CG050_HUMAN - dbPTM
CG050_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CG050_HUMAN
UniProt AC Q9BRJ6
Protein Name Uncharacterized protein C7orf50
Gene Name C7orf50
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization
Protein Description
Protein Sequence MAKQKRKVPEVTEKKNKKLKKASAEGPLLGPEAAPSGEGAGSKGEAVLRPGLDAEPELSPEEQRVLERKLKKERKKEERQRLREAGLVAQHPPARRSGAELALDYLCRWAQKHKNWRFQKTRQTWLLLHMYDSDKVPDEHFSTLLAYLEGLQGRARELTVQKAEALMRELDEEGSDPPLPGRAQRIRQVLQLLS
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
3Acetylation-----MAKQKRKVPE
-----CCCCCCCCCH
55.867304113
142-HydroxyisobutyrylationKVPEVTEKKNKKLKK
CCCHHHHHHCHHHHH
52.89-
14AcetylationKVPEVTEKKNKKLKK
CCCHHHHHHCHHHHH
52.8925953088
23PhosphorylationNKKLKKASAEGPLLG
CHHHHHHCCCCCCCC
35.4130266825
36PhosphorylationLGPEAAPSGEGAGSK
CCCCCCCCCCCCCCC
44.7621815630
42PhosphorylationPSGEGAGSKGEAVLR
CCCCCCCCCCCEEEC
36.6325850435
43AcetylationSGEGAGSKGEAVLRP
CCCCCCCCCCEEECC
60.9126051181
59PhosphorylationLDAEPELSPEEQRVL
CCCCCCCCHHHHHHH
28.7129255136
97PhosphorylationQHPPARRSGAELALD
CCCCCHHCCHHHHHH
36.4825159151
105PhosphorylationGAELALDYLCRWAQK
CHHHHHHHHHHHHHH
14.4622817900
107GlutathionylationELALDYLCRWAQKHK
HHHHHHHHHHHHHHC
2.5122555962
162AcetylationARELTVQKAEALMRE
HHHHHHHHHHHHHHH
43.8125953088
175PhosphorylationRELDEEGSDPPLPGR
HHHHHCCCCCCCCHH
50.6619664994

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CG050_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 CG050_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 CG050_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-23; SER-59; SER-97 ANDSER-175, AND MASS SPECTROMETRY.
"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 SER-59, AND MASSSPECTROMETRY.
"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-175, AND MASSSPECTROMETRY.

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