FYN_RAT
ID FYN_RAT Reviewed; 537 AA.
AC Q62844;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Tyrosine-protein kinase Fyn;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fyn;
DE AltName: Full=p59-Fyn;
GN Name=Fyn {ECO:0000312|RGD:2641};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAA82942.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SHRSP {ECO:0000312|EMBL:AAA82942.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAA82942.1};
RA Nemoto K., Sekimoto M., Kageyama H., Fukamachi K., Nemoto F., Ueyama T.,
RA Senba E., Tomita I.;
RT "Expression of three type mRNAs encoding rat FYN by alternative splicing
RT within 5' untranslated region.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|PIR:PT0199}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2062320; DOI=10.1016/0161-5890(91)90153-b;
RA Yue C.C.;
RT "Novel putative protein kinase clones from a rat large granular lymphocyte
RT tumor cell line.";
RL Mol. Immunol. 28:399-408(1991).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LYS-299.
RX PubMed=10366594; DOI=10.1083/jcb.145.6.1209;
RA Osterhout D.J., Wolven A., Wolf R.M., Resh M.D., Chao M.V.;
RT "Morphological differentiation of oligodendrocytes requires activation of
RT Fyn tyrosine kinase.";
RL J. Cell Biol. 145:1209-1218(1999).
RN [4]
RP INTERACTION WITH KLHL2, AND TISSUE SPECIFICITY.
RX PubMed=15715669; DOI=10.1111/j.1471-4159.2004.02946.x;
RA Jiang S., Avraham H.K., Park S.Y., Kim T.A., Bu X., Seng S., Avraham S.;
RT "Process elongation of oligodendrocytes is promoted by the Kelch-related
RT actin-binding protein Mayven.";
RL J. Neurochem. 92:1191-1203(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-531, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in
CC many biological processes including regulation of cell growth and
CC survival, cell adhesion, integrin-mediated signaling, cytoskeletal
CC remodeling, cell motility, immune response and axon guidance. Inactive
CC FYN is phosphorylated on its C-terminal tail within the catalytic
CC domain. Following activation by PKA, the protein subsequently
CC associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation,
CC activation and targeting to focal adhesions. Involved in the regulation
CC of cell adhesion and motility through phosphorylation of CTNNB1 (beta-
CC catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling
CC by phosphorylating several proteins including the actin regulator WAS
CC and the microtubule-associated proteins MAP2 and MAPT. Promotes cell
CC survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic
CC cleavage. Participates in signal transduction pathways that regulate
CC the integrity of the glomerular slit diaphragm (an essential part of
CC the glomerular filter of the kidney) by phosphorylating several slit
CC diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role
CC in neural processes by phosphorylating DPYSL2, a multifunctional
CC adapter protein within the central nervous system, ARHGAP32, a
CC regulator for Rho family GTPases implicated in various neural
CC functions, and SNCA, a small pre-synaptic protein. Participates in the
CC downstream signaling pathways that lead to T-cell differentiation and
CC proliferation following T-cell receptor (TCR) stimulation.
CC Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation.
CC Also participates in negative feedback regulation of TCR signaling
CC through phosphorylation of PAG1, thereby promoting interaction between
CC PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK
CC and FYN in an inactive form. Promotes CD28-induced phosphorylation of
CC VAV1. In mast cells, phosphorylates CLNK after activation of
CC immunoglobulin epsilon receptor signaling (By similarity).
CC {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688,
CC ECO:0000269|PubMed:10366594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:10366594};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10366594};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-531 by
CC leukocyte common antigen and activated by dephosphorylation of this
CC site. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8.
CC Interacts with FYB1, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-
CC phosphorylated form); the interaction increases FYN activity. Interacts
CC (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity).
CC Interacts with TOM1L1 (phosphorylated form). Interacts with KDR
CC (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via
CC N-terminus) (PubMed:15715669). Interacts with SH2D1A and SLAMF1.
CC Interacts with ITCH; the interaction phosphorylates ITCH and negatively
CC regulates its activity. Interacts with FASLG. Interacts with RUNX3.
CC Interacts with KIT. Interacts with EPHA8; possible downstream effector
CC of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this
CC interaction leads to PTK2/FAK1 phosphorylation and activation.
CC Interacts with CAV1; this interaction couples integrins to the Ras-ERK
CC pathway. Interacts with UNC119. Interacts (via SH2 domain) with PTPRH
CC (phosphorylated form) (By similarity). Interacts with PTPRO
CC (phosphorylated form) (By similarity). Interacts with PTPRB
CC (phosphorylated form) (By similarity). Interacts with FYB2 (By
CC similarity). Interacts with DSCAM (By similarity). Interacts with SKAP1
CC and FYB1; this interaction promotes the phosphorylation of CLNK (By
CC similarity). {ECO:0000250|UniProtKB:P06241,
CC ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:15715669}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Present and
CC active in lipid rafts. Palmitoylation is crucial for proper trafficking
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in spinal cord oligodendrocytes (at
CC protein level). {ECO:0000269|PubMed:15715669}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during oligodendrocyte
CC differentiation. {ECO:0000269|PubMed:10366594}.
CC -!- PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on
CC the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an
CC inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to
CC activation. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates
CC T-cell receptor signaling (By similarity). Phosphorylated at tyrosine
CC residues, which can be enhanced by NTN1 (By similarity).
CC {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688}.
CC -!- PTM: Palmitoylated. Palmitoylation at Cys-3 and Cys-6, probably by
CC ZDHHC21, regulates subcellular location.
CC {ECO:0000250|UniProtKB:P39688}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U35365; AAA82942.1; -; mRNA.
DR PIR; PT0199; PT0199.
DR RefSeq; NP_036887.1; NM_012755.1.
DR AlphaFoldDB; Q62844; -.
DR SMR; Q62844; -.
DR BioGRID; 247215; 5.
DR CORUM; Q62844; -.
DR IntAct; Q62844; 4.
DR MINT; Q62844; -.
DR STRING; 10116.ENSRNOP00000000733; -.
DR iPTMnet; Q62844; -.
DR PhosphoSitePlus; Q62844; -.
DR SwissPalm; Q62844; -.
DR jPOST; Q62844; -.
DR PaxDb; Q62844; -.
DR PRIDE; Q62844; -.
DR Ensembl; ENSRNOT00000000733; ENSRNOP00000000733; ENSRNOG00000000596.
DR GeneID; 25150; -.
DR KEGG; rno:25150; -.
DR UCSC; RGD:2641; rat.
DR CTD; 2534; -.
DR RGD; 2641; Fyn.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000155462; -.
DR InParanoid; Q62844; -.
DR OMA; WMEKADG; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; Q62844; -.
DR TreeFam; TF351634; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1227986; Signaling by ERBB2.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1433559; Regulation of KIT signaling.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-2029481; FCGR activation.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-373753; Nephrin family interactions.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-389356; CD28 co-stimulation.
DR Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5621480; Dectin-2 family.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-RNO-8866376; Reelin signalling pathway.
DR Reactome; R-RNO-9032759; NTRK2 activates RAC1.
DR Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR PRO; PR:Q62844; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000596; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q62844; baseline and differential.
DR Genevisible; Q62844; RN.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0097386; C:glial cell projection; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:ARUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042609; F:CD4 receptor binding; IPI:RGD.
DR GO; GO:0042610; F:CD8 receptor binding; IPI:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0070851; F:growth factor receptor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0051428; F:peptide hormone receptor binding; IPI:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:RGD.
DR GO; GO:0016004; F:phospholipase activator activity; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0042608; F:T cell receptor binding; IDA:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IPI:ARUK-UCL.
DR GO; GO:0050798; P:activated T cell proliferation; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:1905430; P:cellular response to glycine; IMP:ARUK-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:ARUK-UCL.
DR GO; GO:1905232; P:cellular response to L-glutamate; IMP:ARUK-UCL.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0003015; P:heart process; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; TAS:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IMP:ARUK-UCL.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0000304; P:response to singlet oxygen; IDA:ARUK-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12006; SH3_Fyn_Yrk; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035750; Fyn/Yrk_SH3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Kinase; Lipoprotein;
KW Manganese; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Palmitate; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06241"
FT CHAIN 2..537
FT /note="Tyrosine-protein kinase Fyn"
FT /id="PRO_0000282948"
FT DOMAIN 82..143
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 149..246
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 271..524
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 390
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028"
FT BINDING 277..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:10366594"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06241"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06241"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39688"
FT MOD_RES 420
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P39688"
FT MOD_RES 531
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P39688"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P39688"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P39688"
FT MUTAGEN 299
FT /note="K->M: Loss of kinase activity and reduction in
FT oligodendrocyte process extension and myelin membrane
FT formation."
FT /evidence="ECO:0000269|PubMed:10366594"
SQ SEQUENCE 537 AA; 60702 MW; 11AE4420919DBF1C CRC64;
MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
