C102A_HUMAN - dbPTM
C102A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C102A_HUMAN
UniProt AC Q96A19
Protein Name Coiled-coil domain-containing protein 102A
Gene Name CCDC102A
Organism Homo sapiens (Human).
Sequence Length 550
Subcellular Localization
Protein Description
Protein Sequence MSHGPSPRLAESPQLSKGSLLTILGSPSPERMGPADSLPPTPPSGTPSPGPPPALPLPPAPALLADGDWESREELRLRELEEARARAAQMEKTMRRWSDCTANWREKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRDVGSERPPGSQELELVESLLKSMPEESEDCWEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSARFGTEEAEDGTSDLDEDEDLQIQVA
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--MSHGPSPRLAESP
--CCCCCCCCCCCCC
27.5229514088
12PhosphorylationPSPRLAESPQLSKGS
CCCCCCCCCCCCCCC
16.6123401153
16PhosphorylationLAESPQLSKGSLLTI
CCCCCCCCCCCEEHH
29.7130266825
19PhosphorylationSPQLSKGSLLTILGS
CCCCCCCCEEHHCCC
24.7629255136
22PhosphorylationLSKGSLLTILGSPSP
CCCCCEEHHCCCCCH
21.3230266825
26PhosphorylationSLLTILGSPSPERMG
CEEHHCCCCCHHHCC
20.8230266825
28PhosphorylationLTILGSPSPERMGPA
EHHCCCCCHHHCCCC
40.8830266825
71PhosphorylationLADGDWESREELRLR
CCCCCCCCHHHHHHH
40.5122210691
101PhosphorylationMRRWSDCTANWREKW
HHHHHHCCHHHHHHH
28.19-
109PhosphorylationANWREKWSKVRAERN
HHHHHHHHHHHHHHH
32.13-
188PhosphorylationEPVRDVGSERPPGSQ
CCCCCCCCCCCCCHH
30.2227080861
194PhosphorylationGSERPPGSQELELVE
CCCCCCCHHHHHHHH
26.6723663014
202PhosphorylationQELELVESLLKSMPE
HHHHHHHHHHHCCCC
31.3624719451
219PhosphorylationEDCWEARSLGAGGPR
CCHHHHHHCCCCCCC
37.9026657352
228PhosphorylationGAGGPRGSSGRQERS
CCCCCCCCCCCCHHC
30.7924719451
253PhosphorylationEEEASKLTALRLRLD
HHHHHHHHHHHHHCC
27.6424719451
277PhosphorylationREDKLALSRNIEKLE
HHHHHHHHHCHHHHH
20.0624719451
309PhosphorylationQEMLKQLSILKEAHQ
HHHHHHHHHHHHHHH
24.3124719451
396PhosphorylationLARRRRQTASALDCD
HHHHHHHHHHHHCCH
22.2928555341
464UbiquitinationRLRVEELKKELAQAE
HHHHHHHHHHHHHHH
47.70-
529PhosphorylationIRSARFGTEEAEDGT
HHHHCCCCCCCCCCC
28.1330278072
536PhosphorylationTEEAEDGTSDLDEDE
CCCCCCCCCCCCCCC
31.2428634120
537PhosphorylationEEAEDGTSDLDEDED
CCCCCCCCCCCCCCC
41.5329507054

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 C102A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C102A_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 C102A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of C102A_HUMAN !!

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 C102A_HUMAN

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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-26 AND SER-28, AND MASSSPECTROMETRY.

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