CDCA3_HUMAN - dbPTM
CDCA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDCA3_HUMAN
UniProt AC Q99618
Protein Name Cell division cycle-associated protein 3
Gene Name CDCA3
Organism Homo sapiens (Human).
Sequence Length 268
Subcellular Localization Cytoplasm, cytosol.
Protein Description F-box-like protein which is required for entry into mitosis. Acts by participating in E3 ligase complexes that mediate the ubiquitination and degradation of WEE1 kinase at G2/M phase (By similarity)..
Protein Sequence MGSAKSVPVTPARPPPHNKHLARVADPRSPSAGILRTPIQVESSPQPGLPAGEQLEGLKHAQDSDPRSPTLGIARTPMKTSSGDPPSPLVKQLSEVFETEDSKSNLPPEPVLPPEAPLSSELDLPLGTQLSVEEQMPPWNQTEFPSKQVFSKEEARQPTETPVASQSSDKPSRDPETPRSSGSMRNRWKPNSSKVLGRSPLTILQDDNSPGTLTLRQGKRPSPLSENVSELKEGAILGTGRLLKTGGRAWEQGQDHDKENQHFPLVES
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
6Phosphorylation--MGSAKSVPVTPAR
--CCCCCCCCCCCCC		31.2229396449
10PhosphorylationSAKSVPVTPARPPPH
CCCCCCCCCCCCCCC		12.7428985074
28MethylationLARVADPRSPSAGIL
CHHHCCCCCCCCCEE		62.84-
29PhosphorylationARVADPRSPSAGILR
HHHCCCCCCCCCEEC		28.7029255136
31PhosphorylationVADPRSPSAGILRTP
HCCCCCCCCCEECCC		40.1330266825
36MethylationSPSAGILRTPIQVES
CCCCCEECCCEEEEC		36.21-
37PhosphorylationPSAGILRTPIQVESS
CCCCEECCCEEEECC		22.6930266825
43PhosphorylationRTPIQVESSPQPGLP
CCCEEEECCCCCCCC		48.7630266825
44PhosphorylationTPIQVESSPQPGLPA
CCEEEECCCCCCCCC		17.6630266825
44O-linked_GlycosylationTPIQVESSPQPGLPA
CCEEEECCCCCCCCC		17.66OGP
59UbiquitinationGEQLEGLKHAQDSDP
HHHCCCCCCCCCCCC		47.99-
64PhosphorylationGLKHAQDSDPRSPTL
CCCCCCCCCCCCCCC		37.1229255136
68PhosphorylationAQDSDPRSPTLGIAR
CCCCCCCCCCCCEEC		27.8529255136
70PhosphorylationDSDPRSPTLGIARTP
CCCCCCCCCCEECCC		38.5722167270
76PhosphorylationPTLGIARTPMKTSSG
CCCCEECCCCCCCCC		20.7925159151
79MethylationGIARTPMKTSSGDPP
CEECCCCCCCCCCCC		46.59-
80PhosphorylationIARTPMKTSSGDPPS
EECCCCCCCCCCCCC		23.1323403867
81PhosphorylationARTPMKTSSGDPPSP
ECCCCCCCCCCCCCH		27.1423403867
82PhosphorylationRTPMKTSSGDPPSPL
CCCCCCCCCCCCCHH		53.0730266825
87PhosphorylationTSSGDPPSPLVKQLS
CCCCCCCCHHHHHHH		35.9319664994
94PhosphorylationSPLVKQLSEVFETED
CHHHHHHHHHHCCCC		29.2622167270
99PhosphorylationQLSEVFETEDSKSNL
HHHHHHCCCCCCCCC		33.3630266825
102PhosphorylationEVFETEDSKSNLPPE
HHHCCCCCCCCCCCC		31.5822167270
159PhosphorylationKEEARQPTETPVASQ
HHHHCCCCCCCCCCC		44.1217525332
161PhosphorylationEARQPTETPVASQSS
HHCCCCCCCCCCCCC		26.0725159151
165PhosphorylationPTETPVASQSSDKPS
CCCCCCCCCCCCCCC		30.7217525332
167PhosphorylationETPVASQSSDKPSRD
CCCCCCCCCCCCCCC		37.7030266825
168PhosphorylationTPVASQSSDKPSRDP
CCCCCCCCCCCCCCC		41.8530266825
170UbiquitinationVASQSSDKPSRDPET
CCCCCCCCCCCCCCC		47.01-
172PhosphorylationSQSSDKPSRDPETPR
CCCCCCCCCCCCCCC		55.8730266825
177PhosphorylationKPSRDPETPRSSGSM
CCCCCCCCCCCCCCC		29.4117525332
180PhosphorylationRDPETPRSSGSMRNR
CCCCCCCCCCCCCCC		40.0125627689
181PhosphorylationDPETPRSSGSMRNRW
CCCCCCCCCCCCCCC		35.8525159151
183PhosphorylationETPRSSGSMRNRWKP
CCCCCCCCCCCCCCC		19.2725159151
189UbiquitinationGSMRNRWKPNSSKVL
CCCCCCCCCCCCCCC		30.96-
199PhosphorylationSSKVLGRSPLTILQD
CCCCCCCCCCEEEEC		23.5929255136
202PhosphorylationVLGRSPLTILQDDNS
CCCCCCCEEEECCCC		24.0330266825
209PhosphorylationTILQDDNSPGTLTLR
EEEECCCCCCCEEEE		31.5329255136
212PhosphorylationQDDNSPGTLTLRQGK
ECCCCCCCEEEECCC		21.6925463755
214PhosphorylationDNSPGTLTLRQGKRP
CCCCCCEEEECCCCC		21.5229255136
219UbiquitinationTLTLRQGKRPSPLSE
CEEEECCCCCCCCCC		53.44-
222PhosphorylationLRQGKRPSPLSENVS
EECCCCCCCCCCCHH		42.3730266825
225PhosphorylationGKRPSPLSENVSELK
CCCCCCCCCCHHHHH		30.4320068231
229PhosphorylationSPLSENVSELKEGAI
CCCCCCHHHHHCCCC		49.1229978859
232UbiquitinationSENVSELKEGAILGT
CCCHHHHHCCCCCCC		50.48-
239PhosphorylationKEGAILGTGRLLKTG
HCCCCCCCCCHHHCC		18.7128555341
268PhosphorylationQHFPLVES-------
CCCCCCCC-------		37.7325159151
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 CDCA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDCA3_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 CDCA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKP1_HUMANSKP1physical
12679038
CUL1_HUMANCUL1physical
12679038
WEE1_HUMANWEE1physical
12679038
SKP1_HUMANSKP1physical
15070733
A4_HUMANAPPphysical
21832049
PLOD1_HUMANPLOD1physical
22939629
NMT1_HUMANNMT1physical
26186194
FZR1_HUMANFZR1physical
26186194
CTDSL_HUMANCTDSPLphysical
26186194
VATC1_HUMANATP6V1C1physical
26186194
LTOR4_HUMANLAMTOR4physical
26186194
CNEP1_HUMANCTDNEP1physical
26186194
CTDSL_HUMANCTDSPLphysical
28514442
FZR1_HUMANFZR1physical
28514442
VATC1_HUMANATP6V1C1physical
28514442
CHM4A_HUMANCHMP4Aphysical
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 CDCA3_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-87; SER-94 AND SER-199,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-87, AND MASSSPECTROMETRY.
"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-29; SER-31; THR-37;SER-44; SER-64; SER-68; THR-76; SER-87; SER-199 AND SER-209, 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-68; SER-199 AND SER-209,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 SER-68; THR-70; SER-199;THR-202 AND SER-209, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-165 ANDTHR-177, AND MASS SPECTROMETRY.
"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-68; SER-199 AND SER-209,AND MASS SPECTROMETRY.

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