CD123_HUMAN - dbPTM
CD123_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD123_HUMAN
UniProt AC O75794
Protein Name Cell division cycle protein 123 homolog
Gene Name CDC123
Organism Homo sapiens (Human).
Sequence Length 336
Subcellular Localization Cytoplasm.
Protein Description Required for S phase entry of the cell cycle..
Protein Sequence MKKEHVLHCQFSAWYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEAEEIQWSDDENTATLTAPEFPEFATKVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELISENNLNGDFSEVDAQEQDSPAFRCTNSEVTVQPSPYLSYRLPKDFVDLSTGEDAHKLIDFLKLKRNQQEDD
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
24UbiquitinationFFRGVTIKSVILPLP
CCCCCEEEEEEEECC		29.3323000965
24AcetylationFFRGVTIKSVILPLP
CCCCCEEEEEEEECC		29.3326051181
35UbiquitinationLPLPQNVKDYLLDDG
EECCCCHHCEECCCC		48.4821906983
47PhosphorylationDDGTLVVSGRDDPPT
CCCCEEEECCCCCCC		22.1926074081
54PhosphorylationSGRDDPPTHSQPDSD
ECCCCCCCCCCCCCC		39.2823663014
56PhosphorylationRDDPPTHSQPDSDDE
CCCCCCCCCCCCCCC		45.9823663014
60PhosphorylationPTHSQPDSDDEAEEI
CCCCCCCCCCCHHHC		54.3621659604
70PhosphorylationEAEEIQWSDDENTAT
CHHHCCCCCCCCCCE		20.8621659604
75PhosphorylationQWSDDENTATLTAPE
CCCCCCCCCEEECCC		20.9723663014
77PhosphorylationSDDENTATLTAPEFP
CCCCCCCEEECCCCH		23.7023663014
79PhosphorylationDENTATLTAPEFPEF
CCCCCEEECCCCHHH		35.4923663014
88PhosphorylationPEFPEFATKVQEAIN
CCCHHHHHHHHHHHH		36.7528634120
103UbiquitinationSLGGSVFPKLNWSAP
HCCCCCCCCCCCCCC		37.7622817900
104UbiquitinationLGGSVFPKLNWSAPR
CCCCCCCCCCCCCCC		42.8821906983
135UbiquitinationSDIFLLFKSSDFITR
HHHHHHHHCCCCCCC		49.3621906983
168UbiquitinationEYELVLRKWCELIPG
HHHHHHHHHHHHCCC		52.62-
168AcetylationEYELVLRKWCELIPG
HHHHHHHHHHHHCCC		52.6225953088
172UbiquitinationVLRKWCELIPGAEFR
HHHHHHHHCCCCEEE		5.3321890473
174UbiquitinationRKWCELIPGAEFRCF
HHHHHHCCCCEEEEE		48.8723000965
186UbiquitinationRCFVKENKLIGISQR
EEEEECCCEECEECC		42.4429967540
187UbiquitinationCFVKENKLIGISQRD
EEEECCCEECEECCC		6.9927667366
199PhosphorylationQRDYTQYYDHISKQK
CCCHHHHHHHHHHHH		7.3927642862
204UbiquitinationQYYDHISKQKEEIRR
HHHHHHHHHHHHHHH		65.8623000965
206UbiquitinationYDHISKQKEEIRRCI
HHHHHHHHHHHHHHH		62.1423000965
218AcetylationRCIQDFFKKHIQYKF
HHHHHHHHHHHCHHC		43.3626051181
218UbiquitinationRCIQDFFKKHIQYKF
HHHHHHHHHHHCHHC		43.3629967540
219UbiquitinationCIQDFFKKHIQYKFL
HHHHHHHHHHCHHCC		40.5627667366
223PhosphorylationFFKKHIQYKFLDEDF
HHHHHHCHHCCCCCE		11.78-
276UbiquitinationNLNGDFSEVDAQEQD
CCCCCCCCCCCCCCC		44.4021890473
284PhosphorylationVDAQEQDSPAFRCTN
CCCCCCCCCCCEECC		20.1624719451
289UbiquitinationQDSPAFRCTNSEVTV
CCCCCCEECCCCEEE		3.2221890473
295UbiquitinationRCTNSEVTVQPSPYL
EECCCCEEEECCCCC		14.9021890473
295PhosphorylationRCTNSEVTVQPSPYL
EECCCCEEEECCCCC		14.9029978859
297UbiquitinationTNSEVTVQPSPYLSY
CCCCEEEECCCCCCE		24.3221890473
299PhosphorylationSEVTVQPSPYLSYRL
CCEEEECCCCCCEEC		14.7525159151
301PhosphorylationVTVQPSPYLSYRLPK
EEEECCCCCCEECCC		16.7729978859
303PhosphorylationVQPSPYLSYRLPKDF
EECCCCCCEECCCCC		11.4529978859
304PhosphorylationQPSPYLSYRLPKDFV
ECCCCCCEECCCCCC		17.3629978859
308UbiquitinationYLSYRLPKDFVDLST
CCCEECCCCCCCCCC		69.2823000965
314PhosphorylationPKDFVDLSTGEDAHK
CCCCCCCCCCCHHHH		29.8730576142
315PhosphorylationKDFVDLSTGEDAHKL
CCCCCCCCCCHHHHH		52.4629978859
321UbiquitinationSTGEDAHKLIDFLKL
CCCCHHHHHHHHHHH		49.1923000965
321AcetylationSTGEDAHKLIDFLKL
CCCCHHHHHHHHHHH		49.1926051181
327UbiquitinationHKLIDFLKLKRNQQE
HHHHHHHHHHHHCCC		52.5423000965
329UbiquitinationLIDFLKLKRNQQEDD
HHHHHHHHHHCCCCC		47.9523000965
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 CD123_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD123_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 CD123_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPM3_HUMANTPM3physical
22939629
ZPR1_HUMANZPR1physical
22939629
IF2G_YEASTGCD11physical
23775072
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 CD123_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-60, AND MASSSPECTROMETRY.

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