Quick Order

FYN  Protein, Antibody, ELISA Kit, cDNA Clone

FYN Related Area

FYN Related Pathways

FYN Summary & Protein Information

FYN Background

Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028}.
Cofactor: Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Enzyme regulation: ENZYME REGULATION: Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site.
Subunit structure: Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity). Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts with SH2D1A and SLAMF1. Interacts (via its SH3 domain) with HEV ORF3 protein. Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Interacts with UNC119. {ECO:0000250, ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:11518702, ECO:0000269|PubMed:12545174, ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:8394019, ECO:0000269|PubMed:8681387, ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9207119, ECO:0000269|PubMed:9741627}.
Subcellular location: Cytoplasm. Nucleus. Cell membrane. Note=Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking.
Tissue specificity: Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. {ECO:0000269|PubMed:10196263}.
Post-translational: Autophosphorylated at Tyr-420. Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (By similarity). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling. {ECO:0000250, ECO:0000269|PubMed:10196263, ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:1699196, ECO:0000269|PubMed:22080863}.; Palmitoylation at Cys-3 and Cys-6 regulates subcellular location. {ECO:0000250}.
Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 SH2 domain. {ECO:0000255|PROSITE-ProRule:PRU00191}.; Contains 1 SH3 domain. {ECO:0000255|PROSITE-ProRule:PRU00192}.
General information above from UniProt

FYN Alternative Name

SLK,SYN,p59-FYN, [homo-sapiens]
AI448320,AW552119, [mus-musculus]

FYN Related Studies

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"