CCD12_HUMAN - dbPTM
CCD12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD12_HUMAN
UniProt AC Q8WUD4
Protein Name Coiled-coil domain-containing protein 12
Gene Name CCDC12
Organism Homo sapiens (Human).
Sequence Length 166
Subcellular Localization
Protein Description
Protein Sequence MEATTAGVGRLEEEALRRKERLKALREKTGRKDKEDGEPKTKHLREEEEEGEKHRELRLRNYVPEDEDLKKRRVPQAKPVAVEEKVKEQLEAAKPEPVIEEVDLANLAPRKPDWDLKRDVAKKLEKLKKRTQRAIAELIRERLKGQEDSLASAVDAATEQKTCDSD
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
1Acetylation-------MEATTAGV
-------CCCCCCCC
7.7422814378
53AcetylationEEEEEGEKHRELRLR
HHHHHHHHHHHHHHH
59.84-
62PhosphorylationRELRLRNYVPEDEDL
HHHHHHHCCCCCHHH
15.7928674419
78AcetylationKRRVPQAKPVAVEEK
HCCCCCCCCCCHHHH
34.4723749302
85SumoylationKPVAVEEKVKEQLEA
CCCCHHHHHHHHHHH
45.13-
85SumoylationKPVAVEEKVKEQLEA
CCCCHHHHHHHHHHH
45.13-
94SumoylationKEQLEAAKPEPVIEE
HHHHHHCCCCCCEEH
57.89-
94UbiquitinationKEQLEAAKPEPVIEE
HHHHHHCCCCCCEEH
57.89-
94SumoylationKEQLEAAKPEPVIEE
HHHHHHCCCCCCEEH
57.8928112733
111UbiquitinationLANLAPRKPDWDLKR
HHHCCCCCCCCCHHH
46.39-
129AcetylationKKLEKLKKRTQRAIA
HHHHHHHHHHHHHHH
71.737226449
144UbiquitinationELIRERLKGQEDSLA
HHHHHHHCCCCCHHH
65.84-
149PhosphorylationRLKGQEDSLASAVDA
HHCCCCCHHHHHHHH
25.6923401153
152PhosphorylationGQEDSLASAVDAATE
CCCCHHHHHHHHHHH
33.8330266825
158PhosphorylationASAVDAATEQKTCDS
HHHHHHHHHHHCCCC
40.4430266825
162PhosphorylationDAATEQKTCDSD---
HHHHHHHCCCCC---
22.6530266825
165PhosphorylationTEQKTCDSD------
HHHHCCCCC------
47.5723401153

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 CCD12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD12_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 CCD12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRNL1_HUMANCRNKL1physical
22365833
CHM4C_HUMANCHMP4Cphysical
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 CCD12_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-165, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-165, 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-165, AND MASSSPECTROMETRY.

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