Homo sapiens

UniProt Data

Accession P00519 [ UniProt ]
Name ABL1_HUMAN
Description Tyrosine-protein kinase ABL1
Species Homo sapiens
Sequence Length1130

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 (18)

  • GO:0005634 Nucleus
    A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
  • GO:0005634 Nucleus
    A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
  • GO:0005634 Nucleus
    A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
  • GO:0005654 Nucleoplasm
    That part of the nuclear content other than the chromosomes or the nucleolus.
  • GO:0005654 Nucleoplasm
    That part of the nuclear content other than the chromosomes or the nucleolus.
  • GO:0005730 Nucleolus
    A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
  • GO:0005737 Cytoplasm
    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005737 Cytoplasm
    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005739 Mitochondrion
    A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
  • 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:0005829 Cytosol
    The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0015629 Actin cytoskeleton
    The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
  • GO:0016604 Nuclear body
    Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
  • GO:0030425 Dendrite
    A neuron projection that has a short, tapering, often branched, morphology, receives and integrates signals from other neurons or from sensory stimuli, and conducts a nerve impulse towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
  • GO:0043025 Neuronal cell body
    The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
  • GO:0043234 Protein complex
    A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical.
  • GO:0048471 Perinuclear region of cytoplasm
    Cytoplasm situated near, or occurring around, the nucleus.
  • GO:0098794 Postsynapse
    The part of a synapse that is part of the post-synaptic cell.

Molecular function (22)

  • GO:0000287 Magnesium ion binding
    Interacting selectively and non-covalently with magnesium (Mg) ions.
  • GO:0001784 Phosphotyrosine binding
    Interacting selectively and non-covalently with a phosphorylated tyrosine residue within a protein.
  • GO:0003677 DNA binding
    Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
  • GO:0003785 Actin monomer binding
    Interacting selectively and non-covalently with monomeric actin, also known as G-actin.
  • GO:0004515 Nicotinate-nucleotide adenylyltransferase activity
    Catalysis of the reaction: ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+.
  • GO:0004672 Protein kinase activity
    Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
  • 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:0004715 Non-membrane spanning protein tyrosine kinase activity
    Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein.
  • GO:0005080 Protein kinase C binding
    Interacting selectively and non-covalently with protein kinase C.
  • 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:0005524 ATP binding
    Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • 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:0017124 SH3 domain binding
    Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
  • GO:0019905 Syntaxin binding
    Interacting selectively and non-covalently with a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse.
  • GO:0030145 Manganese ion binding
    Interacting selectively and non-covalently with manganese (Mn) ions.
  • 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:0051019 Mitogen-activated protein kinase binding
    Interacting selectively and non-covalently with a mitogen-activated protein kinase.
  • GO:0070064 Proline-rich region binding
    Interacting selectively and non-covalently with a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein.
  • GO:0070064 Proline-rich region binding
    Interacting selectively and non-covalently with a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein.

Biological process (46)

  • GO:0000278 Mitotic cell cycle
    Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.
  • GO:0001934 Positive regulation of protein phosphorylation
    Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.
  • GO:0006298 Mismatch repair
    A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination.
  • GO:0006355 Regulation of transcription, DNA-templated
    Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
  • GO:0006464 Cellular protein modification process
    The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
  • GO:0006974 Cellular response to DNA damage stimulus
    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
  • GO:0006975 DNA damage induced protein phosphorylation
    The widespread phosphorylation of various molecules, triggering many downstream processes, that occurs in response to the detection of DNA damage.
  • GO:0006979 Response to oxidative stress
    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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
  • GO:0007050 Cell cycle arrest
    A regulatory process that halts progression through the cell cycle during one of the normal phases (G1, S, G2, M).
  • GO:0007204 Positive regulation of cytosolic calcium ion concentration
    Any process that increases the concentration of calcium ions in the cytosol.
  • GO:0008630 Intrinsic apoptotic signaling pathway in response to DNA damage
    A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the detection of DNA damage, and ends when the execution phase of apoptosis is triggered.
  • GO:0010506 Regulation of autophagy
    Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
  • 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:0018108 Peptidyl-tyrosine phosphorylation
    The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine.
  • GO:0030036 Actin cytoskeleton organization
    A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
  • GO:0030100 Regulation of endocytosis
    Any process that modulates the frequency, rate or extent of endocytosis.
  • GO:0030155 Regulation of cell adhesion
    Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix.
  • GO:0030516 Regulation of axon extension
    Any process that modulates the rate, direction or extent of axon extension.
  • GO:0031113 Regulation of microtubule polymerization
    Any process that modulates the frequency, rate or extent of microtubule polymerization.
  • GO:0032956 Regulation of actin cytoskeleton organization
    Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
  • GO:0034599 Cellular response to oxidative stress
    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
  • GO:0035791 Platelet-derived growth factor receptor-beta signaling pathway
    A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
  • GO:0038083 Peptidyl-tyrosine autophosphorylation
    The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
  • GO:0038083 Peptidyl-tyrosine autophosphorylation
    The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein.
  • GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis
    An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes.
  • GO:0042770 Signal transduction in response to DNA damage
    A cascade of processes induced by the detection of DNA damage within a cell.
  • GO:0043065 Positive regulation of apoptotic process
    Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
  • GO:0045184 Establishment of protein localization
    The directed movement of a protein to a specific location.
  • 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:0050731 Positive regulation of peptidyl-tyrosine phosphorylation
    Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine.
  • GO:0051149 Positive regulation of muscle cell differentiation
    Any process that activates or increases the frequency, rate or extent of muscle cell differentiation.
  • GO:0051353 Positive regulation of oxidoreductase activity
    Any process that activates or increases the frequency, rate or extent of oxidoreductase activity, the catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered.
  • GO:0051444 Negative regulation of ubiquitin-protein transferase activity
    Any process that stops, prevents, or reduces the frequency, rate or extent of ubiquitin transferase activity.
  • GO:0051444 Negative regulation of ubiquitin-protein transferase activity
    Any process that stops, prevents, or reduces the frequency, rate or extent of ubiquitin transferase activity.
  • GO:0051882 Mitochondrial depolarization
    The process in which the potential difference across the mitochondrial membrane is reduced from its steady state level.
  • GO:0070301 Cellular response to hydrogen peroxide
    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
  • GO:0071901 Negative regulation of protein serine/threonine kinase activity
    Any process that decreases the rate, frequency, or extent of protein serine/threonine kinase activity.
  • GO:1900275 Negative regulation of phospholipase C activity
    Any process that stops, prevents or reduces the frequency, rate or extent of phospholipase C activity.
  • GO:1903351 Cellular response to dopamine
    Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a dopamine stimulus.
  • GO:1904528 Positive regulation of microtubule binding
    Any process that activates or increases the frequency, rate or extent of microtubule binding.
  • GO:1904531 Positive regulation of actin filament binding
    Any process that activates or increases the frequency, rate or extent of actin filament binding.
  • GO:1990051 Activation of protein kinase C activity
    Any process that initiates the activity of the inactive enzyme protein kinase C.
  • GO:2000145 Regulation of cell motility
    Any process that modulates the frequency, rate or extent of cell motility.
  • GO:2000249 Regulation of actin cytoskeleton reorganization
    Any process that modulates the frequency, rate or extent of actin cytoskeleton reorganization.
  • GO:2001020 Regulation of response to DNA damage stimulus
    Any process that modulates the frequency, rate or extent of response to DNA damage stimulus.

Protein Sequence

>P00519
MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTL
SITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQ
RSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERT
DITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY
GNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAK
FPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNP
SDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESD
PLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRD
ISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSAS
CVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKD
IMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKH
SSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVL
PATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALC
LAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSS
VKEISDIVQR