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P06241

- FYN_HUMAN

UniProt

P06241 - FYN_HUMAN

Protein

Tyrosine-protein kinase Fyn

Gene

FYN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 192 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 VAV1.19 Publications

    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.

    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. ephrin receptor binding Source: UniProtKB
    3. glycoprotein binding Source: BHF-UCL
    4. growth factor receptor binding Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein tyrosine kinase activity Source: Reactome

    GO - Biological processi

    1. activated T cell proliferation Source: Ensembl
    2. axon guidance Source: Reactome
    3. blood coagulation Source: Reactome
    4. calcium ion transport Source: UniProtKB
    5. cellular response to peptide hormone stimulus Source: Ensembl
    6. dendrite morphogenesis Source: Ensembl
    7. detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
    8. epidermal growth factor receptor signaling pathway Source: Reactome
    9. Fc-epsilon receptor signaling pathway Source: Reactome
    10. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    11. feeding behavior Source: ProtInc
    12. fibroblast growth factor receptor signaling pathway Source: Reactome
    13. forebrain development Source: Ensembl
    14. innate immune response Source: Reactome
    15. intracellular signal transduction Source: ProtInc
    16. learning Source: ProtInc
    17. leukocyte migration Source: Reactome
    18. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    19. negative regulation of gene expression Source: Ensembl
    20. negative regulation of protein catabolic process Source: Ensembl
    21. neuron migration Source: Ensembl
    22. neurotrophin TRK receptor signaling pathway Source: Reactome
    23. phosphatidylinositol-mediated signaling Source: Reactome
    24. platelet activation Source: Reactome
    25. positive regulation of neuron projection development Source: Ensembl
    26. positive regulation of protein localization to nucleus Source: Ensembl
    27. protein autophosphorylation Source: Ensembl
    28. protein phosphorylation Source: UniProtKB
    29. regulation of cell shape Source: Ensembl
    30. regulation of defense response to virus by virus Source: Reactome
    31. response to drug Source: Ensembl
    32. response to ethanol Source: Ensembl
    33. T cell costimulation Source: Reactome
    34. T cell receptor signaling pathway Source: UniProtKB
    35. viral process Source: Reactome

    Keywords - Molecular functioni

    Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Host-virus interaction, Immunity

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_111040. Signaling by SCF-KIT.
    REACT_111225. Regulation of KIT signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_12519. PECAM1 interactions.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_147814. DAP12 signaling.
    REACT_160274. FCGR activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_19183. CD28 co-stimulation.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_22351. DCC mediated attractive signaling.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23832. Nephrin interactions.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP06241.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fyn (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene Syn
    Proto-oncogene c-Fyn
    Src-like kinase
    Short name:
    SLK
    p59-Fyn
    Gene namesi
    Name:FYN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4037. FYN.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA28454.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 537536Tyrosine-protein kinase FynPRO_0000088099Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Lipidationi6 – 61S-palmitoyl cysteineBy similarity
    Modified residuei12 – 121Phosphothreonine; by PKC1 Publication
    Modified residuei15 – 151Phosphothreonine
    Modified residuei21 – 211Phosphoserine5 Publications
    Modified residuei25 – 251Phosphoserine
    Modified residuei185 – 1851PhosphotyrosineBy similarity
    Modified residuei213 – 2131Phosphotyrosine
    Modified residuei214 – 2141Phosphotyrosine
    Modified residuei257 – 2571Phosphoserine
    Modified residuei420 – 4201Phosphotyrosine; by autocatalysis
    Modified residuei440 – 4401Phosphotyrosine
    Modified residuei512 – 5121Phosphothreonine
    Modified residuei531 – 5311Phosphotyrosine; by CSK2 Publications

    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 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.By similarity9 Publications
    Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP06241.
    PaxDbiP06241.
    PRIDEiP06241.

    PTM databases

    PhosphoSiteiP06241.

    Miscellaneous databases

    PMAP-CutDBP06241.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP06241.
    BgeeiP06241.
    CleanExiHS_FYN.
    GenevestigatoriP06241.

    Organism-specific databases

    HPAiCAB005034.
    CAB018387.
    HPA023887.

    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 (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.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    O929722EBI-515315,EBI-710506From a different organism.
    P279584EBI-515315,EBI-706378From a different organism.
    Q9WMX22EBI-515315,EBI-710918From a different organism.
    ABL2P426842EBI-515315,EBI-1102694
    ADAM15Q134442EBI-515315,EBI-77818
    ARHGAP32A7KAX94EBI-515315,EBI-308663
    ARHGAP33O145592EBI-515315,EBI-1210010
    ASAP1Q9ULH13EBI-515315,EBI-346622
    BCAR1P569453EBI-515315,EBI-702093
    ERBB2P046262EBI-515315,EBI-641062
    FASLGP480232EBI-515315,EBI-495538
    FN1P02751-72EBI-515315,EBI-7133890
    FYBO151172EBI-515315,EBI-1753267
    Grm5P31424-22EBI-515315,EBI-8830305From a different organism.
    HSP90AB1P082382EBI-515315,EBI-352572
    HTR6P504067EBI-515315,EBI-1182222
    KHDRBS1Q076664EBI-515315,EBI-1364
    MAP4K1Q929182EBI-515315,EBI-881
    MED28Q9H2046EBI-515315,EBI-514199
    NELFBQ8WX922EBI-515315,EBI-347721
    PAG1Q9NWQ85EBI-515315,EBI-2828115
    PDCD6IPQ8WUM46EBI-515315,EBI-310624
    PDGFRBP096193EBI-515315,EBI-641237
    PRICKLE3O439002EBI-515315,EBI-1751761
    PRKCDQ056555EBI-515315,EBI-704279
    PRKCQQ047597EBI-515315,EBI-374762
    RAPGEF1Q139052EBI-515315,EBI-976876
    SH2D1AO608802EBI-515315,EBI-6983382

    Protein-protein interaction databases

    BioGridi108810. 139 interactions.
    DIPiDIP-33876N.
    IntActiP06241. 212 interactions.
    MINTiMINT-93594.
    STRINGi9606.ENSP00000357656.

    Structurei

    Secondary structure

    1
    537
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi87 – 915
    Beta strandi96 – 1005
    Beta strandi108 – 1136
    Beta strandi115 – 12410
    Turni125 – 1273
    Beta strandi130 – 1345
    Helixi135 – 1373
    Beta strandi138 – 1414
    Helixi144 – 1463
    Beta strandi147 – 1504
    Helixi156 – 1649
    Turni165 – 1673
    Beta strandi173 – 1775
    Beta strandi179 – 1813
    Beta strandi185 – 1928
    Beta strandi194 – 1963
    Beta strandi198 – 20710
    Turni209 – 2113
    Beta strandi212 – 2165
    Beta strandi220 – 2234
    Helixi224 – 23310
    Beta strandi238 – 2403
    Beta strandi263 – 2653
    Helixi268 – 2703
    Beta strandi271 – 2788
    Beta strandi285 – 2906
    Turni291 – 2933
    Beta strandi294 – 2996
    Turni303 – 3053
    Helixi308 – 31811
    Beta strandi329 – 3335
    Beta strandi335 – 3373
    Beta strandi339 – 3435
    Helixi350 – 3545
    Beta strandi355 – 3573
    Turni358 – 3603
    Helixi364 – 38320
    Helixi393 – 3953
    Beta strandi396 – 3994
    Turni400 – 4023
    Beta strandi403 – 4064
    Beta strandi416 – 4183
    Turni430 – 4323
    Helixi435 – 4384
    Helixi445 – 46016
    Helixi472 – 48110
    Helixi496 – 5027
    Helixi507 – 5093
    Helixi513 – 5219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A0NNMR-B80-148[»]
    1AOTNMR-F143-248[»]
    1AOUNMR-F143-248[»]
    1AVZX-ray3.00C85-141[»]
    1AZGNMR-B82-148[»]
    1EFNX-ray2.50A/C86-143[»]
    1FYNX-ray2.30A81-142[»]
    1G83X-ray2.60A/B82-246[»]
    1M27X-ray2.50C84-144[»]
    1NYFNMR-A82-148[»]
    1NYGNMR-A82-148[»]
    1SHFX-ray1.90A/B84-142[»]
    1ZBJNMR-A84-142[»]
    2DQ7X-ray2.80X261-537[»]
    3H0FX-ray2.61A73-142[»]
    3H0HX-ray1.76A73-142[»]
    3H0IX-ray2.20A/B73-142[»]
    3UA6X-ray1.85A/B81-143[»]
    3UA7X-ray1.50A/B/C/D81-143[»]
    4D8DX-ray2.52A/C84-141[»]
    4EIKX-ray1.60A81-143[»]
    ProteinModelPortaliP06241.
    SMRiP06241. Positions 81-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06241.

    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.
    HOVERGENiHBG008761.
    InParanoidiP06241.
    KOiK05703.
    OMAiSHNSGYR.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP06241.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06241-1) [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 ATKLTEERDG 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 VTEYMNKGSL 350
    LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN 400
    GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 450
    SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI 500
    HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL 537
    Length:537
    Mass (Da):60,762
    Last modified:January 23, 2007 - v3
    Checksum:i4A1E443A4B5A0977
    GO
    Isoform 2 (identifier: P06241-2) [UniParc]FASTAAdd to Basket

    Also known as: T

    The sequence of this isoform differs from the canonical sequence as follows:
         234-287: RAAGLCCRLV...GNGQFGEVWM → KADGLCFNLT...GQGCFAEVWL

    Show »
    Length:534
    Mass (Da):60,141
    Checksum:iFA082D40A24C2802
    GO
    Isoform 3 (identifier: P06241-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         233-287: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:482
    Mass (Da):54,513
    Checksum:i055C3965AC5A9135
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841A → S in AAA36615. (PubMed:3099169)Curated
    Sequence conflicti437 – 4371A → R in AAA36615. (PubMed:3099169)Curated
    Sequence conflicti437 – 4371A → R in AAB33113. (PubMed:7822789)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti243 – 2431V → L in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041704
    Natural varianti410 – 4101G → R in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041705
    Natural varianti445 – 4451I → F.
    Corresponds to variant rs1801121 [ dbSNP | Ensembl ].
    VAR_014661
    Natural varianti506 – 5061D → E.1 Publication
    Corresponds to variant rs28763975 [ dbSNP | Ensembl ].
    VAR_041706

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei233 – 28755Missing in isoform 3. 1 PublicationVSP_024108Add
    BLAST
    Alternative sequencei234 – 28754RAAGL…GEVWM → KADGLCFNLTVIASSCTPQT SGLAKDAWEVARRSLCLEKK LGQGCFAEVWL in isoform 2. 1 PublicationVSP_024110Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14676 mRNA. Translation: AAA36615.1.
    M14333 mRNA. Translation: AAC08285.1.
    S74774 mRNA. Translation: AAB33113.2.
    AB451293 mRNA. Translation: BAG70107.1.
    AB451426 mRNA. Translation: BAG70240.1.
    Z97989 Genomic DNA. Translation: CAI22300.1.
    Z97989 Genomic DNA. Translation: CAI22301.1.
    CH471051 Genomic DNA. Translation: EAW48278.1.
    CH471051 Genomic DNA. Translation: EAW48279.1.
    CH471051 Genomic DNA. Translation: EAW48281.1.
    CH471051 Genomic DNA. Translation: EAW48282.1.
    CH471051 Genomic DNA. Translation: EAW48283.1.
    BC032496 mRNA. Translation: AAH32496.1.
    CCDSiCCDS5094.1. [P06241-1]
    CCDS5095.1. [P06241-2]
    CCDS5096.1. [P06241-3]
    PIRiA24314. TVHUSY.
    RefSeqiNP_002028.1. NM_002037.5. [P06241-1]
    NP_694592.1. NM_153047.3. [P06241-2]
    NP_694593.1. NM_153048.3. [P06241-3]
    XP_005266944.1. XM_005266887.1. [P06241-1]
    XP_005266945.1. XM_005266888.1. [P06241-1]
    XP_005266946.1. XM_005266889.1. [P06241-1]
    XP_005266947.1. XM_005266890.1. [P06241-2]
    XP_005266949.1. XM_005266892.1. [P06241-3]
    XP_006715492.1. XM_006715429.1. [P06241-1]
    UniGeneiHs.390567.
    Hs.664520.

    Genome annotation databases

    EnsembliENST00000229471; ENSP00000229471; ENSG00000010810. [P06241-3]
    ENST00000354650; ENSP00000346671; ENSG00000010810. [P06241-1]
    ENST00000368667; ENSP00000357656; ENSG00000010810. [P06241-1]
    ENST00000368678; ENSP00000357667; ENSG00000010810. [P06241-2]
    ENST00000368682; ENSP00000357671; ENSG00000010810. [P06241-2]
    ENST00000538466; ENSP00000440646; ENSG00000010810. [P06241-2]
    GeneIDi2534.
    KEGGihsa:2534.
    UCSCiuc003pvh.3. human. [P06241-2]
    uc003pvi.3. human. [P06241-3]
    uc003pvj.3. human. [P06241-1]

    Polymorphism databases

    DMDMi125370.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14676 mRNA. Translation: AAA36615.1 .
    M14333 mRNA. Translation: AAC08285.1 .
    S74774 mRNA. Translation: AAB33113.2 .
    AB451293 mRNA. Translation: BAG70107.1 .
    AB451426 mRNA. Translation: BAG70240.1 .
    Z97989 Genomic DNA. Translation: CAI22300.1 .
    Z97989 Genomic DNA. Translation: CAI22301.1 .
    CH471051 Genomic DNA. Translation: EAW48278.1 .
    CH471051 Genomic DNA. Translation: EAW48279.1 .
    CH471051 Genomic DNA. Translation: EAW48281.1 .
    CH471051 Genomic DNA. Translation: EAW48282.1 .
    CH471051 Genomic DNA. Translation: EAW48283.1 .
    BC032496 mRNA. Translation: AAH32496.1 .
    CCDSi CCDS5094.1. [P06241-1 ]
    CCDS5095.1. [P06241-2 ]
    CCDS5096.1. [P06241-3 ]
    PIRi A24314. TVHUSY.
    RefSeqi NP_002028.1. NM_002037.5. [P06241-1 ]
    NP_694592.1. NM_153047.3. [P06241-2 ]
    NP_694593.1. NM_153048.3. [P06241-3 ]
    XP_005266944.1. XM_005266887.1. [P06241-1 ]
    XP_005266945.1. XM_005266888.1. [P06241-1 ]
    XP_005266946.1. XM_005266889.1. [P06241-1 ]
    XP_005266947.1. XM_005266890.1. [P06241-2 ]
    XP_005266949.1. XM_005266892.1. [P06241-3 ]
    XP_006715492.1. XM_006715429.1. [P06241-1 ]
    UniGenei Hs.390567.
    Hs.664520.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A0N NMR - B 80-148 [» ]
    1AOT NMR - F 143-248 [» ]
    1AOU NMR - F 143-248 [» ]
    1AVZ X-ray 3.00 C 85-141 [» ]
    1AZG NMR - B 82-148 [» ]
    1EFN X-ray 2.50 A/C 86-143 [» ]
    1FYN X-ray 2.30 A 81-142 [» ]
    1G83 X-ray 2.60 A/B 82-246 [» ]
    1M27 X-ray 2.50 C 84-144 [» ]
    1NYF NMR - A 82-148 [» ]
    1NYG NMR - A 82-148 [» ]
    1SHF X-ray 1.90 A/B 84-142 [» ]
    1ZBJ NMR - A 84-142 [» ]
    2DQ7 X-ray 2.80 X 261-537 [» ]
    3H0F X-ray 2.61 A 73-142 [» ]
    3H0H X-ray 1.76 A 73-142 [» ]
    3H0I X-ray 2.20 A/B 73-142 [» ]
    3UA6 X-ray 1.85 A/B 81-143 [» ]
    3UA7 X-ray 1.50 A/B/C/D 81-143 [» ]
    4D8D X-ray 2.52 A/C 84-141 [» ]
    4EIK X-ray 1.60 A 81-143 [» ]
    ProteinModelPortali P06241.
    SMRi P06241. Positions 81-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108810. 139 interactions.
    DIPi DIP-33876N.
    IntActi P06241. 212 interactions.
    MINTi MINT-93594.
    STRINGi 9606.ENSP00000357656.

    Chemistry

    BindingDBi P06241.
    ChEMBLi CHEMBL1841.
    DrugBanki DB01254. Dasatinib.
    GuidetoPHARMACOLOGYi 2026.

    PTM databases

    PhosphoSitei P06241.

    Polymorphism databases

    DMDMi 125370.

    Proteomic databases

    MaxQBi P06241.
    PaxDbi P06241.
    PRIDEi P06241.

    Protocols and materials databases

    DNASUi 2534.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229471 ; ENSP00000229471 ; ENSG00000010810 . [P06241-3 ]
    ENST00000354650 ; ENSP00000346671 ; ENSG00000010810 . [P06241-1 ]
    ENST00000368667 ; ENSP00000357656 ; ENSG00000010810 . [P06241-1 ]
    ENST00000368678 ; ENSP00000357667 ; ENSG00000010810 . [P06241-2 ]
    ENST00000368682 ; ENSP00000357671 ; ENSG00000010810 . [P06241-2 ]
    ENST00000538466 ; ENSP00000440646 ; ENSG00000010810 . [P06241-2 ]
    GeneIDi 2534.
    KEGGi hsa:2534.
    UCSCi uc003pvh.3. human. [P06241-2 ]
    uc003pvi.3. human. [P06241-3 ]
    uc003pvj.3. human. [P06241-1 ]

    Organism-specific databases

    CTDi 2534.
    GeneCardsi GC06M111981.
    HGNCi HGNC:4037. FYN.
    HPAi CAB005034.
    CAB018387.
    HPA023887.
    MIMi 137025. gene.
    neXtProti NX_P06241.
    PharmGKBi PA28454.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG008761.
    InParanoidi P06241.
    KOi K05703.
    OMAi SHNSGYR.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P06241.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_11068. Nef and signal transduction.
    REACT_111040. Signaling by SCF-KIT.
    REACT_111225. Regulation of KIT signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_12519. PECAM1 interactions.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_147814. DAP12 signaling.
    REACT_160274. FCGR activation.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_19183. CD28 co-stimulation.
    REACT_19199. CRMPs in Sema3A signaling.
    REACT_19236. Sema3A PAK dependent Axon repulsion.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_22351. DCC mediated attractive signaling.
    REACT_22384. Netrin mediated repulsion signals.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23832. Nephrin interactions.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P06241.

    Miscellaneous databases

    ChiTaRSi FYN. human.
    EvolutionaryTracei P06241.
    GeneWikii FYN.
    GenomeRNAii 2534.
    NextBioi 9997.
    PMAP-CutDB P06241.
    PROi P06241.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06241.
    Bgeei P06241.
    CleanExi HS_FYN.
    Genevestigatori P06241.

    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. "Isolation and oncogenic potential of a novel human src-like gene."
      Kawakami T., Pennington C.Y., Robbins K.C.
      Mol. Cell. Biol. 6:4195-4201(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "Human p59fyn(T) regulates OKT3-induced calcium influx by a mechanism distinct from PIP2 hydrolysis in Jurkat T cells."
      Rigley K., Slocombe P., Proudfoot K., Wahid S., Mandair K., Bebbington C.
      J. Immunol. 154:1136-1145(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
      Tissue: T-cell.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 3).
      Tissue: Blood.
    8. "In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts."
      Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.
      Oncogene 5:1313-1319(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYR-531.
    9. "Regulation of the p59fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase."
      Mustelin T., Pessa-Morikawa T., Autero M., Gassmann M., Andersson L.C., Gahmberg C.G., Burn P.
      Eur. J. Immunol. 22:1173-1178(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPHOSPHORYLATION AT TYR-531 BY PTPRC.
    10. "Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells."
      Prasad K.V., Janssen O., Kapeller R., Raab M., Cantley L.C., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 90:7366-7370(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIK3R1.
    11. "Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization."
      Alland L., Peseckis S.M., Atherton R.E., Berthiaume L., Resh M.D.
      J. Biol. Chem. 269:16701-16705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION.
    12. "p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: implications for T-cell costimulation."
      Raab M., Cai Y.C., Bunnell S.C., Heyeck S.D., Berg L.J., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 92:8891-8895(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CD28.
    13. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
      Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
      J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT.
    14. "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production."
      da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.
      Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FYB.
      Tissue: Tonsil.
    15. "A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth."
      Wary K.K., Mariotti A., Zurzolo C., Giancotti F.G.
      Cell 94:625-634(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAV1.
    16. "Altered expression of tyrosine kinases of the Src and Syk families in human T-cell leukemia virus type 1-infected T-cell lines."
      Weil R., Levraud J.P., Dodon M.D., Bessia C., Hazan U., Kourilsky P., Israel A.
      J. Virol. 73:3709-3717(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, ALTERNATIVE SPLICING.
    17. "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity."
      Choi S., Park S.
      Oncogene 18:5413-5422(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHA8.
    18. "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
      Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
      J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAG1.
    19. "T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase."
      Huang J., Tilly D., Altman A., Sugie K., Grey H.M.
      Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF VAV1.
    20. "Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125."
      Nakamura T., Yamashita H., Takahashi T., Nakamura S.
      Biochem. Biophys. Res. Commun. 280:1085-1092(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SNCA.
    21. "The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
      Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
      J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
    22. "Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation."
      Wolf R.M., Wilkes J.J., Chao M.V., Resh M.D.
      J. Neurobiol. 49:62-78(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "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: SUBCELLULAR LOCATION.
    24. "p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn."
      Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T.
      Biochem. Biophys. Res. Commun. 306:151-155(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ARHGAP32.
    25. Cited for: FUNCTION IN PHOSPHORYLATION OF TRPC6.
    26. "Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone guidance."
      Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I., McFarlane S., Bloch-Gallego E., Lamarche-Vane N.
      J. Cell Biol. 167:687-698(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation."
      Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.
      J. Exp. Med. 199:99-112(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF WAS.
    28. "Unc119, a novel activator of Lck/Fyn, is essential for T cell activation."
      Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.
      J. Exp. Med. 199:369-379(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC119.
    29. "Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation."
      Palacios E.H., Weiss A.
      Oncogene 23:7990-8000(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    30. Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2.
    31. "Regulation of ultraviolet B-induced phosphorylation of histone H3 at serine 10 by Fyn kinase."
      He Z., Cho Y.Y., Ma W.Y., Choi H.S., Bode A.M., Dong Z.
      J. Biol. Chem. 280:2446-2454(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-12, SUBCELLULAR LOCATION.
    32. "Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation."
      Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C.
      Mol. Cell 21:135-141(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITCH, FUNCTION.
    33. "Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival."
      Tang X., Feng Y., Ye K.
      Cell Death Differ. 14:368-377(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF AGAP2.
    34. "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain."
      Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.
      J. Biol. Chem. 282:36444-36453(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT8.
    35. "Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA."
      Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P., Bustelo X.R., Garcia de Herreros A., Dunach M.
      Mol. Cell. Biol. 27:1745-1757(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1.
    36. "Regulation of FynT function by dual domain docking on PAG/Cbp."
      Solheim S.A., Torgersen K.M., Tasken K., Berge T.
      J. Biol. Chem. 283:2773-2783(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PAG1.
    37. "Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2."
      Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T., Hattori S.
      J. Biol. Chem. 283:9177-9186(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF KIRREL.
    38. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    39. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    41. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    42. "Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and activation of phospholipase C-{gamma}1."
      Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T., Ohsawa I., Ohta S., Hattori S.
      J. Biol. Chem. 284:8951-8962(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NPHS1.
    43. "Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation of collapsin response mediator protein 2 at tyrosine 32."
      Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y., Nakamura F., Goshima Y.
      J. Biol. Chem. 284:27393-27401(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2.
    44. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
      Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.
      J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RUNX3.
    46. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    47. "T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice."
      Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C., Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.
      J. Clin. Invest. 121:4758-4774(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION AT TYR-420 BY PTPN2.
    48. "Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin."
      Noble M.E.M., Musacchio A., Saraste M., Courtneidge S.A., Wierenga R.K.
      EMBO J. 12:2617-2624(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
    49. "High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides."
      Musacchio A., Saraste M., Wilmanns M.
      Nat. Struct. Biol. 1:546-551(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-142.
    50. "Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase."
      Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C., Waterfield M.D., Campbell I.D., Ladbury J.E.
      Biochemistry 35:15646-15653(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    51. "Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain."
      Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J.
      Cell 85:931-942(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 85-141 IN COMPLEX WITH NEF.
    52. "Solution structure and peptide binding of the SH3 domain from human Fyn."
      Morton C.J., Pugh D.J.R., Brown E.L.J., Kahmann J.D., Renzoni D.A.C., Campbell I.D.
      Structure 4:705-714(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
    53. "The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity."
      Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.
      Structure 5:1313-1323(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
    54. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1 AND SH2D1A.
    55. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-243; ARG-410 AND GLU-506.

    Entry informationi

    Entry nameiFYN_HUMAN
    AccessioniPrimary (citable) accession number: P06241
    Secondary accession number(s): B5BU57
    , E1P557, H0UI48, Q16248, Q5R3A6, Q5R3A7, Q8N5D7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 192 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3