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Protein

Tyrosine-protein kinase Fyn

Gene

Fyn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1 (By similarity).By similarity4 Publications

Catalytic activityi

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

Cofactori

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei299ATPPROSITE-ProRule annotation1
Active sitei390Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi277 – 285ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ephrin receptor binding Source: MGI
  • glycoprotein binding Source: MGI
  • G-protein coupled receptor binding Source: UniProtKB
  • growth factor receptor binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • protein kinase activity Source: MGI
  • protein tyrosine kinase activity Source: MGI
  • tubulin binding Source: MGI

GO - Biological processi

  • activated T cell proliferation Source: MGI
  • adaptive immune response Source: UniProtKB-KW
  • axon guidance Source: Reactome
  • cell surface receptor signaling pathway Source: MGI
  • cellular response to peptide hormone stimulus Source: Ensembl
  • cellular response to platelet-derived growth factor stimulus Source: MGI
  • cellular response to transforming growth factor beta stimulus Source: MGI
  • dendrite morphogenesis Source: MGI
  • detection of mechanical stimulus involved in sensory perception of pain Source: MGI
  • ephrin receptor signaling pathway Source: Reactome
  • forebrain development Source: MGI
  • innate immune response Source: GO_Central
  • myelination Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein catabolic process Source: MGI
  • negative regulation of protein ubiquitination Source: MGI
  • neuron migration Source: MGI
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • positive regulation of protein localization to nucleus Source: CACAO
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: CACAO
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • regulation of apoptotic process Source: GO_Central
  • regulation of cell proliferation Source: GO_Central
  • regulation of cell shape Source: MGI
  • response to drug Source: Ensembl
  • response to ethanol Source: MGI
  • T cell receptor signaling pathway Source: MGI
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2424491. DAP12 signaling.
R-MMU-373753. Nephrin interactions.
R-MMU-375165. NCAM signaling for neurite out-growth.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-389359. CD28 dependent Vav1 pathway.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928664. Ephrin signaling.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-418885. DCC mediated attractive signaling.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-75892. Platelet Adhesion to exposed collagen.
R-MMU-8866376. Reelin signalling pathway.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fyn (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fyn
p59-Fyn
Gene namesi
Name:Fyn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:95602. Fyn.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell membrane By similarity

  • Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking (By similarity).By similarity

GO - Cellular componenti

  • actin filament Source: MGI
  • cell periphery Source: MGI
  • cytosol Source: Reactome
  • endosome Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • membrane raft Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Abolishes myristoylation and palmitoylation. 1 Publication1
Mutagenesisi3C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. 3 Publications1
Mutagenesisi3C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. 3 Publications1
Mutagenesisi6C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. 2 Publications1
Mutagenesisi6C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. 2 Publications1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL4517.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000881002 – 537Tyrosine-protein kinase FynAdd BLAST536

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteine3 Publications1
Lipidationi6S-palmitoyl cysteine2 Publications1
Modified residuei21PhosphoserineCombined sources1
Modified residuei26PhosphoserineBy similarity1
Modified residuei185PhosphotyrosineCombined sources1
Modified residuei420Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei531PhosphotyrosineCombined sources1 Publication1
Modified residuei531Phosphotyrosine; by CSKBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

EPDiP39688.
MaxQBiP39688.
PaxDbiP39688.
PeptideAtlasiP39688.
PRIDEiP39688.

PTM databases

iPTMnetiP39688.
PhosphoSitePlusiP39688.
SwissPalmiP39688.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000019843.
CleanExiMM_FYN.
ExpressionAtlasiP39688. baseline and differential.
GenevisibleiP39688. MM.

Interactioni

Subunit structurei

Interacts (via its SH3 domain) with PIK3R1 and PRMT8 (By similarity). Interacts with FYB, PAG1, and SH2D1A (By similarity). Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity (PubMed:8168489). Interacts with TOM1L1 (phosphorylated form) (PubMed:11711534). Interacts with SH2D1A and SLAMF1 (By similarity). Interacts with and phosphorylates ITCH, down-regulating its activity (By similarity). Interacts with FASLG (By similarity). Interacts with RUNX3 (By similarity). Interacts with KIT (By similarity). Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion (By similarity). Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation (By similarity). Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway (By similarity). Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts with KDR (tyrosine phosphorylated) (PubMed:16966330). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (PubMed:7681396, PubMed:9312046). Interacts with UNC119 (By similarity). Interacts (via SH2 domain) with PTPRH (phosphorylated form) (PubMed:20398064). Interacts with PTPRO (phosphorylated form) (PubMed:20398064). Interacts with PTPRB (phosphorylated form) (PubMed:20398064).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226813EBI-524514,EBI-518228From a different organism.
Dynlt1P518073EBI-524514,EBI-642797
FZD2Q143324EBI-524514,EBI-6254477From a different organism.
Irs1P355704EBI-524514,EBI-520230From a different organism.
Khdrbs1Q6074915EBI-524514,EBI-519077
Khdrbs2Q9WU012EBI-524514,EBI-8339046
PdgfrbP056223EBI-524514,EBI-1554855
PLXNA2O750513EBI-524514,EBI-308264From a different organism.
PTPRAP184332EBI-524514,EBI-2609645From a different organism.
Slamf1Q9QUM44EBI-524514,EBI-7910086
Sphk2Q9JIA72EBI-524514,EBI-985434

GO - Molecular functioni

  • ephrin receptor binding Source: MGI
  • G-protein coupled receptor binding Source: UniProtKB
  • growth factor receptor binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • tubulin binding Source: MGI

Protein-protein interaction databases

BioGridi199773. 12 interactors.
DIPiDIP-198N.
IntActiP39688. 38 interactors.
MINTiMINT-85422.
STRINGi10090.ENSMUSP00000097547.

Chemistry databases

BindingDBiP39688.

Structurei

Secondary structure

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi87 – 91Combined sources5
Beta strandi108 – 113Combined sources6
Beta strandi115 – 124Combined sources10
Turni125 – 127Combined sources3
Beta strandi130 – 134Combined sources5
Helixi135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Helixi156 – 163Combined sources8
Beta strandi173 – 177Combined sources5
Beta strandi179 – 181Combined sources3
Beta strandi185 – 192Combined sources8
Beta strandi194 – 207Combined sources14
Beta strandi213 – 216Combined sources4
Beta strandi221 – 223Combined sources3
Helixi224 – 233Combined sources10
Beta strandi238 – 240Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UF4X-ray1.98A82-244[»]
ProteinModelPortaliP39688.
SMRiP39688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 143SH3PROSITE-ProRule annotationAdd BLAST62
Domaini149 – 246SH2PROSITE-ProRule annotationAdd BLAST98
Domaini271 – 524Protein kinasePROSITE-ProRule annotationAdd BLAST254

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP39688.
KOiK05703.
OMAiSHNSGYR.
OrthoDBiEOG091G0D46.
TreeFamiTF351634.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P39688-1) [UniParc]FASTAAdd to basket
Also known as: B

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

« Hide

        10         20         30         40         50
MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY
60 70 80 90 100
NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD
110 120 130 140 150
LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY
160 170 180 190 200
FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV
210 220 230 240 250
KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM
260 270 280 290 300
PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
310 320 330 340 350
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL
360 370 380 390 400
LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN
410 420 430 440 450
GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW
460 470 480 490 500
SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI
510 520 530
HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
Length:537
Mass (Da):60,675
Last modified:April 3, 2013 - v4
Checksum:i99558702596DAEE0
GO
Isoform 2 (identifier: P39688-2) [UniParc]FASTAAdd to basket
Also known as: T

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti179E → Q in AAA37644 (PubMed:2488273).Curated1
Sequence conflicti179E → Q in AAB09568 (PubMed:9895129).Curated1
Sequence conflicti432W → R in BAE42585 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024111234 – 236RAA → KAD in isoform 2. 4 Publications3
Alternative sequenceiVSP_024112240 – 287CRLVV…GEVWM → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF AEVWL in isoform 2. 4 PublicationsAdd BLAST48

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27266 mRNA. Translation: AAA37644.1.
U70324 mRNA. Translation: AAB09568.1.
AK156584 mRNA. Translation: BAE33766.1.
AK171646 mRNA. Translation: BAE42585.1.
BC032149 mRNA. Translation: AAH32149.1.
BC092217 mRNA. Translation: AAH92217.1.
CCDSiCCDS23788.1. [P39688-2]
CCDS48538.1. [P39688-1]
PIRiA44991.
RefSeqiNP_001116364.1. NM_001122892.1. [P39688-2]
NP_001116365.1. NM_001122893.1. [P39688-1]
NP_032080.2. NM_008054.2. [P39688-2]
XP_006512602.1. XM_006512539.3. [P39688-1]
XP_006512603.1. XM_006512540.3. [P39688-1]
XP_011241419.1. XM_011243117.2. [P39688-1]
UniGeneiMm.4848.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27266 mRNA. Translation: AAA37644.1.
U70324 mRNA. Translation: AAB09568.1.
AK156584 mRNA. Translation: BAE33766.1.
AK171646 mRNA. Translation: BAE42585.1.
BC032149 mRNA. Translation: AAH32149.1.
BC092217 mRNA. Translation: AAH92217.1.
CCDSiCCDS23788.1. [P39688-2]
CCDS48538.1. [P39688-1]
PIRiA44991.
RefSeqiNP_001116364.1. NM_001122892.1. [P39688-2]
NP_001116365.1. NM_001122893.1. [P39688-1]
NP_032080.2. NM_008054.2. [P39688-2]
XP_006512602.1. XM_006512539.3. [P39688-1]
XP_006512603.1. XM_006512540.3. [P39688-1]
XP_011241419.1. XM_011243117.2. [P39688-1]
UniGeneiMm.4848.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UF4X-ray1.98A82-244[»]
ProteinModelPortaliP39688.
SMRiP39688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199773. 12 interactors.
DIPiDIP-198N.
IntActiP39688. 38 interactors.
MINTiMINT-85422.
STRINGi10090.ENSMUSP00000097547.

Chemistry databases

BindingDBiP39688.
ChEMBLiCHEMBL4517.

PTM databases

iPTMnetiP39688.
PhosphoSitePlusiP39688.
SwissPalmiP39688.

Proteomic databases

EPDiP39688.
MaxQBiP39688.
PaxDbiP39688.
PeptideAtlasiP39688.
PRIDEiP39688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2534.
MGIiMGI:95602. Fyn.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP39688.
KOiK05703.
OMAiSHNSGYR.
OrthoDBiEOG091G0D46.
TreeFamiTF351634.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-2424491. DAP12 signaling.
R-MMU-373753. Nephrin interactions.
R-MMU-375165. NCAM signaling for neurite out-growth.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389357. CD28 dependent PI3K/Akt signaling.
R-MMU-389359. CD28 dependent Vav1 pathway.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928664. Ephrin signaling.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-399954. Sema3A PAK dependent Axon repulsion.
R-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-MMU-399956. CRMPs in Sema3A signaling.
R-MMU-418885. DCC mediated attractive signaling.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-75892. Platelet Adhesion to exposed collagen.
R-MMU-8866376. Reelin signalling pathway.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

ChiTaRSiFyn. mouse.
PROiP39688.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019843.
CleanExiMM_FYN.
ExpressionAtlasiP39688. baseline and differential.
GenevisibleiP39688. MM.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiFYN_MOUSE
AccessioniPrimary (citable) accession number: P39688
Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2013
Last modified: November 30, 2016
This is version 177 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.