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Protein

Tyrosine-protein kinase Fyn

Gene

Fyn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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, KIRREL1 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. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. 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 similarity4 Publications

Catalytic activityi

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

Cofactori

Activity 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

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Kinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Immunity
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-1227986 Signaling by ERBB2
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-2029481 FCGR activation
R-MMU-2424491 DAP12 signaling
R-MMU-373753 Nephrin family 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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:95602 Fyn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 Expressed in 321 organ(s), highest expression level in cranial nerve II
CleanExiMM_FYN
ExpressionAtlasiP39688 baseline and differential
GenevisibleiP39688 MM

Interactioni

Subunit structurei

Interacts (via its SH3 domain) with PIK3R1 and PRMT8 (By similarity). Interacts with FYB1, 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). Interacts with FYB2 (By similarity).By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199773, 14 interactors
CORUMiP39688
DIPiDIP-198N
ELMiP39688
IntActiP39688, 41 interactors
MINTiP39688
STRINGi10090.ENSMUSP00000097547

Chemistry databases

BindingDBiP39688

Structurei

Secondary structure

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

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

Family and domain databases

CDDicd12006 SH3_Fyn_Yrk, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR035750 Fyn/Yrk_SH3
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

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

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YZ57D3YZ57_MOUSE
Tyrosine-protein kinase
Fyn
482Annotation score:
D3YZA2D3YZA2_MOUSE
Tyrosine-protein kinase Fyn
Fyn
114Annotation score:
D3YVZ0D3YVZ0_MOUSE
Tyrosine-protein kinase Fyn
Fyn
36Annotation score:

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

Similar proteinsi

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, 14 interactors
CORUMiP39688
DIPiDIP-198N
ELMiP39688
IntActiP39688, 41 interactors
MINTiP39688
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-1227986 Signaling by ERBB2
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-2029481 FCGR activation
R-MMU-2424491 DAP12 signaling
R-MMU-373753 Nephrin family 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

Miscellaneous databases

ChiTaRSiFyn mouse
PROiPR:P39688
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019843 Expressed in 321 organ(s), highest expression level in cranial nerve II
CleanExiMM_FYN
ExpressionAtlasiP39688 baseline and differential
GenevisibleiP39688 MM

Family and domain databases

CDDicd12006 SH3_Fyn_Yrk, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR035750 Fyn/Yrk_SH3
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiFYN_MOUSE
AccessioniPrimary (citable) accession number: P39688
Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2013
Last modified: November 7, 2018
This is version 197 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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