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Q6EWH2

- FYNA_DANRE

UniProt

Q6EWH2 - FYNA_DANRE

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Protein
Tyrosine-protein kinase fyna
Gene
fyna, fyn
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Manganese.

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei299 – 2991ATP By similarity
Active sitei390 – 3901Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi277 – 2859ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein kinase activity Source: ZFIN

GO - Biological processi

  1. convergent extension involved in gastrulation Source: ZFIN
  2. cytosolic calcium ion homeostasis Source: ZFIN
  3. gastrulation with mouth forming second Source: ZFIN
  4. protein autophosphorylation Source: ZFIN
  5. regulation of protein kinase activity Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_174907. Regulation of KIT signaling.
REACT_175016. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_181648. Signaling by SCF-KIT.
REACT_182699. DAP12 signaling.
REACT_182784. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_210358. Regulation of signaling by CBL.
REACT_214033. Netrin mediated repulsion signals.
REACT_221534. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase fyna (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fyna
Gene namesi
Name:fyna
Synonyms:fyn
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437: Chromosome 17

Organism-specific databases

ZFINiZDB-GENE-030903-5. fyna.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. cytosol Source: ZFIN
  2. nucleus Source: ZFIN
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi299 – 2991K → M: Loss of activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 537536Tyrosine-protein kinase fyna
PRO_0000418878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Lipidationi3 – 31S-palmitoyl cysteine By similarity
Lipidationi6 – 61S-palmitoyl cysteine By similarity
Modified residuei12 – 121Phosphothreonine; by PKC By similarity
Modified residuei420 – 4201Phosphotyrosine; by autocatalysis By similarity
Modified residuei531 – 5311Phosphotyrosine By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Developmental stagei

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

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000003208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 14362SH3
Add
BLAST
Domaini149 – 24698SH2
Add
BLAST
Domaini271 – 524254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

GeneTreeiENSGT00620000087702.
HOVERGENiHBG008761.
InParanoidiQ6EWH2.
KOiK05703.
OMAiSHNSGYR.
OrthoDBiEOG7GTT2V.
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: Q6EWH2-1) [UniParc]FASTAAdd to Basket

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

MGCVQCKDKE ATKLTDERET SVSQHAGYRY GSDPTPQHYP SFGVTAIPNY    50
NNFHAPVSQG VTVFGGVNSS SHSGTLRSRG GTGVTLFVAL YDYEARSEDD 100
LSFRKGEKFQ ILNSTEGDWW EARSLTTGGT GYIPSNYVAP VDSIQAEDWY 150
FGKLGRKDAE RQLLSNGNPR GTFLIRESET TKGAYSLSIQ DWDETKGDHV 200
KHYKIRKLDN GGYYITTRAQ FETLQQLVHH YSARAAGLCC RLIVPCHKGM 250
PRLADLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAVKT 300
LKPGTMSPES FLEEAQIMKK LRHDKLVQLY AVVSEEPIYI VTEYMSKGSL 350
LDFLKDGEGR GLKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGD 400
SLVCKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 450
SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPSSLHELML 500
QCWKRDPEER PTFEYLQAFL EDYFTATEPQ YQPGDNL 537
Length:537
Mass (Da):60,569
Last modified:September 5, 2012 - v2
Checksum:i1C7CB34990049B96
GO
Isoform 2 (identifier: Q6EWH2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-293: N → H
     294-537: Missing.

Note: No experimental confirmation available.

Show »
Length:293
Mass (Da):32,799
Checksum:iCC69174A2FA24017
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei293 – 2931N → H in isoform 2.
VSP_044087
Alternative sequencei294 – 537244Missing in isoform 2.
VSP_044088Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Q → R in AAH75763. 1 Publication
Sequence conflicti60 – 623GVT → RVP in CAF06179. 1 Publication
Sequence conflicti148 – 1481D → E in AAX47959. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001007287.1. NM_001007286.1.
XP_005169873.1. XM_005169816.1. [Q6EWH2-1]
UniGeneiDr.118811.

Genome annotation databases

EnsembliENSDART00000046414; ENSDARP00000046413; ENSDARG00000011370. [Q6EWH2-2]
ENSDART00000150232; ENSDARP00000123888; ENSDARG00000011370. [Q6EWH2-1]
GeneIDi373872.
KEGGidre:373872.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001007287.1. NM_001007286.1.
XP_005169873.1. XM_005169816.1. [Q6EWH2-1 ]
UniGenei Dr.118811.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7955.ENSDARP00000003208.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSDART00000046414 ; ENSDARP00000046413 ; ENSDARG00000011370 . [Q6EWH2-2 ]
ENSDART00000150232 ; ENSDARP00000123888 ; ENSDARG00000011370 . [Q6EWH2-1 ]
GeneIDi 373872.
KEGGi dre:373872.

Organism-specific databases

CTDi 373872.
ZFINi ZDB-GENE-030903-5. fyna.

Phylogenomic databases

GeneTreei ENSGT00620000087702.
HOVERGENi HBG008761.
InParanoidi Q6EWH2.
KOi K05703.
OMAi SHNSGYR.
OrthoDBi EOG7GTT2V.
TreeFami TF351634.

Enzyme and pathway databases

Reactomei REACT_174907. Regulation of KIT signaling.
REACT_175016. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_181648. Signaling by SCF-KIT.
REACT_182699. DAP12 signaling.
REACT_182784. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_210358. Regulation of signaling by CBL.
REACT_214033. Netrin mediated repulsion signals.
REACT_221534. FCGR activation.

Miscellaneous databases

NextBioi 20813409.
PROi Q6EWH2.

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. "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.
    , 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.

Entry informationi

Entry nameiFYNA_DANRE
AccessioniPrimary (citable) accession number: Q6EWH2
Secondary accession number(s): F8W4M2
, Q58HR4, Q6DI27, Q9I8J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: September 5, 2012
Last modified: September 3, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi