Tyrosine-protein kinase Fer

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• ATP

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  + L-tyrosyl-[protein]

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  = ADP

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  + H⁺

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  + O-phospho-L-tyrosyl-[protein]

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  PROSITE-ProRule annotation

  <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesⁱ

  • PROSITE-ProRule:PRU10028

  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.11

    "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
  EC:2.7.10.2
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  • See the description of this EC number in ENZYME.
  PROSITE-ProRule annotation

  Manual assertion according to rulesⁱ

  • PROSITE-ProRule:PRU10028
  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.11

    "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  ATP

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  +

  L-tyrosyl-[protein]

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  L-tyrosine residue

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  =

  ADP

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  +

  H⁺

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  +

  O-phospho-L-tyrosyl-[protein]

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  L-tyrosine-phosphate residue

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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATP binding Source: UniProtKB-KW
• epidermal growth factor receptor binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.22

    "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
    Guo C., Stark G.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL PROLIFERATION, INTERACTION WITH EGFR, PHOSPHORYLATION.
• lipid binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• non-membrane spanning protein tyrosine kinase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• protein phosphatase 1 binding Source: Ensembl
• protein tyrosine kinase activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "Isolation and sequence analysis of a novel human tyrosine kinase gene."
    Hao Q.-L., Heisterkamp N., Groffen J.
    Mol. Cell. Biol. 9:1587-1593(1989) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-439.
• signaling receptor binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• actin cytoskeleton reorganization Source: UniProtKB
• cell adhesion Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cell-cell adhesion mediated by cadherin Source: UniProtKB
• cell differentiation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cell migration Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cell population proliferation Source: InterPro
• cellular response to insulin stimulus Source: UniProtKB
• cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.10

    "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER."
    Kim L., Wong T.W.
    J. Biol. Chem. 273:23542-23548(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, INTERACTION WITH CTTN; CTNND1 AND PDGFR, MUTAGENESIS OF LYS-591, SUBCELLULAR LOCATION.
• cellular response to reactive oxygen species Source: UniProtKB
• chemotaxis Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cytokine-mediated signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.10

    "Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER."
    Kim L., Wong T.W.
    J. Biol. Chem. 273:23542-23548(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF CTTN, INTERACTION WITH CTTN; CTNND1 AND PDGFR, MUTAGENESIS OF LYS-591, SUBCELLULAR LOCATION.
• diapedesis Source: UniProtKB
• extracellular matrix-cell signaling Source: UniProtKB
• Fc-epsilon receptor signaling pathway Source: UniProtKB
• insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
• interleukin-6-mediated signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.18

    "The Fer tyrosine kinase cooperates with interleukin-6 to activate signal transducer and activator of transcription 3 and promote human prostate cancer cell growth."
    Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E., Aprikian A.G., Chevalier S.
    Mol. Cancer Res. 7:142-155(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN IL6 SIGNALING PATHWAY; CELL PROLIFERATION AND IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3.
• intracellular signal transduction Source: ProtIncTraceable author statementⁱ
  • "The human tyrosine kinase gene (FER) maps to chromosome 5 and is deleted in myeloid leukemias with a del(5q)."
    Morris C., Heisterkamp N., Hao Q.L., Testa J.R., Groffen J.
    Cytogenet. Cell Genet. 53:196-200(1990) [PubMed] [Europe PMC] [Abstract]
• Kit signaling pathway Source: UniProtKB
• microtubule cytoskeleton organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
• negative regulation of mast cell activation involved in immune response Source: UniProtKB
• peptidyl-tyrosine autophosphorylation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• peptidyl-tyrosine phosphorylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
    Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
    Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN PHOSPHORYLATION OF PECAM1; PTPN11 AND GAB1, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-483, INTERACTION WITH PECAM1.
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• platelet-derived growth factor receptor signaling pathway Source: UniProtKB
• positive regulation of actin filament polymerization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• positive regulation of cell migration Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• positive regulation of cell population proliferation Source: CACAOInferred from mutant phenotypeⁱ
  • "Integrative analysis of high-throughput RNAi screen data identifies the FER and CRKL tyrosine kinases as new regulators of the mitogenic ERK-dependent pathways in transformed cells."
    Nizard P., Ezan F., Bonnier D., Le Meur N., Langouet S., Baffet G., Arlot-Bonnemains Y., Theret N.
    BMC Genomics 15:1169-1169(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of NF-kappaB transcription factor activity Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.22

    "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
    Guo C., Stark G.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL PROLIFERATION, INTERACTION WITH EGFR, PHOSPHORYLATION.
• protein autophosphorylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "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, SUBUNIT, INTERACTION WITH CTNND1.
• protein phosphorylation Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "Isolation and sequence analysis of a novel human tyrosine kinase gene."
    Hao Q.-L., Heisterkamp N., Groffen J.
    Mol. Cell. Biol. 9:1587-1593(1989) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-439.
• regulation of cell population proliferation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of epidermal growth factor receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.22

    "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
    Guo C., Stark G.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL PROLIFERATION, INTERACTION WITH EGFR, PHOSPHORYLATION.
• regulation of fibroblast migration Source: Ensembl
• regulation of lamellipodium assembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration."
    Itoh T., Hasegawa J., Tsujita K., Kanaho Y., Takenawa T.
    Sci. Signal. 2:RA52-RA52(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN REGULATION OF ACTIN CYTOSKELETON AND CELL MIGRATION, CATALYTIC ACTIVITY, DOMAIN, LIPID-BINDING, ACTIVITY REGULATION.
• regulation of mast cell degranulation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of protein phosphorylation Source: UniProtKB
• response to lipopolysaccharide Source: UniProtKB
• response to platelet-derived growth factor Source: UniProtKB
• substrate adhesion-dependent cell spreading Source: UniProtKB
• transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• tyrosine phosphorylation of STAT protein Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "The Fer tyrosine kinase cooperates with interleukin-6 to activate signal transducer and activator of transcription 3 and promote human prostate cancer cell growth."
    Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E., Aprikian A.G., Chevalier S.
    Mol. Cancer Res. 7:142-155(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN IL6 SIGNALING PATHWAY; CELL PROLIFERATION AND IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• epidermal growth factor receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.22

    "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
    Guo C., Stark G.R.
    Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN ACTIVATION OF NF-KAPPA-B DOWNSTREAM OF EGFR AND CELL PROLIFERATION, INTERACTION WITH EGFR, PHOSPHORYLATION.
• protein phosphatase 1 binding Source: Ensembl
• signaling receptor binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Coiled coil

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC 
        60         70         80         90        100
NQVDKESTVQ MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 
       110        120        130        140        150
TMMIKDKQQV KKSYIGVHQQ IEAEMIKVTK TELEKLKCSY RQLIKEMNSA 
       160        170        180        190        200
KEKYKEALAK GKETEKAKER YDKATMKLHM LHNQYVLALK GAQLHQNQYY 
       210        220        230        240        250
DITLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI VNVHKEIQMS 
       260        270        280        290        300
VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 
       310        320        330        340        350
TAESLQVMLK TLAEELMQTQ QMLLNKEEAV LELEKRIEES SETCEKKSDI 
       360        370        380        390        400
VLLLSQKQAL EELKQSVQQL RCTEAKFSAQ KELLEQKVQE NDGKEPPPVV 
       410        420        430        440        450
NYEEDARSVT SMERKERLSK FESIRHSIAG IIRSPKSALG SSALSDMISI 
       460        470        480        490        500
SEKPLAEQDW YHGAIPRIEA QELLKKQGDF LVRESHGKPG EYVLSVYSDG 
       510        520        530        540        550
QRRHFIIQYV DNMYRFEGTG FSNIPQLIDH HYTTKQVITK KSGVVLLNPI 
       560        570        580        590        600
PKDKKWILSH EDVILGELLG KGNFGEVYKG TLKDKTSVAV KTCKEDLPQE 
       610        620        630        640        650
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV SGGDFLTFLR 
       660        670        680        690        700
RKKDELKLKQ LVKFSLDAAA GMLYLESKNC IHRDLAARNC LVGENNVLKI 
       710        720        730        740        750
SDFGMSRQED GGVYSSSGLK QIPIKWTAPE ALNYGRYSSE SDVWSFGILL 
       760        770        780        790        800
WETFSLGVCP YPGMTNQQAR EQVERGYRMS APQHCPEDIS KIMMKCWDYK 
       810        820 
PENRPKFSEL QKELTIIKRK LT                               

        10         20         30         40         50
MKLHMLHNQY VLALKGAQLH QNQYYDITLP LLLDSLQKMQ EEMIKALKGI 
        60         70         80         90        100
FDEYSQITSL VTEEIVNVHK EIQMSVEQID PSTEYNNFID VHRTTAAKEQ 
       110        120        130        140        150
EIEFDTSLLE ENENLQANEI MWNNLTAESL QVMLKTLAEE LMQTQQMLLN 
       160        170        180        190        200
KEEAVLELEK RIEESSETCE KKSDIVLLLS QKQALEELKQ SVQQLRCTEA 
       210        220        230        240        250
KFSAQKELLE QKVQENDGKE PPPVVNYEED ARSVTSMERK ERLSKFESIR 
       260        270        280        290        300
HSIAGIIRSP KSALGSSALS DMISISEKPL AEQDWYHGAI PRIEAQELLK 
       310        320        330        340        350
KQGDFLVRES HGKPGEYVLS VYSDGQRRHF IIQYVDNMYR FEGTGFSNIP 
       360        370        380        390        400
QLIDHHYTTK QVITKKSGVV LLNPIPKDKK WILSHEDVIL GELLGKGNFG 
       410        420        430        440        450
EVYKGTLKDK TSVAVKTCKE DLPQELKIKF LQEAKILKQY DHPNIVKLIG 
       460        470        480        490        500
VCTQRQPVYI IMELVSGGDF LTFLRRKKDE LKLKQLVKFS LDAAAGMLYL 
       510        520        530        540        550
ESKNCIHRDL AARNCLVGEN NVLKISDFGM SRQEDGGVYS SSGLKQIPIK 
       560        570        580        590        600
WTAPEALNYG RYSSESDVWS FGILLWETFS LGVCPYPGMT NQQAREQVER 
       610        620        630        640 
GYRMSAPQHC PEDISKIMMK CWDYKPENRP KFSELQKELT IIKRKLT    

        10         20         30         40         50
MEQKMKCPHC KDQLESGFGS QSCKTCALMF SSEPSTSEVH RDQERKERLS 
        60         70         80         90        100
KFESIRHSIA GIIRSPKSAL GSSALSDMIS ISEKPLAEQD WYHGAIPRIE 
       110        120        130        140        150
AQELLKKQGD FLVRESHGKP GEYVLSVYSD GQRRHFIIQY VDNMYRFEGT 
       160        170        180        190        200
GFSNIPQLID HHYTTKQVIT KKSGVVLLNP IPKDKKWILS HEDVILGELL 
       210        220        230        240        250
GKGNFGEVYK GTLKDKTSVA VKTCKEDLPQ ELKIKFLQEA KILKQYDHPN 
       260        270        280        290        300
IVKLIGVCTQ RQPVYIIMEL VSGGDFLTFL RRKKDELKLK QLVKFSLDAA 
       310        320        330        340        350
AGMLYLESKN CIHRDLAARN CLVGENNVLK ISDFGMSRQE DGGVYSSSGL 
       360        370        380        390        400
KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA 
       410        420        430        440        450
REQVERGYRM SAPQHCPEDI SKIMMKCWDY KPENRPKFSE LQKELTIIKR 

KLT                                                    

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human and mouse protein kinases
   Human and mouse protein kinases: classification and index
2. SIMILARITY comments
   Index of protein domains and families
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. Human chromosome 5
   Human chromosome 5: entries, gene names and cross-references to MIM
7. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references