLVALKKIRLDLE
CCCEEEEEEEECCEE		36.10-
37UbiquitinationVALKKIRLDLEMEGV
EEEEEEECCEECCCC		11.3921906983
46PhosphorylationLEMEGVPSTAIREIS
EECCCCCHHHHHHHH		28.2322210691
47PhosphorylationEMEGVPSTAIREISL
ECCCCCHHHHHHHHH		21.7522210691
53PhosphorylationSTAIREISLLKELKH
HHHHHHHHHHHHCCC		23.9324719451
59UbiquitinationISLLKELKHPNIVRL
HHHHHHCCCCCEEHH		59.10-
158PhosphorylationAFGVPLRTYTHEVVT
HHCCCCCCCCCCEEE		40.2222167270
159PhosphorylationFGVPLRTYTHEVVTL
HCCCCCCCCCCEEEH		10.3222167270
160PhosphorylationGVPLRTYTHEVVTLW
CCCCCCCCCCEEEHE		15.7922167270
165PhosphorylationTYTHEVVTLWYRAPE
CCCCCEEEHEEECCH		19.4228152594
168PhosphorylationHEVVTLWYRAPEILL
CCEEEHEEECCHHHH		10.46-
181PhosphorylationLLGSKFYTTAVDIWS
HHCCCCCCHHHHHHH		16.0624719451
182PhosphorylationLGSKFYTTAVDIWSI
HCCCCCCHHHHHHHH		17.1924719451
198PhosphorylationCIFAEMVTRKALFPG
HHHHHHHHHHHHCCC		25.7424719451
207PhosphorylationKALFPGDSEIDQLFR
HHHCCCCHHHHHHHH		42.2217192257
221PhosphorylationRIFRMLGTPSEDTWP
HHHHHHCCCCCCCCC		21.4928851738
226PhosphorylationLGTPSEDTWPGVTQL
HCCCCCCCCCCCCCC		29.5228851738
231PhosphorylationEDTWPGVTQLPDYKG
CCCCCCCCCCCCCCC		30.2428851738
236PhosphorylationGVTQLPDYKGSFPKW
CCCCCCCCCCCCCHH		18.47-
239PhosphorylationQLPDYKGSFPKWTRK
CCCCCCCCCCHHHHC		33.9328851738
272PhosphorylationQLLQYDPSQRITAKT
HHHCCCHHHCCCHHH		29.23-
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 CDK3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK3_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 CDK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD5R1_HUMANCDK5R1physical
22654103
A4_HUMANAPPphysical
21832049
RB_HUMANRB1physical
9190208
CCNE2_HUMANCCNE2physical
9840943
RB_HUMANRB1physical
15084261
PPARA_HUMANPPARAphysical
21988832
CDN1A_HUMANCDKN1Aphysical
23602568
CCNA2_HUMANCCNA2physical
23602568
CDN1B_HUMANCDKN1Bphysical
23602568
CCNE1_HUMANCCNE1physical
23602568
STIP1_HUMANSTIP1physical
23602568
SKP2_HUMANSKP2physical
23602568
CKS1_HUMANCKS1Bphysical
23602568
SKP1_HUMANSKP1physical
23602568
EF1A2_HUMANEEF1A2physical
23602568
HS90A_HUMANHSP90AA1physical
26186194
HS90B_HUMANHSP90AB1physical
26186194
HS71L_HUMANHSPA1Lphysical
26186194
CDT1_HUMANCDT1physical
26186194
FKBP5_HUMANFKBP5physical
26186194
GEMI_HUMANGMNNphysical
26186194
CCNE1_HUMANCCNE1physical
26186194
CCNE2_HUMANCCNE2physical
26186194
HSP74_HUMANHSPA4physical
26186194
SKP2_HUMANSKP2physical
26186194
AKT2_HUMANAKT2physical
26186194
CDN1B_HUMANCDKN1Bphysical
26186194
CDN1C_HUMANCDKN1Cphysical
26186194
CDN1A_HUMANCDKN1Aphysical
26186194
CKS1_HUMANCKS1Bphysical
26186194
CKS2_HUMANCKS2physical
26186194
CDT1_HUMANCDT1physical
28514442
CCNE1_HUMANCCNE1physical
28514442
CCNE2_HUMANCCNE2physical
28514442
CDN1B_HUMANCDKN1Bphysical
28514442
CDN1C_HUMANCDKN1Cphysical
28514442
GEMI_HUMANGMNNphysical
28514442
CDN1A_HUMANCDKN1Aphysical
28514442
SKP2_HUMANSKP2physical
28514442
HS90A_HUMANHSP90AA1physical
28514442
CKS2_HUMANCKS2physical
28514442
AKT2_HUMANAKT2physical
28514442
HS90B_HUMANHSP90AB1physical
28514442
FKBP5_HUMANFKBP5physical
28514442
HSP7C_HUMANHSPA8physical
28514442
CCNB1_HUMANCCNB1physical
28514442
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 CDK3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-207, 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 THR-14; TYR-15; TYR-19 ANDTHR-158, 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 THR-14; TYR-15; TYR-19 ANDTHR-160, AND MASS 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 TYR-15; TYR-159 AND THR-160,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159 AND THR-160, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, 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 THR-14 AND TYR-15, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory