FCG2A_HUMAN - dbPTM
FCG2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FCG2A_HUMAN
UniProt AC P12318
Protein Name Low affinity immunoglobulin gamma Fc region receptor II-a
Gene Name FCGR2A
Organism Homo sapiens (Human).
Sequence Length 317
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens..
Protein Sequence MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN
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
2Phosphorylation------MTMETQMSQ
------CCHHHHHCC		24.5824043423
5Phosphorylation---MTMETQMSQNVC
---CCHHHHHCCCCC		20.8124043423
8PhosphorylationMTMETQMSQNVCPRN
CCHHHHHCCCCCCCH		14.5824043423
23PhosphorylationLWLLQPLTVLLLLAS
HHHHHHHHHHHHHHC		18.7824043423
30PhosphorylationTVLLLLASADSQAAA
HHHHHHHCCCCCCCC		32.3624043423
33PhosphorylationLLLASADSQAAAPPK
HHHHCCCCCCCCCCC		22.8024043423
97N-linked_GlycosylationYRFKANNNDSGEYTC
EEEECCCCCCCCEEE		44.6310397151
178N-linked_GlycosylationTFSIPQANHSHSGDY
CCCCCCCCCCCCCCC		31.7610397151
240PhosphorylationAAVVALIYCRKKRIS
HHHHHHHHHHHCCCC		6.2522817900
255UbiquitinationANSTDPVKAAQFEPP
CCCCCCCHHHHCCCC		43.31-
271AcetylationRQMIAIRKRQLEETN
CEEEEEEHHHHHHHC		38.087708185
277PhosphorylationRKRQLEETNNDYETA
EHHHHHHHCCCCCCC		29.91-
281PhosphorylationLEETNNDYETADGGY
HHHHCCCCCCCCCCE		19.8024927040
283PhosphorylationETNNDYETADGGYMT
HHCCCCCCCCCCEEE		24.6628060719
288PhosphorylationYETADGGYMTLNPRA
CCCCCCCEEEECCCC		7.7728060719
290PhosphorylationTADGGYMTLNPRAPT
CCCCCEEEECCCCCC		18.2028857561
297PhosphorylationTLNPRAPTDDDKNIY
EECCCCCCCCCCCEE		51.59-
304PhosphorylationTDDDKNIYLTLPPND
CCCCCCEEEECCCCC		11.7421082442
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
281YPhosphorylationKinaseBLKP51451
PhosphoELM
281YPhosphorylationKinaseFYNP06241
PhosphoELM
281YPhosphorylationKinaseSYKP43405
PSP
281YPhosphorylationKinaseLYNP07948
PhosphoELM
281YPhosphorylationKinaseSYKQ15046
PhosphoELM
288YPhosphorylationKinaseBLKP51451
PSP
288YPhosphorylationKinaseFYNP06241
PSP
288YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot
288YPhosphorylationKinaseSYKP43405
GPS
288YPhosphorylationKinaseSRC-FAMILY-GPS
288YPhosphorylationKinaseLYNP07948
PhosphoELM
288YPhosphorylationKinaseSYKQ15046
PhosphoELM
304YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot
304YPhosphorylationKinaseBLKP51451
PSP
304YPhosphorylationKinaseSRC-FAMILY-GPS
304YPhosphorylationKinaseSYKQ15046
PhosphoELM
304YPhosphorylationKinaseLYNP25911
PSP
304YPhosphorylationKinaseLYNP07948
PSP
304YPhosphorylationKinaseSYKP43405
PSP
304YPhosphorylationKinaseFYNP39688
PSP
304YPhosphorylationKinaseFYNP06241
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FCG2A_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 FCG2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P85A_HUMANPIK3R1physical
8631888
LYN_HUMANLYNphysical
9268059
KSYK_HUMANSYKphysical
9268059
P85A_HUMANPIK3R1physical
9268059
LAT_HUMANLATphysical
10781611
CBL_HUMANCBLphysical
19201892
RO52_HUMANTRIM21physical
17118455
CRYAB_HUMANCRYABphysical
21357544
UBQL1_HUMANUBQLN1physical
25416956
FCG2C_HUMANFCGR2Cphysical
26186194
EEA1_HUMANEEA1physical
26186194
PLSI_HUMANPLS1physical
26186194
PLPHP_HUMANPROSCphysical
26186194
FAH2A_HUMANFAHD2Aphysical
26186194
CANB1_HUMANPPP3R1physical
26186194
APEX1_HUMANAPEX1physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
PRDC1_HUMANPRTFDC1physical
26186194
ARPIN_HUMANARPINphysical
26186194
AGFG1_HUMANAGFG1physical
26186194
ARHL2_HUMANADPRHL2physical
26186194
PTN11_HUMANPTPN11physical
26186194
NFYC_HUMANNFYCphysical
26186194
BLVRB_HUMANBLVRBphysical
26186194
BID_HUMANBIDphysical
26186194
APEX1_HUMANAPEX1physical
28514442
FCG2C_HUMANFCGR2Cphysical
28514442
PRDC1_HUMANPRTFDC1physical
28514442
PLPHP_HUMANPROSCphysical
28514442
PLSI_HUMANPLS1physical
28514442
FAH2A_HUMANFAHD2Aphysical
28514442
BLVRB_HUMANBLVRBphysical
28514442
CANB1_HUMANPPP3R1physical
28514442
TES_HUMANTESphysical
28514442
PTN11_HUMANPTPN11physical
28514442
EEA1_HUMANEEA1physical
28514442
Drug and Disease Associations
Kegg Disease
H00080 Systemic lupus erythematosus
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 FCG2A_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Biochemical analysis and crystallisation of Fc gamma RIIa, the lowaffinity receptor for IgG.";
Powell M.S., Barton P.A., Emmanouilidis D., Wines B.D., Neumann G.M.,Peitersz G.A., Maxwell K.F., Garrett T.P., Hogarth P.M.;
Immunol. Lett. 68:17-23(1999).
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-97 AND ASN-178,AND CRYSTALLIZATION.
Phosphorylation
ReferencePubMed
"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-288, AND MASSSPECTROMETRY.
"In vivo and in vitro specificity of protein tyrosine kinases forimmunoglobulin G receptor (FcgammaRII) phosphorylation.";
Bewarder N., Weinrich V., Budde P., Hartmann D., Flaswinkel H.,Reth M., Frey J.;
Mol. Cell. Biol. 16:4735-4743(1996).
Cited for: PHOSPHORYLATION AT TYR-288 AND TYR-304.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory