FYN

From Wikipedia, the free encyclopedia

FYN oncogene related to SRC, FGR, YES

PDB rendering based on 1a0n.

Available structures: 1a0n, 1aot, 1aou, 1avz, 1azg, 1efn, 1fyn, 1g83, 1m27, 1nyf, 1nyg, 1shf, 1zbj, 2dq7

Identifiers

Symbol(s)

FYN; MGC45350; SLK; SYN

External IDs

OMIM: 137025 MGI: 95602 HomoloGene: 48068

Gene ontology
Molecular Function:	• nucleotide binding • protein-tyrosine kinase activity • non-membrane spanning protein tyrosine kinase activity • protein binding • ATP binding • tubulin binding • transferase activity • identical protein binding
Cellular Component:	• cellular_component
Biological Process:	• neuron migration • protein amino acid phosphorylation • calcium ion transport • intracellular signaling cascade • protein kinase cascade • learning • feeding behavior • regulation of cell shape • peptidyl-tyrosine phosphorylation • forebrain development • T cell receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002037 (mRNA)
NP_002028 (protein)

NM_008054 (mRNA)
NP_032080 (protein)

Location

Chr 6: 112.09 - 112.3 Mb

Chr 10: 39.06 - 39.25 Mb

Pubmed search

[1]

[2]

FYN oncogene related to SRC, FGR, YES, also known as FYN, is a human gene.

This gene is a member of the protein-tyrosine kinase oncogene family. It encodes a membrane-associated tyrosine kinase that has been implicated in the control of cell growth. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist.^[1]

[edit] References

^ Entrez Gene: FYN FYN oncogene related to SRC, FGR, YES.

[edit] Further reading

O'Sullivan E, Kinnon C, Brickell P (1999). "Wiskott-Aldrich syndrome protein, WASP.". Int. J. Biochem. Cell Biol. 31 (3-4): 383–7. PMID 10224664.
Sasaoka T, Kobayashi M (2000). "The functional significance of Shc in insulin signaling as a substrate of the insulin receptor.". Endocr. J. 47 (4): 373–81. PMID 11075717.
Leavitt SA, SchOn A, Klein JC, et al. (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm.". Curr. Protein Pept. Sci. 5 (1): 1–8. PMID 14965316.
Tolstrup M, Ostergaard L, Laursen AL, et al. (2004). "HIV/SIV escape from immune surveillance: focus on Nef.". Curr. HIV Res. 2 (2): 141–51. PMID 15078178.
Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87–94. PMID 15638726.
Stove V, Verhasselt B (2006). "Modelling thymic HIV-1 Nef effects.". Curr. HIV Res. 4 (1): 57–64. PMID 16454711.