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Q9TTY2

- FER_CANFA

UniProt

Q9TTY2 - FER_CANFA

Protein

Tyrosine-protein kinase Fer

Gene

FER

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell attachment and cell migration. Acts downstream of EGFR, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei591 – 5911ATPPROSITE-ProRule annotation
    Active sitei684 – 6841Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi569 – 5779ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. lipid binding Source: UniProtKB-KW
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: InterPro
    2. cell proliferation Source: InterPro
    3. positive regulation of cell migration Source: InterPro
    4. positive regulation of NF-kappaB transcription factor activity Source: InterPro
    5. regulation of epidermal growth factor receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fer (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fer
    p94-Fer
    Gene namesi
    Name:FER
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity. Cytoplasmcell cortex By similarity
    Note: Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts By similarity.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell junction Source: UniProtKB-SubCell
    3. cell projection Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 823823Tyrosine-protein kinase FerPRO_0000260824Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei402 – 4021PhosphotyrosineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei615 – 6151PhosphotyrosineBy similarity
    Modified residuei714 – 7141Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with CTNND1, EGFR, FLT3, IRS1, PECAM1, PIK3R1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000011047.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TTY2.
    SMRiQ9TTY2. Positions 449-820.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5858FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini460 – 55091SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini563 – 816254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili123 – 18563Sequence AnalysisAdd
    BLAST
    Coiled coili301 – 39090Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domains mediate homooligomerization and are required for location at microtubules.By similarity
    The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000059550.
    HOVERGENiHBG005655.
    InParanoidiQ9TTY2.
    KOiK08889.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR028539. Fer.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9TTY2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC    50
    NQVDKESTVQ MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 100
    TMMIKDKQQV KKSFIGVHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA 150
    KEKYKEALAK GKETEKAKER YDKATMKLHV LHNQYVLALK GAQLHQNQYY 200
    DTTLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI VNVHKEIQMS 250
    VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 300
    TAESLQVMLK TLAEELIQTQ QMLVNKEEAV LELEKRIEES SKTCEKKSDI 350
    VLLLSQKQTL EELKQSVQQL RCTEAKFTAQ KELLEQKVQE NEGKEPPPVV 400
    NYEEDARSVT SMERKERLSK FESIRHSIAG IIRSPKSALG SSTFSDTIPI 450
    SEKPLAEQDW YHGAIPRIEA QDLLKQQGDF LVRESHGKPG EYVLSVYSDG 500
    QRRHFIIQFV DNLYRFEGTG FSNIPQLIDH HYTTKQVITK KSGVVLLNPI 550
    PKDKKWVLNH EDVTLGELLG KGNFGEVYKG ILKDKTAVAV KTCKEDLPQE 600
    LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPIYIIMELV PGGDFLSFLR 650
    KKKDEIKLKQ LVKFSLDAAS GMSYLESKNC IHRDLAARNC LVGENNVLKI 700
    SDFGMSRQED GGVYSSSGLK QIPIKWTAPE ALNYGRYSSE SDVWSFGILL 750
    WETFSLGVCP YPGMTNQQAT EQVERGYRIS APQHCPEDIF KIMMKCWDYK 800
    PENRPKFSEL QKELTVIKKK VTQ 823
    Length:823
    Mass (Da):94,611
    Last modified:May 1, 2000 - v1
    Checksum:i33E88A6A15B37897
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187884 mRNA. Translation: AAF00543.1.
    RefSeqiNP_001003141.1. NM_001003141.1.
    UniGeneiCfa.3618.

    Genome annotation databases

    GeneIDi403754.
    KEGGicfa:403754.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187884 mRNA. Translation: AAF00543.1 .
    RefSeqi NP_001003141.1. NM_001003141.1.
    UniGenei Cfa.3618.

    3D structure databases

    ProteinModelPortali Q9TTY2.
    SMRi Q9TTY2. Positions 449-820.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000011047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403754.
    KEGGi cfa:403754.

    Organism-specific databases

    CTDi 2241.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000059550.
    HOVERGENi HBG005655.
    InParanoidi Q9TTY2.
    KOi K08889.

    Miscellaneous databases

    NextBioi 20817256.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR028539. Fer.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    PANTHERi PTHR24418:SF227. PTHR24418:SF227. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Links between Fer tyrosine kinase expression levels and prostate cell proliferation."
      Allard P., Zoubeidi A., Nguyen L.T., Tessier S., Tanguay S., Chevrette M., Aprikian A., Chevalier S.
      Mol. Cell. Endocrinol. 159:63-77(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Prostate.

    Entry informationi

    Entry nameiFER_CANFA
    AccessioniPrimary (citable) accession number: Q9TTY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 95 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