FCERG_HUMAN - dbPTM
FCERG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCERG_HUMAN
UniProt AC P30273
Protein Name High affinity immunoglobulin epsilon receptor subunit gamma
Gene Name FCER1G
Organism Homo sapiens (Human).
Sequence Length 86
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Associates with a variety of FcR alpha chains to form a functional signaling complex. Regulates several aspects of the immune response. The gamma subunit has a critical role in allowing the IgE Fc receptor to reach the cell surface. Also involved in collagen-mediated platelet activation and in neutrophil activation mediated by integrin..
Protein Sequence MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAITSYEKSDGVYTGLSTRNQETYETLKHEKPPQ
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
56PhosphorylationQVRKAAITSYEKSDG
HHHHHHHHEEECCCC
22.1125219547
57PhosphorylationVRKAAITSYEKSDGV
HHHHHHHEEECCCCC
25.7725219547
58PhosphorylationRKAAITSYEKSDGVY
HHHHHHEEECCCCCE
20.8025219547
60UbiquitinationAAITSYEKSDGVYTG
HHHHEEECCCCCEEC
45.6821890473
61PhosphorylationAITSYEKSDGVYTGL
HHHEEECCCCCEECC
27.8829970186
65PhosphorylationYEKSDGVYTGLSTRN
EECCCCCEECCCCCC
10.7121082442
66PhosphorylationEKSDGVYTGLSTRNQ
ECCCCCEECCCCCCH
29.2820058876
69PhosphorylationDGVYTGLSTRNQETY
CCCEECCCCCCHHHH
27.0223401153
70PhosphorylationGVYTGLSTRNQETYE
CCEECCCCCCHHHHH
38.3929978859
75PhosphorylationLSTRNQETYETLKHE
CCCCCHHHHHHHHCC
19.5228857561
76PhosphorylationSTRNQETYETLKHEK
CCCCHHHHHHHHCCC
13.2323911959
78PhosphorylationRNQETYETLKHEKPP
CCHHHHHHHHCCCCC
30.6023911959

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
69SPhosphorylationKinasePRKACAP17612
GPS
69SPhosphorylationKinasePRKCBP05771
GPS
69SPhosphorylationKinasePRKCDQ05655
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCERG_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 FCERG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FCAR_HUMANFCARphysical
15096494

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 FCERG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65 AND TYR-76, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65 AND TYR-76, AND MASSSPECTROMETRY.

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