Mus musculus

UniProt Data

Accession P06240 [ UniProt ]
Name LCK_MOUSE
Description Proto-oncogene tyrosine-protein kinase LCK
Species Mus musculus
Sequence Length509

Enzyme Annotations (1)

  • EC:2.7.10.2 Non-specific protein-tyrosine kinase.
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

GO Annotations

Cellular component (9)

  • GO:0000242 Pericentriolar material
    A network of small fibers that surrounds the centrioles in cells; contains the microtubule nucleating activity of the centrosome.
  • GO:0000242 Pericentriolar material
    A network of small fibers that surrounds the centrioles in cells; contains the microtubule nucleating activity of the centrosome.
  • GO:0001772 Immunological synapse
    An area of close contact between a lymphocyte (T-, B-, or natural killer cell) and a target cell formed through the clustering of particular signaling and adhesion molecules and their associated membrane rafts on both the lymphocyte and the target cell and facilitating activation of the lymphocyte, transfer of membrane from the target cell to the lymphocyte, and in some situations killing of the target cell through release of secretory granules and/or death-pathway ligand-receptor interaction.
  • GO:0005829 Cytosol
    The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0005886 Plasma membrane
    The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0005911 Cell-cell junction
    A cell junction that forms a connection between two or more cells in a multicellular organism; excludes direct cytoplasmic junctions such as ring canals.
  • GO:0045121 Membrane raft
    Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
  • GO:0045121 Membrane raft
    Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
  • GO:0070062 Extracellular exosome
    A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.

Molecular function (23)

  • GO:0001784 Phosphotyrosine binding
    Interacting selectively and non-covalently with a phosphorylated tyrosine residue within a protein.
  • GO:0001948 Glycoprotein binding
    Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.
  • GO:0004713 Protein tyrosine kinase activity
    Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
  • GO:0004713 Protein tyrosine kinase activity
    Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
  • GO:0004713 Protein tyrosine kinase activity
    Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
  • GO:0004713 Protein tyrosine kinase activity
    Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
  • GO:0004713 Protein tyrosine kinase activity
    Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
  • GO:0004722 Protein serine/threonine phosphatase activity
    Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
  • GO:0004722 Protein serine/threonine phosphatase activity
    Catalysis of the reaction: protein serine phosphate + H2O = protein serine + phosphate, and protein threonine phosphate + H2O = protein threonine + phosphate.
  • GO:0005515 Protein binding
    Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
  • GO:0008022 Protein C-terminus binding
    Interacting selectively and non-covalently with a protein C-terminus, the end of any peptide chain at which the 1-carboxy function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
  • GO:0019901 Protein kinase binding
    Interacting selectively and non-covalently with a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
  • GO:0019903 Protein phosphatase binding
    Interacting selectively and non-covalently with any protein phosphatase.
  • GO:0042169 SH2 domain binding
    Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
  • GO:0042169 SH2 domain binding
    Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.
  • GO:0042608 T cell receptor binding
    Interacting selectively and non-covalently with a T cell receptor, the antigen-recognizing receptor on the surface of T cells.
  • GO:0042609 CD4 receptor binding
    Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages.
  • GO:0042609 CD4 receptor binding
    Interacting selectively and non-covalently with a CD4, a receptor found on the surface of T cells, monocytes and macrophages.
  • GO:0042610 CD8 receptor binding
    Interacting selectively and non-covalently with a CD8, a receptor found on the surface of thymocytes and cytotoxic and suppressor T-lymphocytes.
  • GO:0042802 Identical protein binding
    Interacting selectively and non-covalently with an identical protein or proteins.
  • GO:0043548 Phosphatidylinositol 3-kinase binding
    Interacting selectively and non-covalently with a phosphatidylinositol 3-kinase, any enzyme that catalyzes the addition of a phosphate group to an inositol lipid at the 3' position of the inositol ring.
  • GO:0051117 ATPase binding
    Interacting selectively and non-covalently with an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
  • GO:1990405 Protein antigen binding
    Interacting selectively and non-covalently with a protein antigen.

Biological process (24)

  • GO:0006468 Protein phosphorylation
    The process of introducing a phosphate group on to a protein.
  • GO:0006468 Protein phosphorylation
    The process of introducing a phosphate group on to a protein.
  • GO:0006882 Cellular zinc ion homeostasis
    Any process involved in the maintenance of an internal steady state of zinc ions at the level of a cell.
  • GO:0006919 Activation of cysteine-type endopeptidase activity involved in apoptotic process
    Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
  • GO:0006919 Activation of cysteine-type endopeptidase activity involved in apoptotic process
    Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
  • GO:0007166 Cell surface receptor signaling pathway
    A series of molecular signals initiated by activation of a receptor on the surface of a cell. The pathway begins with binding of an extracellular ligand to a cell surface receptor, or for receptors that signal in the absence of a ligand, by ligand-withdrawal or the activity of a constitutively active receptor. The pathway ends with regulation of a downstream cellular process, e.g. transcription.
  • GO:0010628 Positive regulation of gene expression
    Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
  • GO:0018108 Peptidyl-tyrosine phosphorylation
    The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
  • GO:0018108 Peptidyl-tyrosine phosphorylation
    The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
  • GO:0030217 T cell differentiation
    The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
  • GO:0030217 T cell differentiation
    The process in which a precursor cell type acquires characteristics of a more mature T-cell. A T cell is a type of lymphocyte whose definin characteristic is the expression of a T cell receptor complex.
  • GO:0042493 Response to drug
    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
  • GO:0042493 Response to drug
    Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
  • GO:0042531 Positive regulation of tyrosine phosphorylation of STAT protein
    Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein.
  • GO:0045588 Positive regulation of gamma-delta T cell differentiation
    Any process that activates or increases the frequency, rate or extent of gamma-delta T cell differentiation.
  • GO:0045589 Regulation of regulatory T cell differentiation
    Any process that modulates the frequency, rate or extent of differentiation of regulatory T cells.
  • GO:0046777 Protein autophosphorylation
    The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
  • GO:0050853 B cell receptor signaling pathway
    A series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell.
  • GO:0050856 Regulation of T cell receptor signaling pathway
    Any process that modulates the frequency, rate or extent of signaling pathways initiated by the cross-linking of an antigen receptor on a T cell.
  • GO:0050870 Positive regulation of T cell activation
    Any process that activates or increases the frequency, rate or extent of T cell activation.
  • GO:0050870 Positive regulation of T cell activation
    Any process that activates or increases the frequency, rate or extent of T cell activation.
  • GO:0051209 Release of sequestered calcium ion into cytosol
    The process in which calcium ions sequestered in the endoplasmic reticulum, Golgi apparatus or mitochondria are released into the cytosolic compartment.
  • GO:2001244 Positive regulation of intrinsic apoptotic signaling pathway
    Any process that activates or increases the frequency, rate or extent of intrinsic apoptotic signaling pathway.
  • GO:2001244 Positive regulation of intrinsic apoptotic signaling pathway
    Any process that activates or increases the frequency, rate or extent of intrinsic apoptotic signaling pathway.

Protein Sequence

>P06240
MGCVCSSNPEDDWMENIDVCENCHYPIVPLDSKISLPIRNGSEVRDPLVTYEGSLPPASPLQDNLVIALHSYEPSHDGDL
GFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTA
GSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHDLVRHYTNASDGLCTKLSRPCQTQKPQKPWWEDEWEV
PRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHPRLVRLYAVVTQEPIYIITEYME
NGSLVDFLKTPSGIKLNVNKLLDMAAQIAEGMAFIEEQNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGA
KFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYHLMMLCWKER
PEDRPTFDYLRSVLDDFFTATEGQYQPQP