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P06241 (FYN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 187. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FYN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.12 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.41 Ref.42 Ref.44 Ref.46

Catalytic activity

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

Cofactor

Manganese.

Enzyme regulation

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

Subunit structure

Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) By similarity. Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via N-terminus) By similarity. Interacts with SH2D1A and SLAMF1. Interacts (via its SH3 domain) with HEV ORF3 protein. Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.31 Ref.33 Ref.40 Ref.44

Subcellular location

Cytoplasm. Nucleus. Cell membrane. Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking. Ref.23 Ref.30

Tissue specificity

Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. Ref.16

Post-translational modification

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. Ref.8 Ref.9 Ref.16 Ref.30 Ref.46

Palmitoylation at Cys-3 and Cys-6 regulates subcellular location By similarity. Ref.11

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Host-virus interaction
Immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Inferred from direct assay PubMed 7722293. Source: UniProtKB

activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transport

Non-traceable author statement Ref.3. Source: UniProtKB

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

detection of mechanical stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

feeding behavior

Traceable author statement PubMed 8264796. Source: ProtInc

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

forebrain development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement PubMed 1361685. Source: ProtInc

learning

Traceable author statement PubMed 1361685. Source: ProtInc

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Non-traceable author statement Ref.3. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome

Inferred from direct assay PubMed 15611048. Source: HGNC

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 12150984. Source: BHF-UCL

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor binding

Inferred from physical interaction Ref.17. Source: UniProtKB

glycoprotein binding

Inferred from physical interaction PubMed 16831868. Source: BHF-UCL

growth factor receptor binding

Inferred from physical interaction PubMed 16479011. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Non-traceable author statement Ref.3. Source: UniProtKB

protein tyrosine kinase activity

Inferred from experiment. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06241-1)

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.
Isoform 2 (identifier: P06241-2)

Also known as: T;

The sequence of this isoform differs from the canonical sequence as follows:
     234-287: RAAGLCCRLV...GNGQFGEVWM → KADGLCFNLT...GQGCFAEVWL
Isoform 3 (identifier: P06241-3)

The sequence of this isoform differs from the canonical sequence as follows:
     233-287: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 537536Tyrosine-protein kinase Fyn
PRO_0000088099

Regions

Domain82 – 14362SH3
Domain149 – 24698SH2
Domain271 – 524254Protein kinase
Nucleotide binding277 – 2859ATP By similarity

Sites

Active site3901Proton acceptor By similarity
Binding site2991ATP By similarity

Amino acid modifications

Modified residue121Phosphothreonine; by PKC Ref.30
Modified residue151Phosphothreonine
Modified residue211Phosphoserine Ref.37 Ref.38 Ref.39 Ref.43 Ref.45
Modified residue251Phosphoserine
Modified residue1851Phosphotyrosine By similarity
Modified residue2131Phosphotyrosine
Modified residue2141Phosphotyrosine
Modified residue2571Phosphoserine
Modified residue4201Phosphotyrosine; by autocatalysis Ref.46
Modified residue4401Phosphotyrosine
Modified residue5121Phosphothreonine
Modified residue5311Phosphotyrosine; by CSK Ref.8 Ref.9 Ref.38
Lipidation21N-myristoyl glycine Ref.8
Lipidation31S-palmitoyl cysteine By similarity
Lipidation61S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence233 – 28755Missing in isoform 3.
VSP_024108
Alternative sequence234 – 28754RAAGL…GEVWM → KADGLCFNLTVIASSCTPQT SGLAKDAWEVARRSLCLEKK LGQGCFAEVWL in isoform 2.
VSP_024110
Natural variant2431V → L in a lung squamous cell carcinoma sample; somatic mutation. Ref.54
VAR_041704
Natural variant4101G → R in a metastatic melanoma sample; somatic mutation. Ref.54
VAR_041705
Natural variant4451I → F.
Corresponds to variant rs1801121 [ dbSNP | Ensembl ].
VAR_014661
Natural variant5061D → E. Ref.54
Corresponds to variant rs28763975 [ dbSNP | Ensembl ].
VAR_041706

Experimental info

Sequence conflict1841A → S in AAA36615. Ref.1
Sequence conflict4371A → R in AAA36615. Ref.1
Sequence conflict4371A → R in AAB33113. Ref.3

Secondary structure

.................................................................................... 537
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4A1E443A4B5A0977

FASTA53760,762
        10         20         30         40         50         60 
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 

        70         80         90        100        110        120 
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 

       130        140        150        160        170        180 
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 

       190        200        210        220        230        240 
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 

       250        260        270        280        290        300 
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 

       310        320        330        340        350        360 
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR 

       370        380        390        400        410        420 
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 

       430        440        450        460        470        480 
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 

       490        500        510        520        530 
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL 

« Hide

Isoform 2 (T) [UniParc].

Checksum: FA082D40A24C2802
Show »

FASTA53460,141
Isoform 3 [UniParc].

Checksum: 055C3965AC5A9135
Show »

FASTA48254,513

References

« Hide 'large scale' references
[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]"Yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family."
Semba K., Nishizawa M., Miyajima N., Yoshida M.C., Sukegawa J., Yamanashi Y., Sasaki M., Yamamoto T., Toyoshima K.
Proc. Natl. Acad. Sci. U.S.A. 83:5459-5463(1986) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Regulation of TRPC6 channel activity by tyrosine phosphorylation."
Hisatsune C., Kuroda Y., Nakamura K., Inoue T., Nakamura T., Michikawa T., Mizutani A., Mikoshiba K.
J. Biol. Chem. 279:18887-18894(2004) [PubMed] [Europe PMC] [Abstract]
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]"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.
[29]"Fyn phosphorylates human MAP-2c on tyrosine 67."
Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.
J. Biol. Chem. 280:1962-1970(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[38]"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.
[39]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[40]"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.
[41]"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.
[42]"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.
[43]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"SAP couples Fyn to SLAM immune receptors."
Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J.
Nat. Cell Biol. 5:155-160(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1 AND SH2D1A.
[54]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTVHUSY. A24314.
RefSeqNP_002028.1. NM_002037.5.
NP_694592.1. NM_153047.3.
NP_694593.1. NM_153048.3.
XP_005266944.1. XM_005266887.1.
XP_005266945.1. XM_005266888.1.
XP_005266946.1. XM_005266889.1.
XP_005266947.1. XM_005266890.1.
XP_005266949.1. XM_005266892.1.
UniGeneHs.390567.
Hs.664520.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0NNMR-B82-148[»]
1AOTNMR-F143-248[»]
1AOUNMR-F143-248[»]
1AVZX-ray3.00C85-140[»]
1AZGNMR-B82-148[»]
1EFNX-ray2.50A/C86-143[»]
1FYNX-ray2.30A81-142[»]
1G83X-ray2.60A/B82-245[»]
1M27X-ray2.50C84-144[»]
1NYFNMR-A82-148[»]
1NYGNMR-A82-148[»]
1SHFX-ray1.90A/B84-142[»]
1ZBJNMR-A84-141[»]
2DQ7X-ray2.80X261-536[»]
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[»]
ProteinModelPortalP06241.
SMRP06241. Positions 81-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108810. 139 interactions.
DIPDIP-33876N.
IntActP06241. 208 interactions.
MINTMINT-93594.
STRING9606.ENSP00000357656.

Chemistry

BindingDBP06241.
ChEMBLCHEMBL1841.
DrugBankDB01254. Dasatinib.
GuidetoPHARMACOLOGY2026.

PTM databases

PhosphoSiteP06241.

Polymorphism databases

DMDM125370.

Proteomic databases

PaxDbP06241.
PRIDEP06241.

Protocols and materials databases

DNASU2534.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229471; ENSP00000229471; ENSG00000010810. [P06241-3]
ENST00000354650; ENSP00000346671; ENSG00000010810. [P06241-1]
ENST00000356013; ENSP00000348295; ENSG00000010810. [P06241-3]
ENST00000368667; ENSP00000357656; ENSG00000010810. [P06241-1]
ENST00000368678; ENSP00000357667; ENSG00000010810. [P06241-2]
ENST00000368682; ENSP00000357671; ENSG00000010810. [P06241-2]
ENST00000538466; ENSP00000440646; ENSG00000010810. [P06241-2]
GeneID2534.
KEGGhsa:2534.
UCSCuc003pvh.3. human. [P06241-2]
uc003pvi.3. human. [P06241-3]
uc003pvj.3. human. [P06241-1]

Organism-specific databases

CTD2534.
GeneCardsGC06M111981.
HGNCHGNC:4037. FYN.
HPACAB005034.
CAB018387.
HPA023887.
MIM137025. gene.
neXtProtNX_P06241.
PharmGKBPA28454.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG008761.
InParanoidP06241.
KOK05703.
OMANNFHATG.
OrthoDBEOG7GTT2V.
PhylomeDBP06241.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP06241.

Gene expression databases

ArrayExpressP06241.
BgeeP06241.
CleanExHS_FYN.
GenevestigatorP06241.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

ChiTaRSFYN. human.
EvolutionaryTraceP06241.
GeneWikiFYN.
GenomeRNAi2534.
NextBio9997.
PMAP-CutDBP06241.
PROP06241.
SOURCESearch...

Entry information

Entry nameFYN_HUMAN
AccessionPrimary (citable) accession number: P06241
Secondary accession number(s): B5BU57 expand/collapse secondary AC list , E1P557, H0UI48, Q16248, Q5R3A6, Q5R3A7, Q8N5D7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 187 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM