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P39688

- FYN_MOUSE

UniProt

P39688 - FYN_MOUSE

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Protein

Tyrosine-protein kinase Fyn

Gene

Fyn

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 similarity

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

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

ReactomeiREACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_204081. CD28 co-stimulation.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_227425. Regulation of KIT signaling.
REACT_237796. NCAM signaling for neurite out-growth.
REACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_244852. CRMPs in Sema3A signaling.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_248291. DCC mediated attractive signaling.
REACT_254306. Sema3A PAK dependent Axon repulsion.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261451. CD28 dependent Vav1 pathway.
REACT_261568. CTLA4 inhibitory signaling.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:95602. Fyn.

Subcellular locationi

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

GO - Cellular componenti

  1. actin filament Source: MGI
  2. cell periphery Source: MGI
  3. cytosol Source: Reactome
  4. endosome Source: MGI
  5. membrane raft Source: Ensembl
  6. mitochondrion Source: Ensembl
  7. nucleus Source: UniProtKB-KW
  8. plasma membrane Source: UniProtKB-KW
  9. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes myristoylation and palmitoylation. 1 Publication
Mutagenesisi3 – 31C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. 3 Publications
Mutagenesisi3 – 31C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. 3 Publications
Mutagenesisi6 – 61C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. 2 Publications
Mutagenesisi6 – 61C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. 2 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP39688.
PRIDEiP39688.

PTM databases

PhosphoSiteiP39688.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP39688.
CleanExiMM_FYN.
ExpressionAtlasiP39688. baseline and differential.
GenevestigatoriP39688.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP39688.
KOiK05703.
OMAiSHNSGYR.
TreeFamiTF351634.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

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

Also known as: B

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

« Hide

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

Alternative sequence

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

Sequence databases

Select the link destinations:
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_006512539.1. [P39688-1]
XP_006512603.1. XM_006512540.1. [P39688-1]
UniGeneiMm.4848.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
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 .
CCDSi CCDS23788.1. [P39688-2 ]
CCDS48538.1. [P39688-1 ]
PIRi A44991.
RefSeqi NP_001116364.1. NM_001122892.1. [P39688-2 ]
NP_001116365.1. NM_001122893.1. [P39688-1 ]
NP_032080.2. NM_008054.2. [P39688-2 ]
XP_006512602.1. XM_006512539.1. [P39688-1 ]
XP_006512603.1. XM_006512540.1. [P39688-1 ]
UniGenei Mm.4848.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLi CHEMBL4517.

PTM databases

PhosphoSitei P39688.

Proteomic databases

PaxDbi P39688.
PRIDEi P39688.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 2534.
MGIi MGI:95602. Fyn.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P39688.
KOi K05703.
OMAi SHNSGYR.
TreeFami TF351634.

Enzyme and pathway databases

Reactomei REACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198634. Regulation of signaling by CBL.
REACT_204081. CD28 co-stimulation.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_227425. Regulation of KIT signaling.
REACT_237796. NCAM signaling for neurite out-growth.
REACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_244852. CRMPs in Sema3A signaling.
REACT_246154. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_248291. DCC mediated attractive signaling.
REACT_254306. Sema3A PAK dependent Axon repulsion.
REACT_257032. Nephrin interactions.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261451. CD28 dependent Vav1 pathway.
REACT_261568. CTLA4 inhibitory signaling.

Miscellaneous databases

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

Gene expression databases

Bgeei P39688.
CleanExi MM_FYN.
ExpressionAtlasi P39688. baseline and differential.
Genevestigatori P39688.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiFYN_MOUSE
AccessioniPrimary (citable) accession number: P39688
Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2013
Last modified: November 26, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3