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F1RDG9 (FYNB_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 26. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase fynb

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

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Catalytic activity

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

Cofactor

Manganese By similarity.

Enzyme regulation

Inhibited by phosphorylation of Tyr-538 by leukocyte common antigen and activated by dephosphorylation of this site By similarity.

Subcellular location

Cytoplasm By similarity.

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
Chain2 – 544543Tyrosine-protein kinase fynb
PRO_0000418879

Regions

Domain89 – 15062SH3
Domain156 – 25398SH2
Domain278 – 531254Protein kinase
Nucleotide binding284 – 2929ATP By similarity

Sites

Active site3971Proton acceptor By similarity
Binding site3061ATP By similarity

Amino acid modifications

Modified residue4271Phosphotyrosine; by autocatalysis By similarity
Modified residue5381Phosphotyrosine By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation61S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict651S → P in AAH98534. Ref.2

Sequences

Sequence LengthMass (Da)Tools
F1RDG9 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 287C2FCF09C51B15

FASTA54461,030
        10         20         30         40         50         60 
MGCVQCKDKE AAKLTDDRDT SLSQSGVGYR YGVDPTPQHY PAFSGTGTAV AAIPNYNNFH 

        70         80         90        100        110        120 
GAAVSQGMTV FGGISTSTHQ GTLRTRGGTG VTLFVALYDY EARTEDDLSF RKGEKFQIIN 

       130        140        150        160        170        180 
STEGDWWDAR SLTTGGTGYI PSNYVAPVDS IQAEDWYFGK LGRKDAERQL LSTGNPRGTF 

       190        200        210        220        230        240 
LIRESETTKG AFSLSIRDWD DVKGDHVKHY KIRKLDSGGY YITTRAQFET LQQLVQHYTE 

       250        260        270        280        290        300 
RAAGLCCRLV VPCHKGMPRL TDLSVKTKDV WEIPRESLQL IKRLGNGQFG EVWMGTWNGN 

       310        320        330        340        350        360 
TKVAIKTLKP GTMSPESFLE EAQIMKKLRH DKLVQLYAVV SEEPIYIVTE YMGKGSLLDF 

       370        380        390        400        410        420 
LKDGEGRALK LPNLVDMAAQ VAGGMAYIER MNYIHRDLRS ANILVGDSLV CKIADFGLAR 

       430        440        450        460        470        480 
LIEDNEYTAR QGAKFPIKWT APEAALYGKF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR 

       490        500        510        520        530        540 
EVLEQVERGY RMQCPQDCPS SLHELMVQCW KKDAEERPTF EYLQAFLEDY FTATEPQYQP 


GDNL 

« Hide

References

[1]"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.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954744 Genomic DNA. No translation available.
FP015917 Genomic DNA. No translation available.
BC098534 mRNA. Translation: AAH98534.1.
RefSeqNP_001025140.1. NM_001029969.1.
XP_005160359.1. XM_005160302.1.
UniGeneDr.134137.

3D structure databases

ProteinModelPortalF1RDG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000037198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000036635; ENSDARP00000037198; ENSDARG00000025319.
GeneID574422.
KEGGdre:574422.

Organism-specific databases

CTD574422.
ZFINZDB-GENE-050706-89. fynb.

Phylogenomic databases

GeneTreeENSGT00620000087702.
KOK05703.
OMAQCWKKDA.
OrthoDBEOG7GTT2V.
TreeFamTF351634.

Gene expression databases

BgeeF1RDG9.

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

NextBio20891930.

Entry information

Entry nameFYNB_DANRE
AccessionPrimary (citable) accession number: F1RDG9
Secondary accession number(s): Q4KMJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 26 of the entry and version 1 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