FGR
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Official Full Name
feline Gardner-Rasheed sarcoma viral oncogene homolog -
Overview
This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to plasma membrane ruffles, and functions as a negative regulator of cell migration and adhesion triggered by the beta-2 integrin signal transduction pathway. Infection with Epstein-Barr virus results in the overexpression of this gene. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jul 2008] -
Synonyms
FGR;feline Gardner-Rasheed sarcoma viral oncogene homolog;SRC2;c-fgr;c-src2;p55-Fgr;p58-Fgr;p55c-fgr;p58c-fgr;tyrosine-protein kinase Fgr;p55-c-fgr protein;c-fgr protooncogene;proto-oncogene c-Fgr;c-src-2 proto-oncogene;proto-oncogene tyrosine-protein kinase FGR;v-fgr feline Gardner-Rasheed sarcoma viral oncogene homolog;Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog
Recombinant Proteins
- Human
- Rhesus macaque
- Rat
- Mouse
- Sf9 Insect Cell
- Mammalian cells
- Mammalian Cell
- HEK293
- Insect Cell
- HEK293T
- Insect (sf21)
- Wheat Germ
- In Vitro Cell Free System
- GST
- Flag
- His
- Non
- His&Fc&Avi
- Myc&DDK
- His&GST
Involved Pathway
FGR involved in several pathways and played different roles in them. We selected most pathways FGR participated on our site, such as Chemokine signaling pathway,Epstein-Barr virus infection, which may be useful for your reference. Also, other proteins which involved in the same pathway with FGR were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Epstein-Barr virus infection | CDK1,SPI1,PSMD13,EIF2AK1,HSPA6,POLR2A,PSMC1,POLR2J3,SNW1,TAB2 |
Chemokine signaling pathway | CCL3L3,CRKL,DOCK2,FOXO3,PIK3CB,RAF1,PIK3CA,ARRB1,NFKBIB,STAT1 |
Protein Function
FGR has several biochemical functions, for example, ATP binding,Fc-gamma receptor I complex binding,immunoglobulin receptor binding. Some of the functions are cooperated with other proteins, some of the functions could acted by FGR itself. We selected most functions FGR had, and list some proteins which have the same functions with FGR. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
Fc-gamma receptor I complex binding | FLNA |
protein tyrosine kinase activity | TNK1,ABL1,NEK1,CSF1RA,EPHB2B,SRC,MAP2K1,PTK6B,MAP2K2,MAP2K7 |
non-membrane spanning protein tyrosine kinase activity | ZAP70,JAK3,FYN,PKDCC,MELK,BLK,LYN,ABL1,PTK2BB,STK16 |
phosphotyrosine binding | ZAP70,STAP1,CBLC,CBL,MAPK3,CBLB,LDLRAP1,SHC1,ACP2,GRB2 |
ATP binding | VRK1,PSMC1B,MAP4K5,NMNAT3,SNRKB,C22orf28,STK35,RFC2,MAP4K3,XYLB |
immunoglobulin receptor binding | Ighg2a,Ighg,IGLL1,IgG3,FES,CLEC4D,IGKC,IGLC2,Ighg2b |
protein binding | ERBB3,NKX2,LDLRAD1,DUSP5,ARF1,RNF175,IL32,NDUFAF4,IGSF21B,ENO1 |
protein kinase binding | CDK5,STAP1,PPP1R15A,SPRY2,TRP53,SPDYB,MAP3K13,PPME1,STXBP1,DCX |
Interacting Protein
FGR has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with FGR here. Most of them are supplied by our site. Hope this information will be useful for your research of FGR.
HSP90AB1;EGFR;ERBB2;MET;ALOX5;AR;KIT;WAS;EEF1A2;ABI1;abl-tide
Resources
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References
- Abu Shehab, M; Damerill, I; et al. Liver mTOR Controls IGF-I Bioavailability by Regulation of Protein Kinase CK2 and IGFBP-1 Phosphorylation in Fetal Growth Restriction. ENDOCRINOLOGY 155:1327-1339(2014).
- Deng, L; Kitova, EN; et al. Mapping Protein-Ligand Interactions in the Gas Phase Using a Functional Group Replacement Strategy. Comparison of CID and BIRD Activation Methods. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY 24:988-996(2013).