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P13406

- FYN_XENLA

UniProt

P13406 - FYN_XENLA

Protein

Tyrosine-protein kinase Fyn

Gene

fyn

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 By similarity. 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.By similarity1 Publication

    Catalytic activityi

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

    Cofactori

    Manganese.

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei299 – 2991ATPPROSITE-ProRule annotation
    Active sitei390 – 3901Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi277 – 2859ATPPROSITE-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. multicellular organismal development Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 6726.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fyn (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fyn
    p59-Fyn
    Gene namesi
    Name:fyn
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6252893. fyn.

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 537536Tyrosine-protein kinase FynPRO_0000088101Add
    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 residuei12 – 121Phosphothreonine; by PKCBy similarity
    Modified residuei420 – 4201Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei531 – 5311PhosphotyrosineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Expressioni

    Developmental stagei

    Expressed in early tail-bud embryos at stage 20 in the brain region of the neural tube and at lower levels throughout the remaining length of the neural tube. Present at stage 32 in the forebrain, midbrain, the ventral half of the hindbrain and the spinal cord.1 Publication

    Interactioni

    Subunit structurei

    Associates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase.

    Structurei

    3D structure databases

    ProteinModelPortaliP13406.
    SMRiP13406. Positions 84-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 14362SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 24698SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 524254Protein 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

    HOVERGENiHBG008761.
    KOiK05703.

    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.

    P13406-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCVQCKDKE ATKLTDERDN SLTQSLGYRY GTDPTPQHYP SFTVTTIPNY    50
    NNFHATAGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD 100
    LSFQKGEKFQ ILNSSEGDWW EARSLTTGGT GYIPSNYVAP VDSIQAEEWY 150
    FGKLGRKDAE RQLLSFGNPR GTYLIRESET TKGAYSLSIR DWDDMKGDHV 200
    KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM 250
    PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 300
    LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL 350
    LDFLKDGEGR ALKLPNLVDM AAQVARGMAY IERMNYIHRD LRSANILVGN 400
    GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 450
    SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELML 500
    NCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGDNL 537
    Length:537
    Mass (Da):60,846
    Last modified:January 23, 2007 - v3
    Checksum:i771E5799682A1326
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021S → N in AAH43749. 1 PublicationCurated
    Sequence conflicti223 – 2231T → A in AAH43749. 1 PublicationCurated
    Sequence conflicti376 – 3761R → A in AAH43749. 1 PublicationCurated
    Sequence conflicti493 – 4931I → N in AAH43749. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52188 Genomic DNA. Translation: CAA36435.1.
    M27502 mRNA. Translation: AAA49719.1.
    BC043749 mRNA. Translation: AAH43749.1.
    PIRiA43806.
    RefSeqiNP_001079077.1. NM_001085608.1.
    NP_001080120.1. NM_001086651.1.
    UniGeneiXl.21919.
    Xl.501.

    Genome annotation databases

    GeneIDi373609.
    379812.
    KEGGixla:373609.
    xla:379812.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52188 Genomic DNA. Translation: CAA36435.1 .
    M27502 mRNA. Translation: AAA49719.1 .
    BC043749 mRNA. Translation: AAH43749.1 .
    PIRi A43806.
    RefSeqi NP_001079077.1. NM_001085608.1.
    NP_001080120.1. NM_001086651.1.
    UniGenei Xl.21919.
    Xl.501.

    3D structure databases

    ProteinModelPortali P13406.
    SMRi P13406. Positions 84-537.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 373609.
    379812.
    KEGGi xla:373609.
    xla:379812.

    Organism-specific databases

    CTDi 2534.
    Xenbasei XB-GENE-6252893. fyn.

    Phylogenomic databases

    HOVERGENi HBG008761.
    KOi K05703.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 6726.

    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. "Structure and expression of fyn genes in Xenopus laevis."
      Steele R.E., Deng J.C., Ghosn C.R., Fero J.B.
      Oncogene 5:369-376(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    3. "Overexpression of Fyn tyrosine kinase causes abnormal development of primary sensory neurons in Xenopus laevis embryos."
      Saito R., Fujita N., Nagata S.
      Dev. Growth Differ. 43:229-238(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    4. "Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone guidance."
      Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I., McFarlane S., Bloch-Gallego E., Lamarche-Vane N.
      J. Cell Biol. 167:687-698(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiFYN_XENLA
    AccessioniPrimary (citable) accession number: P13406
    Secondary accession number(s): Q7ZYK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3