FCG2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FCG2C_HUMAN
• UniProt AC: P31995
• Protein Name: Low affinity immunoglobulin gamma Fc region receptor II-c
• Gene Name: FCGR2C
• Organism: Homo sapiens (Human).
• Sequence Length: 323
• Subcellular Localization: Isoform IIC4: Cytoplasm .; Isoform IIC3: Cell membrane; Single-pass type I membrane protein.; Isoform IIC2: Cell membrane; Single-pass type I membrane protein.; Isoform IIC1: Cell membrane; Single-pass type I membrane protein.
• Protein Description: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells..
• Protein Sequence: MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWINVLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPNFSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQPEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN

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
106	N-linked_Glycosylation	YRFKANNNDSGEYTC EEEECCCCCCCCEEE	44.63	UniProtKB CARBOHYD
180	N-linked_Glycosylation	KFSRSDPNFSIPQAN CCCCCCCCCCCCCCC	48.57	UniProtKB CARBOHYD
187	N-linked_Glycosylation	NFSIPQANHSHSGDY CCCCCCCCCCCCCCC	31.76	23744091
246	Phosphorylation	AAVVALIYCRKKRIS HHHHHHHHHHHCCCC	6.25	22817900
261	Ubiquitination	ANSTDPVKAAQFEPP CCCCCCCHHHHCCCC	43.31	-
277	Acetylation	RQMIAIRKRQPEETN CEEEEEECCCCCCCC	49.63	7708235
287	Phosphorylation	PEETNNDYETADGGY CCCCCCCCCCCCCCE	19.80	8756631
289	Phosphorylation	ETNNDYETADGGYMT CCCCCCCCCCCCEEE	24.66	-
294	Phosphorylation	YETADGGYMTLNPRA CCCCCCCEEEECCCC	7.77	18083107
296	Phosphorylation	TADGGYMTLNPRAPT CCCCCEEEECCCCCC	18.20	-
303	Phosphorylation	TLNPRAPTDDDKNIY EECCCCCCCCCCCEE	51.59	-
310	Phosphorylation	TDDDKNIYLTLPPND CCCCCCEEEECCCCC	11.74	21082442

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
287	Y	Phosphorylation	Kinase	SYK	P43405	PSP
287	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
294	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
294	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot
310	Y	Phosphorylation	Kinase	BLK	P51451	PSP
310	Y	Phosphorylation	Kinase	FYN	P39688	PSP
310	Y	Phosphorylation	Kinase	SYK	P43405	PSP
310	Y	Phosphorylation	Kinase	LYN	P07948	PSP
310	Y	Phosphorylation	Kinase	LYN	P25911	PSP
310	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
310	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FCG2C_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FCG2C_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of FCG2C_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-310, AND MASSSPECTROMETRY.
PubMed: 18083107

"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-294 AND TYR-310.
PubMed: 8756631