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P70451

- FER_MOUSE

UniProt

P70451 - FER_MOUSE

Protein

Tyrosine-protein kinase Fer

Gene

Fer

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      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 adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. 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. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3 according to PubMed:10878010 and PubMed:19159681, but clearly plays a redundant role in STAT3 phosphorylation. According to PubMed:11134346, cells where wild type FER has been replaced by a kinase-dead mutant show no reduction in STAT3 phosphorylation. Phosphorylates TMF1. Isoform 3 lacks kinase activity.12 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    Activated by phosphatidic acid binding By similarity. Activated by hydrogen peroxide (in vitro). Activated by reactive oxygen species (ROS).By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei592 – 5921ATPPROSITE-ProRule annotation
    Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi570 – 5789ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. epidermal growth factor receptor binding Source: UniProtKB
    3. lipid binding Source: UniProtKB
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    5. protein binding Source: MGI
    6. protein kinase activity Source: MGI
    7. protein phosphatase 1 binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. cell adhesion Source: MGI
    3. cell-cell adhesion mediated by cadherin Source: UniProtKB
    4. cell proliferation Source: Ensembl
    5. cellular response to insulin stimulus Source: UniProtKB
    6. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
    7. cellular response to reactive oxygen species Source: UniProtKB
    8. chemotaxis Source: MGI
    9. cytokine-mediated signaling pathway Source: UniProtKB
    10. diapedesis Source: UniProtKB
    11. extracellular matrix-cell signaling Source: UniProtKB
    12. Fc-epsilon receptor signaling pathway Source: UniProtKB
    13. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
    14. interleukin-6-mediated signaling pathway Source: Ensembl
    15. Kit signaling pathway Source: UniProtKB
    16. microtubule cytoskeleton organization Source: UniProtKB
    17. mitotic cell cycle Source: Ensembl
    18. negative regulation of mast cell activation involved in immune response Source: UniProtKB
    19. peptidyl-tyrosine phosphorylation Source: UniProtKB
    20. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    21. positive regulation of actin filament polymerization Source: UniProtKB
    22. positive regulation of cell migration Source: UniProtKB
    23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    24. protein autophosphorylation Source: MGI
    25. protein phosphorylation Source: MGI
    26. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    27. regulation of fibroblast migration Source: UniProtKB
    28. regulation of lamellipodium assembly Source: UniProtKB
    29. regulation of protein phosphorylation Source: UniProtKB
    30. response to lipopolysaccharide Source: UniProtKB
    31. response to platelet-derived growth factor Source: UniProtKB
    32. signal transduction Source: MGI
    33. substrate adhesion-dependent cell spreading Source: UniProtKB
    34. tyrosine phosphorylation of Stat3 protein Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188578. Signaling by SCF-KIT.

    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
    Synonyms:Fert2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:105917. Fer.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. 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. Cytoplasmcell cortex By similarity
    Note: 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. Not detected in the nucleus, but detected in the nuclear area surrounding the chromosomes after breakdown of the nuclear envelope during mitosis (PubMed:11339827).By similarity1 Publication

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cell cortex Source: UniProtKB-SubCell
    3. cell junction Source: UniProtKB-SubCell
    4. cytoplasm Source: UniProtKB
    5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    6. lamellipodium Source: Ensembl
    7. microtubule cytoskeleton Source: Ensembl
    8. nuclear chromatin Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype, and the mice are fertile. Mice have reduced CTTN phosphorylation. Mice lacking both Fps/Fes and Fer activity are viable and fertile, but produce slightly fewer pups per litter than normal. They display elevated levels of circulating neutrophils, erythrocytes and platelets, while other cell counts are normal.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1362KL → RP: Abolishes homooligomerization.
    Mutagenesisi322 – 3232ML → RP: Abolishes homooligomerization.
    Mutagenesisi571 – 5711G → R: Abolishes kinase activity. 1 Publication
    Mutagenesisi592 – 5921K → R: Abolishes kinase activity. 1 Publication
    Mutagenesisi606 – 6061F → A: Abolishes interaction with PPP1CA. 1 Publication
    Mutagenesisi616 – 6161Y → F: Abolishes autophosphorylation. 1 Publication
    Mutagenesisi715 – 7151Y → F: Abolishes autophosphorylation. 1 Publication
    Mutagenesisi743 – 7431D → R: Abolishes kinase activity. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 823823Tyrosine-protein kinase FerPRO_0000260825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei402 – 4021Phosphotyrosine2 Publications
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei616 – 6161Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated.6 Publications
    Polyubiquitinated; this leads to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP70451.
    PaxDbiP70451.
    PRIDEiP70451.

    PTM databases

    PhosphoSiteiP70451.

    Expressioni

    Tissue specificityi

    Detected in liver and testis. Isoform 4 is detected only in testis (at protein level). Widely expressed.3 Publications

    Inductioni

    Up-regulated by insulin in myogenic cells (in vitro).1 Publication

    Gene expression databases

    ArrayExpressiP70451.
    BgeeiP70451.
    GenevestigatoriP70451.

    Interactioni

    Subunit structurei

    Homotrimer. Isoform 4 is a monomer, due to the absence of the N-terminal coiled coil domains. Interacts with CTNND1, EGFR, FLT3, PECAM1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity. Interacts with IRS1 and PIK3R1. Interacts with STAT3. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with JAK1. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Interacts with ARHGDIA, NRP1, PLEC and TMF1.By similarity10 Publications

    Protein-protein interaction databases

    BioGridi199633. 3 interactions.
    STRINGi10090.ENSMUSP00000000129.

    Structurei

    3D structure databases

    ProteinModelPortaliP70451.
    SMRiP70451. Positions 1-400, 453-820.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5858FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 55191SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 817254Protein 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 – 38181Sequence 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.
    GeneTreeiENSGT00750000117264.
    HOGENOMiHOG000233858.
    HOVERGENiHBG005655.
    InParanoidiQ9EQ77.
    KOiK08889.
    OMAiFVDNLYR.
    OrthoDBiEOG708VXW.
    PhylomeDBiP70451.
    TreeFamiTF315363.

    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]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70451-1) [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

    MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC    50
    NQVDKESTVQ VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 100
    TMMIKDKQQV KKSYVGIHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA 150
    KEKYKEALAK GKETEKAKER YDKATMKLHM LHNQYVLALK GAQLHQSQYY 200
    DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI VNVHKEIQMS 250
    VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 300
    TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI 350
    VLLLGQKQAL EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV 400
    NYEEDARSVT SMERKERLSK FESIRHSIAG IIKSPKSVLG SSTQVCDVIS 450
    VGERPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP GEYVLSVYSD 500
    GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP 550
    IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ 600
    ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL 650
    RKRKDELKLK QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK 700
    ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP EALNYGRYSS ESDVWSFGIL 750
    LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEV FTIMMKCWDY 800
    KPENRPKFND LHKELTVIKK MIT 823
    Length:823
    Mass (Da):94,579
    Last modified:November 28, 2006 - v2
    Checksum:iF4C22E1E63721663
    GO
    Isoform 2 (identifier: P70451-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-127: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:765
    Mass (Da):87,762
    Checksum:i91FCCCAAFEF1C283
    GO
    Isoform 3 (identifier: P70451-3) [UniParc]FASTAAdd to Basket

    Also known as: iFer

    The sequence of this isoform differs from the canonical sequence as follows:
         491-542: GEYVLSVYSD...FNTKQVITKK → ESVSIRGHRV...GGSAQPHPKG
         543-823: Missing.

    Show »
    Length:532
    Mass (Da):61,094
    Checksum:i7468E01E9EB6F6E2
    GO
    Isoform 4 (identifier: P70451-4) [UniParc]FASTAAdd to Basket

    Also known as: FerT, p51FerT

    The sequence of this isoform differs from the canonical sequence as follows:
         1-369: Missing.
         370-412: LRCTEAKCAA...EEDARSVTSM → MDKSMECPHC...PSSSEILRYK
         444-444: Missing.

    Show »
    Length:453
    Mass (Da):51,601
    Checksum:i1CDAA93ED40B6A1D
    GO
    Isoform 5 (identifier: P70451-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         444-444: Missing.

    Show »
    Length:822
    Mass (Da):94,451
    Checksum:iF08F6BB10161D738
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti328 – 3281A → G in BAC38626. (PubMed:16141072)Curated
    Sequence conflicti373 – 3731T → S in AAB18988. 1 PublicationCurated
    Sequence conflicti373 – 3731T → S in AAG40730. (PubMed:11006284)Curated
    Sequence conflicti730 – 7301P → A in AAA37617. (PubMed:2294399)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 369369Missing in isoform 4. 1 PublicationVSP_041766Add
    BLAST
    Alternative sequencei70 – 12758Missing in isoform 2. 1 PublicationVSP_021634Add
    BLAST
    Alternative sequencei370 – 41243LRCTE…SVTSM → MDKSMECPHCEGVLEPESDP QFSKKCSIPLSPGPSSSEIL RYK in isoform 4. 1 PublicationVSP_041767Add
    BLAST
    Alternative sequencei444 – 4441Missing in isoform 4 and isoform 5. 2 PublicationsVSP_041768
    Alternative sequencei491 – 54252GEYVL…VITKK → ESVSIRGHRVFKHSPAYRSP LQYKASHHQEVWGGSAQPHP KG in isoform 3. 1 PublicationVSP_041769Add
    BLAST
    Alternative sequencei543 – 823281Missing in isoform 3. 1 PublicationVSP_041770Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76762 mRNA. Translation: AAB18988.1.
    M32054 mRNA. Translation: AAA37617.1.
    AF286537 mRNA. Translation: AAG40730.1.
    BC051249 mRNA. Translation: AAH51249.1.
    BC058100 mRNA. Translation: AAH58100.1.
    AK082799 mRNA. Translation: BAC38626.1.
    CCDSiCCDS28936.1. [P70451-1]
    CCDS28937.1. [P70451-4]
    PIRiI49663.
    RefSeqiNP_001033086.2. NM_001037997.3. [P70451-1]
    NP_001273344.1. NM_001286415.1. [P70451-2]
    NP_032026.2. NM_008000.2. [P70451-4]
    XP_006523703.1. XM_006523640.1. [P70451-1]
    XP_006523704.1. XM_006523641.1. [P70451-1]
    XP_006523705.1. XM_006523642.1. [P70451-5]
    XP_006523706.1. XM_006523643.1. [P70451-5]
    UniGeneiMm.151391.
    Mm.23039.

    Genome annotation databases

    EnsembliENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127. [P70451-1]
    ENSMUST00000038080; ENSMUSP00000037418; ENSMUSG00000000127. [P70451-4]
    GeneIDi14158.
    KEGGimmu:14158.
    UCSCiuc008dfo.2. mouse. [P70451-2]
    uc008dfp.1. mouse. [P70451-3]
    uc008dfq.2. mouse. [P70451-1]
    uc008dfr.2. mouse. [P70451-5]
    uc008dfs.2. mouse. [P70451-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76762 mRNA. Translation: AAB18988.1 .
    M32054 mRNA. Translation: AAA37617.1 .
    AF286537 mRNA. Translation: AAG40730.1 .
    BC051249 mRNA. Translation: AAH51249.1 .
    BC058100 mRNA. Translation: AAH58100.1 .
    AK082799 mRNA. Translation: BAC38626.1 .
    CCDSi CCDS28936.1. [P70451-1 ]
    CCDS28937.1. [P70451-4 ]
    PIRi I49663.
    RefSeqi NP_001033086.2. NM_001037997.3. [P70451-1 ]
    NP_001273344.1. NM_001286415.1. [P70451-2 ]
    NP_032026.2. NM_008000.2. [P70451-4 ]
    XP_006523703.1. XM_006523640.1. [P70451-1 ]
    XP_006523704.1. XM_006523641.1. [P70451-1 ]
    XP_006523705.1. XM_006523642.1. [P70451-5 ]
    XP_006523706.1. XM_006523643.1. [P70451-5 ]
    UniGenei Mm.151391.
    Mm.23039.

    3D structure databases

    ProteinModelPortali P70451.
    SMRi P70451. Positions 1-400, 453-820.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199633. 3 interactions.
    STRINGi 10090.ENSMUSP00000000129.

    PTM databases

    PhosphoSitei P70451.

    Proteomic databases

    MaxQBi P70451.
    PaxDbi P70451.
    PRIDEi P70451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000129 ; ENSMUSP00000000129 ; ENSMUSG00000000127 . [P70451-1 ]
    ENSMUST00000038080 ; ENSMUSP00000037418 ; ENSMUSG00000000127 . [P70451-4 ]
    GeneIDi 14158.
    KEGGi mmu:14158.
    UCSCi uc008dfo.2. mouse. [P70451-2 ]
    uc008dfp.1. mouse. [P70451-3 ]
    uc008dfq.2. mouse. [P70451-1 ]
    uc008dfr.2. mouse. [P70451-5 ]
    uc008dfs.2. mouse. [P70451-4 ]

    Organism-specific databases

    CTDi 14158.
    MGIi MGI:105917. Fer.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117264.
    HOGENOMi HOG000233858.
    HOVERGENi HBG005655.
    InParanoidi Q9EQ77.
    KOi K08889.
    OMAi FVDNLYR.
    OrthoDBi EOG708VXW.
    PhylomeDBi P70451.
    TreeFami TF315363.

    Enzyme and pathway databases

    Reactomei REACT_188578. Signaling by SCF-KIT.

    Miscellaneous databases

    NextBioi 285280.
    PROi P70451.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70451.
    Bgeei P70451.
    Genevestigatori P70451.

    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. "Murine Fer."
      Letwin K., Pawson T.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A murine fer testis-specific transcript (ferT) encodes a truncated Fer protein."
      Fischman K., Edman J.C., Shackleford G.M., Turner J.A., Rutter W.J., Nir U.
      Mol. Cell. Biol. 10:146-153(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    3. "The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase."
      Iwanishi M., Czech M.P., Cherniack A.D.
      J. Biol. Chem. 275:38995-39000(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH IRS1 AND PIK3R1, SUBUNIT.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6 and FVB/N-3.
      Tissue: Brain and Mammary tumor.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-823 (ISOFORM 5).
      Strain: C57BL/6J.
    6. "The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors."
      Kim L., Wong T.W.
      Mol. Cell. Biol. 15:4553-4561(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1, AUTOPHOSPHORYLATION, INTERACTION WITH CTNND1 AND PDGFR.
    7. "Tyrosine phosphorylation of the TATA element modulatory factor by the FER nuclear tyrosine kinases."
      Schwartz Y., Ben-Dor I., Navon A., Motro B., Nir U.
      FEBS Lett. 434:339-345(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TMF1, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-571, CHARACTERIZATION OF ISOFORM 4.
    8. "Cell cycle-dependent nuclear accumulation of the p94fer tyrosine kinase is regulated by its NH2 terminus and is affected by kinase domain integrity and ATP binding."
      Ben-Dor I., Bern O., Tennenbaum T., Nir U.
      Cell Growth Differ. 10:113-129(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-715, MUTAGENESIS OF TYR-715.
    9. "Disruption of coiled-coil domains in Fer protein-tyrosine kinase abolishes trimerization but not kinase activation."
      Craig A.W., Zirngibl R., Greer P.
      J. Biol. Chem. 274:19934-19942(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF 135-LYS-LEU-136; 322-MET-LEU-323; LYS-592 AND ASP-743, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    10. Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION.
    11. "Subcellular localization analysis of the closely related Fps/Fes and Fer protein-tyrosine kinases suggests a distinct role for Fps/Fes in vesicular trafficking."
      Zirngibl R., Schulze D., Mirski S.E., Cole S.P., Greer P.A.
      Exp. Cell Res. 266:87-94(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation."
      Craig A.W., Zirngibl R., Williams K., Cole L.A., Greer P.A.
      Mol. Cell. Biol. 21:603-613(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    13. "Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity."
      Lunter P.C., Wiche G.
      Biochem. Biophys. Res. Commun. 296:904-910(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLEC.
    14. "Absence of Fer protein-tyrosine kinase exacerbates leukocyte recruitment in response to endotoxin."
      McCafferty D.M., Craig A.W., Senis Y.A., Greer P.A.
      J. Immunol. 168:4930-4935(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RESPONSE TO LIPOPOLYSACCHARIDE AND LEUKOCYTE DIAPEDESIS.
    15. "Fps/Fes and Fer protein-tyrosine kinases play redundant roles in regulating hematopoiesis."
      Senis Y.A., Craig A.W., Greer P.A.
      Exp. Hematol. 31:673-681(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    16. "Fer is a downstream effector of insulin and mediates the activation of signal transducer and activator of transcription 3 in myogenic cells."
      Taler M., Shpungin S., Salem Y., Malovani H., Pasder O., Nir U.
      Mol. Endocrinol. 17:1580-1592(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY INSULIN, INTERACTION WITH STAT3 AND JAK1.
    17. "Continuous association of cadherin with beta-catenin requires the non-receptor tyrosine-kinase Fer."
      Xu G., Craig A.W., Greer P., Miller M., Anastasiadis P.Z., Lilien J., Balsamo J.
      J. Cell Sci. 117:3207-3219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PTPN1.
    18. "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
      Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
      Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMF1.
    19. "Phosphorylation of N-cadherin-associated cortactin by Fer kinase regulates N-cadherin mobility and intercellular adhesion strength."
      El Sayegh T.Y., Arora P.D., Fan L., Laschinger C.A., Greer P.A., McCulloch C.A., Kapus A.
      Mol. Biol. Cell 16:5514-5527(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    20. "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
      Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
      J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAST CELL ACTIVATION, FUNCTION IN PHOSPHORYLATION OF PECAM1, PHOSPHORYLATION, ENZYME REGULATION.
    21. "Downregulation of Fer induces PP1 activation and cell-cycle arrest in malignant cells."
      Pasder O., Shpungin S., Salem Y., Makovsky A., Vilchick S., Michaeli S., Malovani H., Nir U.
      Oncogene 25:4194-4206(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PHE-606, INTERACTION WITH PPP1CA.
    22. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    23. "Fer-mediated cortactin phosphorylation is associated with efficient fibroblast migration and is dependent on reactive oxygen species generation during integrin-mediated cell adhesion."
      Sangrar W., Gao Y., Scott M., Truesdell P., Greer P.A.
      Mol. Cell. Biol. 27:6140-6152(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    24. "Hsp90 and a tyrosine embedded in the Hsp90 recognition loop are required for the Fer tyrosine kinase activity."
      Hikri E., Shpungin S., Nir U.
      Cell. Signal. 21:588-596(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STAT3 PHOSPHORYLATION, INTERACTION WITH HSP90, PHOSPHORYLATION AT TYR-616, MUTAGENESIS OF TYR-616, UBIQUITINATION, PROTEASOMAL DEGRADATION.
    25. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    26. "Neuropilin 1 directly interacts with Fer kinase to mediate semaphorin 3A-induced death of cortical neurons."
      Jiang S.X., Whitehead S., Aylsworth A., Slinn J., Zurakowski B., Chan K., Li J., Hou S.T.
      J. Biol. Chem. 285:9908-9918(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEURONAL CELL DEATH AFTER BRAIN DAMAGE, INTERACTION WITH NRP1.

    Entry informationi

    Entry nameiFER_MOUSE
    AccessioniPrimary (citable) accession number: P70451
    Secondary accession number(s): Q61561
    , Q6PEE5, Q80UI3, Q8C481, Q9EQ77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 122 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3