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P39688

- FYN_MOUSE

UniProt

P39688 - FYN_MOUSE

Protein

Tyrosine-protein kinase Fyn

Gene

Fyn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (03 Apr 2013)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1 By similarity.By similarity

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Cofactori

    Manganese.

    Enzyme regulationi

    Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei299 – 2991ATPPROSITE-ProRule annotation
    Active sitei390 – 3901Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 2859ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. G-protein coupled receptor binding Source: UniProt
    3. ion channel binding Source: BHF-UCL
    4. metal ion binding Source: UniProtKB-KW
    5. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    6. protein binding Source: UniProtKB
    7. protein kinase activity Source: MGI
    8. protein tyrosine kinase activity Source: MGI
    9. tubulin binding Source: MGI

    GO - Biological processi

    1. activated T cell proliferation Source: MGI
    2. cell surface receptor signaling pathway Source: MGI
    3. cellular response to growth factor stimulus Source: Ensembl
    4. cellular response to peptide hormone stimulus Source: Ensembl
    5. dendrite morphogenesis Source: MGI
    6. detection of mechanical stimulus involved in sensory perception of pain Source: MGI
    7. forebrain development Source: MGI
    8. myelination Source: MGI
    9. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    10. negative regulation of gene expression Source: BHF-UCL
    11. negative regulation of protein catabolic process Source: MGI
    12. neuron migration Source: MGI
    13. peptidyl-tyrosine phosphorylation Source: MGI
    14. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    15. positive regulation of neuron projection development Source: MGI
    16. positive regulation of protein localization to nucleus Source: MGI
    17. protein autophosphorylation Source: MGI
    18. protein phosphorylation Source: MGI
    19. regulation of cell shape Source: MGI
    20. response to drug Source: Ensembl
    21. response to ethanol Source: MGI
    22. T cell receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196487. FCGR activation.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198634. Regulation of signaling by CBL.
    REACT_204081. CD28 co-stimulation.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_227425. Regulation of KIT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fyn (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fyn
    p59-Fyn
    Gene namesi
    Name:Fyn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:95602. Fyn.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity
    Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome Source: Ensembl
    3. mitochondrion Source: Ensembl
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell
    6. postsynaptic density Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice have various neural defects, including defective long term potentiation, impaired spatial memory, hypomyelination, abnormal dendrite orientation and uncoordinated hippocampal structure.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes myristoylation and palmitoylation. 1 Publication
    Mutagenesisi3 – 31C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. 3 Publications
    Mutagenesisi3 – 31C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. 3 Publications
    Mutagenesisi6 – 61C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. 2 Publications
    Mutagenesisi6 – 61C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 537536Tyrosine-protein kinase FynPRO_0000088100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteine3 Publications
    Lipidationi6 – 61S-palmitoyl cysteine2 Publications
    Modified residuei15 – 151PhosphothreonineBy similarity
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei185 – 1851Phosphotyrosine1 Publication
    Modified residuei213 – 2131PhosphotyrosineBy similarity
    Modified residuei214 – 2141PhosphotyrosineBy similarity
    Modified residuei257 – 2571PhosphoserineBy similarity
    Modified residuei420 – 4201Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei440 – 4401PhosphotyrosineBy similarity
    Modified residuei512 – 5121PhosphothreonineBy similarity
    Modified residuei531 – 5311Phosphotyrosine; alternate2 Publications
    Modified residuei531 – 5311Phosphotyrosine; by CSK; alternateBy similarity

    Post-translational modificationi

    Autophosphorylated at Tyr-420. Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-15 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling By similarity.By similarity
    Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.3 Publications
    Myristoylation is required prior to palmitoylation.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP39688.
    PRIDEiP39688.

    PTM databases

    PhosphoSiteiP39688.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in the brain, isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes.2 Publications

    Gene expression databases

    ArrayExpressiP39688.
    BgeeiP39688.
    CleanExiMM_FYN.
    GenevestigatoriP39688.

    Interactioni

    Subunit structurei

    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 with TOM1L1 (phosphorylated form). Interacts with SH2D1A and SLAMF1. Interacts with and phosphorylates ITCH, down-regulating 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 (via SH3 domain) with KLHL2 (via N-terminus) By similarity. Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with UNC119 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBLP226813EBI-524514,EBI-518228From a different organism.
    Dynlt1P518073EBI-524514,EBI-642797
    Irs1P355704EBI-524514,EBI-520230From a different organism.
    Khdrbs1Q6074913EBI-524514,EBI-519077
    PdgfrbP056223EBI-524514,EBI-1554855
    PLXNA2O750513EBI-524514,EBI-308264From a different organism.
    PTPRAP184332EBI-524514,EBI-2609645From a different organism.
    Slamf1Q9QUM44EBI-524514,EBI-7910086
    Sphk2Q9JIA72EBI-524514,EBI-985434

    Protein-protein interaction databases

    BioGridi199773. 12 interactions.
    DIPiDIP-198N.
    IntActiP39688. 34 interactions.
    MINTiMINT-85422.

    Structurei

    Secondary structure

    1
    537
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi87 – 915
    Beta strandi108 – 1136
    Beta strandi115 – 12410
    Turni125 – 1273
    Beta strandi130 – 1345
    Helixi135 – 1373
    Beta strandi138 – 1403
    Helixi156 – 1638
    Beta strandi173 – 1775
    Beta strandi179 – 1813
    Beta strandi185 – 1928
    Beta strandi194 – 20714
    Beta strandi213 – 2164
    Beta strandi221 – 2233
    Helixi224 – 23310
    Beta strandi238 – 2403

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UF4X-ray1.98A82-244[»]
    ProteinModelPortaliP39688.
    SMRiP39688. Positions 81-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 14362SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 24698SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 524254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087702.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP39688.
    KOiK05703.
    OMAiSHNSGYR.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P39688-1) [UniParc]FASTAAdd to Basket

    Also known as: B

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY    50
    NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD 100
    LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY 150
    FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV 200
    KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM 250
    PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 300
    LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL 350
    LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN 400
    GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 450
    SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI 500
    HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL 537
    Length:537
    Mass (Da):60,675
    Last modified:April 3, 2013 - v4
    Checksum:i99558702596DAEE0
    GO
    Isoform 2 (identifier: P39688-2) [UniParc]FASTAAdd to Basket

    Also known as: T

    The sequence of this isoform differs from the canonical sequence as follows:
         234-236: RAA → KAD
         240-287: CRLVVPCHKG...GNGQFGEVWM → FNLTVVSSSC...GQGCFAEVWL

    Show »
    Length:534
    Mass (Da):60,059
    Checksum:i782C93B2003B7DCD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791E → Q in AAA37644. (PubMed:2488273)Curated
    Sequence conflicti179 – 1791E → Q in AAB09568. (PubMed:9895129)Curated
    Sequence conflicti432 – 4321W → R in BAE42585. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei234 – 2363RAA → KAD in isoform 2. 4 PublicationsVSP_024111
    Alternative sequencei240 – 28748CRLVV…GEVWM → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF AEVWL in isoform 2. 4 PublicationsVSP_024112Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27266 mRNA. Translation: AAA37644.1.
    U70324 mRNA. Translation: AAB09568.1.
    AK156584 mRNA. Translation: BAE33766.1.
    AK171646 mRNA. Translation: BAE42585.1.
    BC032149 mRNA. Translation: AAH32149.1.
    BC092217 mRNA. Translation: AAH92217.1.
    CCDSiCCDS23788.1. [P39688-2]
    CCDS48538.1. [P39688-1]
    PIRiA44991.
    RefSeqiNP_001116364.1. NM_001122892.1. [P39688-2]
    NP_001116365.1. NM_001122893.1. [P39688-1]
    NP_032080.2. NM_008054.2. [P39688-2]
    XP_006512602.1. XM_006512539.1. [P39688-1]
    XP_006512603.1. XM_006512540.1. [P39688-1]
    UniGeneiMm.4848.

    Genome annotation databases

    EnsembliENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843. [P39688-2]
    ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843. [P39688-1]
    ENSMUST00000126486; ENSMUSP00000115233; ENSMUSG00000019843. [P39688-2]
    ENSMUST00000135242; ENSMUSP00000117111; ENSMUSG00000019843. [P39688-2]
    ENSMUST00000146287; ENSMUSP00000114188; ENSMUSG00000019843. [P39688-2]
    GeneIDi14360.
    KEGGimmu:14360.
    UCSCiuc007evx.2. mouse. [P39688-1]
    uc007evy.2. mouse. [P39688-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27266 mRNA. Translation: AAA37644.1 .
    U70324 mRNA. Translation: AAB09568.1 .
    AK156584 mRNA. Translation: BAE33766.1 .
    AK171646 mRNA. Translation: BAE42585.1 .
    BC032149 mRNA. Translation: AAH32149.1 .
    BC092217 mRNA. Translation: AAH92217.1 .
    CCDSi CCDS23788.1. [P39688-2 ]
    CCDS48538.1. [P39688-1 ]
    PIRi A44991.
    RefSeqi NP_001116364.1. NM_001122892.1. [P39688-2 ]
    NP_001116365.1. NM_001122893.1. [P39688-1 ]
    NP_032080.2. NM_008054.2. [P39688-2 ]
    XP_006512602.1. XM_006512539.1. [P39688-1 ]
    XP_006512603.1. XM_006512540.1. [P39688-1 ]
    UniGenei Mm.4848.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UF4 X-ray 1.98 A 82-244 [» ]
    ProteinModelPortali P39688.
    SMRi P39688. Positions 81-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199773. 12 interactions.
    DIPi DIP-198N.
    IntActi P39688. 34 interactions.
    MINTi MINT-85422.

    Chemistry

    BindingDBi P39688.
    ChEMBLi CHEMBL4517.

    PTM databases

    PhosphoSitei P39688.

    Proteomic databases

    PaxDbi P39688.
    PRIDEi P39688.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063091 ; ENSMUSP00000057707 ; ENSMUSG00000019843 . [P39688-2 ]
    ENSMUST00000099967 ; ENSMUSP00000097547 ; ENSMUSG00000019843 . [P39688-1 ]
    ENSMUST00000126486 ; ENSMUSP00000115233 ; ENSMUSG00000019843 . [P39688-2 ]
    ENSMUST00000135242 ; ENSMUSP00000117111 ; ENSMUSG00000019843 . [P39688-2 ]
    ENSMUST00000146287 ; ENSMUSP00000114188 ; ENSMUSG00000019843 . [P39688-2 ]
    GeneIDi 14360.
    KEGGi mmu:14360.
    UCSCi uc007evx.2. mouse. [P39688-1 ]
    uc007evy.2. mouse. [P39688-2 ]

    Organism-specific databases

    CTDi 2534.
    MGIi MGI:95602. Fyn.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087702.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P39688.
    KOi K05703.
    OMAi SHNSGYR.
    TreeFami TF351634.

    Enzyme and pathway databases

    Reactomei REACT_188185. DAP12 signaling.
    REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196487. FCGR activation.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198634. Regulation of signaling by CBL.
    REACT_204081. CD28 co-stimulation.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_227425. Regulation of KIT signaling.

    Miscellaneous databases

    ChiTaRSi FYN. mouse.
    NextBioi 285821.
    PROi P39688.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P39688.
    Bgeei P39688.
    CleanExi MM_FYN.
    Genevestigatori P39688.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of a novel form of the fyn proto-oncogene in hematopoietic cells."
      Cooke M.P., Perlmutter R.M.
      New Biol. 1:66-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Two species of mRNAs for the fyn proto-oncogene are produced by an alternative polyadenylation."
      Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.
      Mol. Cells 8:746-749(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: T-cell.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: NOD.
      Tissue: Spleen.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Mammary tumor.
    5. "Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice."
      Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., Kandel E.R.
      Science 258:1903-1910(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    6. "Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
      Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
      EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSF1R.
    7. "Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases."
      Hurley T.R., Hyman R., Sefton B.M.
      Mol. Cell. Biol. 13:1651-1656(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-420 AND TYR-531, ENZYME REGULATION.
    8. "Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins."
      Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.
      Mol. Cell. Biol. 13:6385-6392(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF CYS-3 AND CYS-6.
    9. "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
      Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
      Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-6.
    10. "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
      Clark M.R., Johnson S.A., Cambier J.C.
      EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A.
    11. "Unique catalytic properties dictate the enhanced function of p59fynT, the hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T cells."
      Davidson D., Viallet J., Veillette A.
      Mol. Cell. Biol. 14:4554-4564(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. "Multiple features of the p59fyn src homology 4 domain define a motif for immune-receptor tyrosine-based activation motif (ITAM) binding and for plasma membrane localization."
      Gauen L.K.T., Linder M.E., Shaw A.S.
      J. Cell Biol. 133:1007-1015(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    13. "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
      Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
      EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSF1R.
    14. "Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association."
      Wolven A., Okamura H., Rosenblatt Y., Resh M.D.
      Mol. Biol. Cell 8:1159-1173(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF CYS-3.
    15. "'Srcasm: a novel Src activating and signaling molecule."
      Seykora J.T., Mei L., Dotto G.P., Stein P.L.
      J. Biol. Chem. 277:2812-2822(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOM1L1.
    16. "Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
      Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
      J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."
      Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M.
      Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTNNB1.
    18. "Transmembrane phosphoprotein Cbp senses cell adhesion signaling mediated by Src family kinase in lipid rafts."
      Shima T., Nada S., Okada M.
      Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
    20. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
      Roskoski R. Jr.
      Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    21. "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
      Lamalice L., Houle F., Huot J.
      J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KDR.
    22. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    23. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Decreased dendritic spine density and abnormal spine morphology in Fyn knockout mice."
      Babus L.W., Little E.M., Keenoy K.E., Minami S.S., Chen E., Song J.M., Caviness J., Koo S.Y., Pak D.T., Rebeck G.W., Turner R.S., Hoe H.S.
      Brain Res. 1415:96-102(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    25. "Crystal structure of a SH3 and SH2 domains of fyn protein (proto-concogene tyrosine-protein kinase fyn) from Mus musculus at 1.98 a resolution."
      Joint center for structural genomics (JCSG)
      Submitted (DEC-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 81-239.

    Entry informationi

    Entry nameiFYN_MOUSE
    AccessioniPrimary (citable) accession number: P39688
    Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: April 3, 2013
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3