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F1RDG9

- FYNB_DANRE

UniProt

F1RDG9 - FYNB_DANRE

Protein

Tyrosine-protein kinase fynb

Gene

fynb

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei306 – 3061ATPPROSITE-ProRule annotation
    Active sitei397 – 3971Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi284 – 2929ATPPROSITE-ProRule annotation

    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

    GO - Biological processi

    1. convergent extension involved in gastrulation Source: ZFIN
    2. fin regeneration Source: ZFIN
    3. regulation of protein kinase activity Source: ZFIN

    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 fynb (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fynb
    Gene namesi
    Name:fynb
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Chromosome 20

    Organism-specific databases

    ZFINiZDB-GENE-050706-89. fynb.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 544543Tyrosine-protein kinase fynbPRO_0000418879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Lipidationi6 – 61S-palmitoyl cysteineBy similarity
    Modified residuei427 – 4271Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei538 – 5381PhosphotyrosineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Expressioni

    Gene expression databases

    BgeeiF1RDG9.

    Interactioni

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000037198.

    Structurei

    3D structure databases

    ProteinModelPortaliF1RDG9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini89 – 15062SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 25398SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini278 – 531254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    GeneTreeiENSGT00620000087702.
    KOiK05703.
    OMAiQCWKKDA.
    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    F1RDG9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCVQCKDKE AAKLTDDRDT SLSQSGVGYR YGVDPTPQHY PAFSGTGTAV    50
    AAIPNYNNFH GAAVSQGMTV FGGISTSTHQ GTLRTRGGTG VTLFVALYDY 100
    EARTEDDLSF RKGEKFQIIN STEGDWWDAR SLTTGGTGYI PSNYVAPVDS 150
    IQAEDWYFGK LGRKDAERQL LSTGNPRGTF LIRESETTKG AFSLSIRDWD 200
    DVKGDHVKHY KIRKLDSGGY YITTRAQFET LQQLVQHYTE RAAGLCCRLV 250
    VPCHKGMPRL TDLSVKTKDV WEIPRESLQL IKRLGNGQFG EVWMGTWNGN 300
    TKVAIKTLKP GTMSPESFLE EAQIMKKLRH DKLVQLYAVV SEEPIYIVTE 350
    YMGKGSLLDF LKDGEGRALK LPNLVDMAAQ VAGGMAYIER MNYIHRDLRS 400
    ANILVGDSLV CKIADFGLAR LIEDNEYTAR QGAKFPIKWT APEAALYGKF 450
    TIKSDVWSFG ILLTELVTKG RVPYPGMNNR EVLEQVERGY RMQCPQDCPS 500
    SLHELMVQCW KKDAEERPTF EYLQAFLEDY FTATEPQYQP GDNL 544
    Length:544
    Mass (Da):61,030
    Last modified:May 3, 2011 - v1
    Checksum:i287C2FCF09C51B15
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651S → P in AAH98534. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL954744 Genomic DNA. No translation available.
    FP015917 Genomic DNA. No translation available.
    BC098534 mRNA. Translation: AAH98534.1.
    RefSeqiNP_001025140.1. NM_001029969.1.
    XP_005160359.1. XM_005160302.1.
    UniGeneiDr.134137.

    Genome annotation databases

    EnsembliENSDART00000036635; ENSDARP00000037198; ENSDARG00000025319.
    GeneIDi574422.
    KEGGidre:574422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL954744 Genomic DNA. No translation available.
    FP015917 Genomic DNA. No translation available.
    BC098534 mRNA. Translation: AAH98534.1 .
    RefSeqi NP_001025140.1. NM_001029969.1.
    XP_005160359.1. XM_005160302.1.
    UniGenei Dr.134137.

    3D structure databases

    ProteinModelPortali F1RDG9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000037198.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000036635 ; ENSDARP00000037198 ; ENSDARG00000025319 .
    GeneIDi 574422.
    KEGGi dre:574422.

    Organism-specific databases

    CTDi 574422.
    ZFINi ZDB-GENE-050706-89. fynb.

    Phylogenomic databases

    GeneTreei ENSGT00620000087702.
    KOi K05703.
    OMAi QCWKKDA.
    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 20891930.

    Gene expression databases

    Bgeei F1RDG9.

    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

    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.
      , 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.

    Entry informationi

    Entry nameiFYNB_DANRE
    AccessioniPrimary (citable) accession number: F1RDG9
    Secondary accession number(s): Q4KMJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 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