CC28A_HUMAN - dbPTM
CC28A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC28A_HUMAN
UniProt AC Q8IWP9
Protein Name Coiled-coil domain-containing protein 28A
Gene Name CCDC28A
Organism Homo sapiens (Human).
Sequence Length 274
Subcellular Localization
Protein Description
Protein Sequence MPRAEPRATLGEQEKAGLPLGAWRLYLLRHFRKQTELRRSGSRDVTGALLVAAAVASEAVGSLRVAEGGPNTLLLQVLRSWPWCNKELKTMEERKVKRRSPKSFSAHCTQVVNAKKNAIPVSKSTGFSNPASQSTSQRPKLKRVMKEKTKPQGGEGKGAQSTPIQHSFLTDVSDVQEMERGLLSLLNDFHSGKLQAFGNECSIEQMEHVRGMQEKLARLNLELYGELEELPEDKRKTASDSNLDRLLSDLEELNSSIQKLHLADAQDVPNTSAS
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
26PhosphorylationPLGAWRLYLLRHFRK
CHHHHHHHHHHHHHH
8.6317287340
95AcetylationLKTMEERKVKRRSPK
HHHHHHHHHHHCCCC
56.227668735
100PhosphorylationERKVKRRSPKSFSAH
HHHHHHCCCCCHHHH
40.4929214152
103PhosphorylationVKRRSPKSFSAHCTQ
HHHCCCCCHHHHHHH
28.0225159151
105PhosphorylationRRSPKSFSAHCTQVV
HCCCCCHHHHHHHHH
24.9729978859
109PhosphorylationKSFSAHCTQVVNAKK
CCHHHHHHHHHCCCC
17.9629978859
135PhosphorylationSNPASQSTSQRPKLK
CCCCCCCCCCCHHHH
22.6528555341
136PhosphorylationNPASQSTSQRPKLKR
CCCCCCCCCCHHHHH
29.46-
161PhosphorylationGEGKGAQSTPIQHSF
CCCCCCCCCCCCCCC
35.3029978859
162PhosphorylationEGKGAQSTPIQHSFL
CCCCCCCCCCCCCCC
16.6029978859
167PhosphorylationQSTPIQHSFLTDVSD
CCCCCCCCCCCCHHH
12.9429978859
170PhosphorylationPIQHSFLTDVSDVQE
CCCCCCCCCHHHHHH
32.1429978859
173PhosphorylationHSFLTDVSDVQEMER
CCCCCCHHHHHHHHH
34.5729978859
184PhosphorylationEMERGLLSLLNDFHS
HHHHHHHHHHHHHHH
35.5328348404
224PhosphorylationARLNLELYGELEELP
HHHCHHHHHHHHHCC
10.1227642862
237PhosphorylationLPEDKRKTASDSNLD
CCCCHHHCCCHHHHH
35.1126434776
239PhosphorylationEDKRKTASDSNLDRL
CCHHHCCCHHHHHHH
46.9721815630
241PhosphorylationKRKTASDSNLDRLLS
HHHCCCHHHHHHHHH
36.4826434776
248PhosphorylationSNLDRLLSDLEELNS
HHHHHHHHHHHHHHH
44.7528450419
255PhosphorylationSDLEELNSSIQKLHL
HHHHHHHHHHHHHHH
41.2525159151
256PhosphorylationDLEELNSSIQKLHLA
HHHHHHHHHHHHHHH
28.1521815630
271PhosphorylationDAQDVPNTSAS----
CHHCCCCCCCC----
21.4327134283
271O-linked_GlycosylationDAQDVPNTSAS----
CHHCCCCCCCC----
21.4328657654
272PhosphorylationAQDVPNTSAS-----
HHCCCCCCCC-----
32.9128985074
274O-linked_GlycosylationDVPNTSAS-------
CCCCCCCC-------
40.2928657654
274PhosphorylationDVPNTSAS-------
CCCCCCCC-------
40.2925159151

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 CC28A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC28A_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 CC28A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI54_HUMANTRIM54physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956

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 CC28A_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 TYR-26, AND MASSSPECTROMETRY.

TOP