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Q6EWH2 (FYNA_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase fyna

EC=2.7.10.2
Alternative name(s):
Proto-oncogene c-Fyna
Gene names
Name:fyna
Synonyms:fyn
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

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

Tyrosine-protein kinase 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. Role in cntn1-mediated signaling By similarity. Required for convergent extension cell movements during gastrulation, acting with yes via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling. Ref.1 Ref.2

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 By similarity. Relatively inactive in the unfertilized oocyte, undergoes rapid activation immediately following fertilization. Total activity increases progressively during later development and remains elevated during sphere and epiboly stage. Ref.5

Subcellular location

Cytoplasm. Nucleus. Note: Transiently expressed in the nucleus at mid-blastula stage (3.3 hpf) in a large subset of cells. Nuclear localization is not observed from late blastula stage onward. Ref.5

Tissue specificity

Widely expressed. Ref.2 Ref.5

Developmental stage

Expressed in the pre-gastrula embryo (at protein level).

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 caution

The sequence AAX47959.1 differs from that shown. Reason: Frameshift at positions 126 and 131.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6EWH2-1)

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: Q6EWH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     293-293: N → H
     294-537: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 537536Tyrosine-protein kinase fyna
PRO_0000418878

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 By similarity
Modified residue4201Phosphotyrosine; by autocatalysis By similarity
Modified residue5311Phosphotyrosine By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation61S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence2931N → H in isoform 2.
VSP_044087
Alternative sequence294 – 537244Missing in isoform 2.
VSP_044088

Experimental info

Mutagenesis2991K → M: Loss of activity. Ref.1
Sequence conflict51Q → R in AAH75763. Ref.4
Sequence conflict60 – 623GVT → RVP in CAF06179. Ref.2
Sequence conflict1481D → E in AAX47959. Ref.1

Sequences

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

Last modified September 5, 2012. Version 2.
Checksum: 1C7CB34990049B96

FASTA53760,569
        10         20         30         40         50         60 
MGCVQCKDKE ATKLTDERET SVSQHAGYRY GSDPTPQHYP SFGVTAIPNY NNFHAPVSQG 

        70         80         90        100        110        120 
VTVFGGVNSS SHSGTLRSRG GTGVTLFVAL YDYEARSEDD LSFRKGEKFQ ILNSTEGDWW 

       130        140        150        160        170        180 
EARSLTTGGT GYIPSNYVAP VDSIQAEDWY FGKLGRKDAE RQLLSNGNPR GTFLIRESET 

       190        200        210        220        230        240 
TKGAYSLSIQ DWDETKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVHH YSARAAGLCC 

       250        260        270        280        290        300 
RLIVPCHKGM PRLADLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAVKT 

       310        320        330        340        350        360 
LKPGTMSPES FLEEAQIMKK LRHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR 

       370        380        390        400        410        420 
GLKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGD SLVCKIADFG LARLIEDNEY 

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

       490        500        510        520        530 
RGYRMPCPQD CPSSLHELML QCWKRDPEER PTFEYLQAFL EDYFTATEPQ YQPGDNL 

« Hide

Isoform 2 [UniParc].

Checksum: CC69174A2FA24017
Show »

FASTA29332,799

References

« Hide 'large scale' references
[1]"Role of Fyn kinase in signaling associated with epiboly during zebrafish development."
Sharma D., Holets L., Zhang X., Kinsey W.H.
Dev. Biol. 285:462-476(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF LYS-299.
Tissue: Embryo.
[2]"Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate gastrulation cell movements."
Jopling C., den Hertog J.
EMBO Rep. 6:426-431(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[3]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[4]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryo.
[5]"Transient nuclear localization of Fyn kinase during development in zebrafish."
Rongish B.J., Kinsey W.H.
Anat. Rec. 260:115-123(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY948197 mRNA. Translation: AAX47959.1. Frameshift.
AJ620748 mRNA. Translation: CAF06179.1.
CU306817 Genomic DNA. No translation available.
BC075763 mRNA. Translation: AAH75763.1.
AF269145 mRNA. Translation: AAF81748.1.
RefSeqNP_001007287.1. NM_001007286.1.
XP_005169873.1. XM_005169816.1.
UniGeneDr.118811.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000003208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000046414; ENSDARP00000046413; ENSDARG00000011370. [Q6EWH2-2]
ENSDART00000150232; ENSDARP00000123888; ENSDARG00000011370. [Q6EWH2-1]
GeneID373872.
KEGGdre:373872.

Organism-specific databases

CTD373872.
ZFINZDB-GENE-030903-5. fyna.

Phylogenomic databases

GeneTreeENSGT00620000087702.
HOVERGENHBG008761.
InParanoidQ6EWH2.
KOK05703.
OMANNFHATG.
OrthoDBEOG7GTT2V.
TreeFamTF351634.

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

NextBio20813409.
PROQ6EWH2.

Entry information

Entry nameFYNA_DANRE
AccessionPrimary (citable) accession number: Q6EWH2
Secondary accession number(s): F8W4M2 expand/collapse secondary AC list , Q58HR4, Q6DI27, Q9I8J8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 5, 2012
Last modified: April 16, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families