Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q62844 (FYN_RAT)

Last modified February 9, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proto-oncogene tyrosine-protein kinase Fyn
    EC=2.7.10.2
Alternative name(s):
    Proto-oncogene c-Fyn
    p59-Fyn
Gene names
Name: Fyn
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

Implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Blocks axon outgrowth and attraction induced by NTN1 by phosphorylating its receptor DDC. Ref.3 UniProtKB P06241 UniProtKB P39688

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.3

Cofactor

Manganese. Ref.3

Enzyme regulation

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

Subunit structure

Associates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase. Interacts with the FYN-binding protein (FYB). Interacts with phosphorylated TOM1L1. Interacts with PAG1. Interacts with CD79A upon activation of the B-cell antigen receptor which increases FYN activity By similarity. Interacts with SH2D1A and SLAMF1. Interacts (via SH3 domain) with PRMT8 By similarity.

Subcellular location

Cell membrane. Note: Present and active in lipid rafts By similarity. Present in cell body and along the process of mature and developing oligodendroyctes. Ref.3 UniProtKB P39688

Developmental stage

Up-regulated during oligodendrocyte differentiation. Ref.3

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P06241
Chain2 – 537536Proto-oncogene tyrosine-protein kinase Fyn UniProtKB P06241
PRO_0000282948

Regions

Domain82 – 14362SH3
Domain149 – 24698SH2
Domain271 – 524254Protein kinase
Nucleotide binding277 – 2859ATP By similarity UniProtKB P28523

Sites

Active site3901Proton acceptor By similarity UniProtKB P28523
Binding site2991ATP Ref.3

Amino acid modifications

Modified residue151Phosphothreonine By similarity
Modified residue211Phosphoserine By similarity UniProtKB P06241
Modified residue251Phosphoserine By similarity
Modified residue1851Phosphotyrosine By similarity
Modified residue2131Phosphotyrosine By similarity
Modified residue2141Phosphotyrosine By similarity
Modified residue2541Phosphothreonine By similarity
Modified residue2571Phosphoserine By similarity
Modified residue4201Phosphotyrosine; by autocatalysis By similarity UniProtKB P06241
Modified residue4401Phosphotyrosine By similarity
Modified residue5121Phosphothreonine By similarity
Modified residue5311Phosphotyrosine By similarity UniProtKB P39688
Lipidation21N-myristoyl glycine By similarity UniProtKB P39688
Lipidation31S-palmitoyl cysteine By similarity UniProtKB P39688
Lipidation61S-palmitoyl cysteine By similarity UniProtKB P39688

Experimental info

Mutagenesis2991K → M: Loss of kinase activity and reduction in oligodendrocyte process extension and myelin membrane formation. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q62844-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 11AE4420919DBF1C

FASTA53760,702
        10         20         30         40         50         60 
MGCVQCKDKE AAKLTEERDG 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 PTFEYLQGFL EDYFTATEPQ YQPGENL 

« Hide

References

[1]"Expression of three type mRNAs encoding rat FYN by alternative splicing within 5' untranslated region."
Nemoto K., Sekimoto M., Kageyama H., Fukamachi K., Nemoto F., Ueyama T., Senba E., Tomita I.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SHRSP.
Tissue: Brain.
[2]"Novel putative protein kinase clones from a rat large granular lymphocyte tumor cell line."
Yue C.C.
Mol. Immunol. 28:399-408(1991) [PubMed: 2062320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Morphological differentiation of oligodendrocytes requires activation of Fyn tyrosine kinase."
Osterhout D.J., Wolven A., Wolf R.M., Resh M.D., Chao M.V.
J. Cell Biol. 145:1209-1218(1999) [PubMed: 10366594] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-299.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35365 mRNA. Translation: AAA82942.1.
IPIIPI00209210.
PIRPT0199.
RefSeqNP_036887.1.
UniGeneRn.19361

3D structure databases

HSSPHSSP built from PDB template 1FYN based on UniProtKB P06241.
SMRQ62844. Positions 81-142, 84-537.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ62844.

PTM databases

PhosphoSiteQ62844.

Genome annotation databases

EnsemblENSRNOT00000000733; ENSRNOP00000000733; ENSRNOG00000000596; Rattus norvegicus. [Genome view]
GeneID25150.
KEGGrno:25150.

Organism-specific databases

CTD25150.
RGD2641. Fyn.

Phylogenomic databases

eggNOGmaNOG10466.
HOVERGENQ62844.
InParanoidQ62844.
OMATTIPNYN.
OrthoDBEOG9PP12J.
PhylomeDBQ62844.

Enzyme and pathway databases

BRENDA2.7.10.2. 248.

Gene expression databases

ArrayExpressQ62844.
GenevestigatorQ62844.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
IPR020745. Tyr_kinase_non-rcpt_Fyn.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PANTHERPTHR23256:SF256. Tyr_kinase_non-rcpt_Fyn. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
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 Resources

NextBio605589.

Entry information

Entry nameFYN_RAT
AccessionPrimary (citable) accession number: Q62844
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents