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Entry version 237 (13 Feb 2019)
Sequence version 3 (15 Feb 2005)
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Protein

Tyrosine-protein kinase ABL1

Gene

Abl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (By similarity). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Regulates T-cell differentiation in a TBX21-dependent manner (PubMed:21690296). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (PubMed:21690296).By similarity12 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Mg2+ and Mn2+ were both present in the kinase buffer but Mg2+ is likely to be the in vivo cofactor.Curated

<p>This subsection of the ‘Function’ 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

Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the N-terminal cap, and contributions from an N-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation (By similarity). Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage (By similarity). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei271ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei363Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi248 – 256ATPCurated9
Nucleotide bindingi316 – 322ATPCurated7

<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

GO - Biological processi

<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

Molecular functionDNA-binding, Kinase, Transferase, Tyrosine-protein kinase
Biological processApoptosis, Autophagy, Cell adhesion, DNA damage, DNA repair, Endocytosis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.2 3474

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-375170 CDO in myogenesis
R-MMU-428890 Role of ABL in ROBO-SLIT signaling
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-69231 Cyclin D associated events in G1
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tyrosine-protein kinase ABL1 (EC:2.7.10.24 Publications)
Alternative name(s):
Abelson murine leukemia viral oncogene homolog 1
Abelson tyrosine-protein kinase 1
Proto-oncogene c-Abl
p150
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Abl1
Synonyms:Abl
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:87859 Abl1

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutants are born with the expected Mendelian frequency, but fail to thrive and most die within three weeks after birth. Most mutants are runted, and have atrophied thymuses with severe thymocyte deficiency. Mutants that survive to weaning age are most often runted, and about half of them show lymphopenia. They display a major reduction in the number of pre-B and immature B-cell classes in bone marrow with a wide variation between individuals, but essentially normal mature B-cell levels. Mutants are highly susceptible to infections.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi112P → S: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi128Y → D: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi139Y → C: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi226Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi229S → P: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi271K → M: Loss of kinase activity. 1 Publication1
Mutagenesisi315T → I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi393Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi446S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. 1 Publication1
Mutagenesisi464C → Y: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi465P → S: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi497F → L: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi505E → K: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi506V → L: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi1083L → A: Loss of nuclear export. 1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3099

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000880511 – 1123Tyrosine-protein kinase ABL1Add BLAST1123
Isoform IV (identifier: P00520-4)
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei50PhosphoserineBy similarity1
Modified residuei70Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei115PhosphotyrosineBy similarity1
Modified residuei128PhosphotyrosineBy similarity1
Modified residuei139PhosphotyrosineBy similarity1
Modified residuei172PhosphotyrosineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei215PhosphotyrosineBy similarity1
Modified residuei226Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei229PhosphoserineBy similarity1
Modified residuei253PhosphotyrosineBy similarity1
Modified residuei257PhosphotyrosineBy similarity1
Modified residuei393Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases2 Publications1
Modified residuei413PhosphotyrosineBy similarity1
Modified residuei446Phosphoserine1 Publication1
Modified residuei547Phosphothreonine1 Publication1
Modified residuei559PhosphoserineBy similarity1
Modified residuei569Phosphoserine1 Publication1
Modified residuei618Phosphoserine; by PAK2By similarity1
Modified residuei619Phosphoserine; by PAK2By similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1
Modified residuei682PhosphoserineBy similarity1
Modified residuei710N6-acetyllysine; by EP300By similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei734PhosphothreonineBy similarity1
Modified residuei750PhosphothreonineBy similarity1
Modified residuei812PhosphothreonineBy similarity1
Modified residuei821PhosphothreonineBy similarity1
Modified residuei844PhosphothreonineBy similarity1
Modified residuei909PhosphoserineBy similarity1
Modified residuei970PhosphoserineBy similarity1
Isoform IV (identifier: P00520-4)
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation.By similarity
Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity (By similarity). Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity (By similarity). DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation (By similarity). Phosphorylated by PDGFRB and PRKDC.By similarity7 Publications
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity).By similarity
Isoform IV is myristoylated on Gly-2.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00520

MaxQB - The MaxQuant DataBase

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MaxQBi
P00520

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P00520

PeptideAtlas

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PeptideAtlasi
P00520

PRoteomics IDEntifications database

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PRIDEi
P00520

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00520

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P00520

<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

Widely expressed.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026842 Expressed in 297 organ(s), highest expression level in external carotid artery

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00520 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00520 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm. Interacts (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation (By similarity). Interacts with ABI1, ABI2, BCR, CRK, FYN, LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Interacts with STX17; probably phosphorylates STX17 (By similarity). Interacts with ITGB1, HCK and FGR. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity). Interacts with TBX21 (PubMed:21690296).By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
197906, 20 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P00520

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P00520

Protein interaction database and analysis system

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IntActi
P00520, 22 interactors

Molecular INTeraction database

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MINTi
P00520

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000075167

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00520

<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

11123
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABOX-ray2.00A/B61-121[»]
1ABQX-ray2.80A61-121[»]
1FPUX-ray2.40A/B229-515[»]
1IEPX-ray2.10A/B229-515[»]
1M52X-ray2.60A/B229-515[»]
1OPJX-ray1.75A/B229-515[»]
1OPKX-ray1.80A27-515[»]
2HZNX-ray2.70A229-515[»]
2QOHX-ray1.95A/B229-515[»]
2Z60X-ray1.95A229-515[»]
3DK3X-ray2.02A/B233-514[»]
3DK6X-ray2.02A/B233-514[»]
3DK7X-ray2.01A/B233-505[»]
3IK3X-ray1.90A/B229-513[»]
3K5VX-ray1.74A/B229-515[»]
3KF4X-ray1.90A/B229-515[»]
3KFAX-ray1.22A/B229-515[»]
3MS9X-ray1.80A/B229-515[»]
3MSSX-ray1.95A/B/C/D229-515[»]
3OXZX-ray2.20A229-511[»]
3OY3X-ray1.95A/B229-511[»]
5IH2X-ray1.80M/N757-765[»]
6HD4X-ray2.03A/B229-515[»]
6HD6X-ray2.30A/B229-515[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00520

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00520

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00520

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 121SH3PROSITE-ProRule annotationAdd BLAST61
Domaini127 – 217SH2PROSITE-ProRule annotationAdd BLAST91
Domaini242 – 493Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 60CAPAdd BLAST60
Regioni863 – 961DNA-bindingAdd BLAST99
Regioni945 – 1123F-actin-bindingBy similarityAdd BLAST179

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi381 – 405Kinase activation loopAdd BLAST25
Motifi605 – 609Nuclear localization signal 1Sequence analysis5
Motifi708 – 714Nuclear localization signal 2Sequence analysis7
Motifi761 – 768Nuclear localization signal 3Sequence analysis8
Motifi1083 – 1093Nuclear export signalAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi18 – 22Poly-Ser5
Compositional biasi605 – 609Poly-Lys5
Compositional biasi804 – 1012Pro-richAdd BLAST209
Compositional biasi891 – 897Poly-Pro7

<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

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153838

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004162

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00520

KEGG Orthology (KO)

More...
KOi
K06619

Identification of Orthologs from Complete Genome Data

More...
OMAi
GAFRESG

Database of Orthologous Groups

More...
OrthoDBi
182823at2759

TreeFam database of animal gene trees

More...
TreeFami
TF105081

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09935 SH2_ABL, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR033221 ABL1
IPR035837 ABL_SH2
IPR015015 F-actin_binding
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

The PANTHER Classification System

More...
PANTHERi
PTHR24418:SF88 PTHR24418:SF88, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08919 F_actin_bind, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00401 SH2DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00808 FABD, 1 hit
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 1 hit

<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform I (identifier: P00520-1) [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
        10         20         30         40         50
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS
60 70 80 90 100
KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC
110 120 130 140 150
EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL
160 170 180 190 200
VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH
210 220 230 240 250
HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT DITMKHKLGG
260 270 280 290 300
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
310 320 330 340 350
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA
360 370 380 390 400
MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK
410 420 430 440 450
FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE
460 470 480 490 500
LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES
510 520 530 540 550
SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE QKDAPDTPEL
560 570 580 590 600
LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
610 620 630 640 650
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS
660 670 680 690 700
DAAEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA
710 720 730 740 750
EEESGMSSSK RFLRSCSASC MPHGARDTEW RSVTLPRDLP SAGKQFDSST
760 770 780 790 800
FGGHKSEKPA LPRKRTSESR SEQVAKSTAM PPPRLVKKNE EAAEEGFKDT
810 820 830 840 850
ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS GMGTPATAEP
860 870 880 890 900
APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
910 920 930 940 950
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP
960 970 980 990 1000
VPPSVPKPQS TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS
1010 1020 1030 1040 1050
TRVSLRKTRQ PPERIASGTI TKGVVLDSTE ALCLAISRNS EQMASHSAVL
1060 1070 1080 1090 1100
EAGKNLYTFC VSYVDSIQQM RNKFAFREAI NKLESNLREL QICPATASSG
1110 1120
PAATQDFSKL LSSVKEISDI VRR
Length:1,123
Mass (Da):122,673
Last modified:February 15, 2005 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBD48ADE8557AE95C
GO
Isoform II (identifier: P00520-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MISFDLLSDELHLKLLVLDV

Show »
Length:1,117
Mass (Da):122,179
Checksum:i002F9D346307028A
GO
Isoform III (identifier: P00520-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MSQRWTYTKCRVQRDPALPFM

Show »
Length:1,118
Mass (Da):122,480
Checksum:iAB3B4510AE8C5C38
GO
Isoform IV (identifier: P00520-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MGQQPGKVLGDQRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH

Show »
Length:1,142
Mass (Da):124,769
Checksum:i7A9DB9E772EAF05F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AV23A2AV23_MOUSE
Tyrosine-protein kinase ABL1
Abl1
114Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A6YXS9A0A0A6YXS9_MOUSE
Tyrosine-protein kinase ABL1
Abl1
78Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A6YY65A0A0A6YY65_MOUSE
Tyrosine-protein kinase ABL1
Abl1
64Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A6YVY6A0A0A6YVY6_MOUSE
Tyrosine-protein kinase ABL1
Abl1
71Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti184 – 187LYVS → VGDW in AAB60451 (PubMed:7665185).Curated4
Sequence conflicti184 – 187LYVS → VGDW in AAB60450 (PubMed:7665185).Curated4
Sequence conflicti782 – 786PPRLV → LPGWL in AAA88241 (PubMed:3317402).Curated5
Sequence conflicti987D → G in BAC41088 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0049591 – 26MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II. CuratedAdd BLAST26
Alternative sequenceiVSP_0049581 – 26MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III. CuratedAdd BLAST26
Alternative sequenceiVSP_0049601 – 26MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV. 1 PublicationAdd BLAST26

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J02995 mRNA Translation: AAA88241.1
AK090095 mRNA Translation: BAC41088.1
BC059260 mRNA Translation: AAH59260.1
U14721, U14720 Genomic DNA Translation: AAB60451.1
U14721, U14720 Genomic DNA Translation: AAB60450.1
U14721, U13835 Genomic DNA Translation: AAB60448.1
U14721, U13835 Genomic DNA Translation: AAB60449.1
X07539 Genomic DNA Translation: CAA30411.1
X07539 Genomic DNA Translation: CAA30412.1
X07540 Genomic DNA Translation: CAA30413.1
X07541 Genomic DNA Translation: CAA30414.1
M12263 mRNA Translation: AAA37136.1
M12264 mRNA Translation: AAA37137.1
M12265 mRNA Translation: AAA37138.1
M12266 Genomic DNA Translation: AAA37134.1
K03228 mRNA Translation: AAA37135.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS15901.1 [P00520-1]
CCDS50563.1 [P00520-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
A39962
S00774

NCBI Reference Sequences

More...
RefSeqi
NP_001106174.1, NM_001112703.2 [P00520-4]
NP_001269974.1, NM_001283045.1 [P00520-3]
NP_001269975.1, NM_001283046.1 [P00520-2]
NP_033724.2, NM_009594.4 [P00520-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.1318

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842 [P00520-1]
ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842 [P00520-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
11350

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11350

UCSC genome browser

More...
UCSCi
uc008jdz.3 mouse [P00520-1]
uc033hmk.1 mouse [P00520-2]
uc033hml.1 mouse [P00520-3]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<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

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02995 mRNA Translation: AAA88241.1
AK090095 mRNA Translation: BAC41088.1
BC059260 mRNA Translation: AAH59260.1
U14721, U14720 Genomic DNA Translation: AAB60451.1
U14721, U14720 Genomic DNA Translation: AAB60450.1
U14721, U13835 Genomic DNA Translation: AAB60448.1
U14721, U13835 Genomic DNA Translation: AAB60449.1
X07539 Genomic DNA Translation: CAA30411.1
X07539 Genomic DNA Translation: CAA30412.1
X07540 Genomic DNA Translation: CAA30413.1
X07541 Genomic DNA Translation: CAA30414.1
M12263 mRNA Translation: AAA37136.1
M12264 mRNA Translation: AAA37137.1
M12265 mRNA Translation: AAA37138.1
M12266 Genomic DNA Translation: AAA37134.1
K03228 mRNA Translation: AAA37135.1
CCDSiCCDS15901.1 [P00520-1]
CCDS50563.1 [P00520-4]
PIRiA39962
S00774
RefSeqiNP_001106174.1, NM_001112703.2 [P00520-4]
NP_001269974.1, NM_001283045.1 [P00520-3]
NP_001269975.1, NM_001283046.1 [P00520-2]
NP_033724.2, NM_009594.4 [P00520-1]
UniGeneiMm.1318

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABOX-ray2.00A/B61-121[»]
1ABQX-ray2.80A61-121[»]
1FPUX-ray2.40A/B229-515[»]
1IEPX-ray2.10A/B229-515[»]
1M52X-ray2.60A/B229-515[»]
1OPJX-ray1.75A/B229-515[»]
1OPKX-ray1.80A27-515[»]
2HZNX-ray2.70A229-515[»]
2QOHX-ray1.95A/B229-515[»]
2Z60X-ray1.95A229-515[»]
3DK3X-ray2.02A/B233-514[»]
3DK6X-ray2.02A/B233-514[»]
3DK7X-ray2.01A/B233-505[»]
3IK3X-ray1.90A/B229-513[»]
3K5VX-ray1.74A/B229-515[»]
3KF4X-ray1.90A/B229-515[»]
3KFAX-ray1.22A/B229-515[»]
3MS9X-ray1.80A/B229-515[»]
3MSSX-ray1.95A/B/C/D229-515[»]
3OXZX-ray2.20A229-511[»]
3OY3X-ray1.95A/B229-511[»]
5IH2X-ray1.80M/N757-765[»]
6HD4X-ray2.03A/B229-515[»]
6HD6X-ray2.30A/B229-515[»]
ProteinModelPortaliP00520
SMRiP00520
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197906, 20 interactors
CORUMiP00520
ELMiP00520
IntActiP00520, 22 interactors
MINTiP00520
STRINGi10090.ENSMUSP00000075167

Chemistry databases

BindingDBiP00520
ChEMBLiCHEMBL3099

PTM databases

iPTMnetiP00520
PhosphoSitePlusiP00520

Proteomic databases

jPOSTiP00520
MaxQBiP00520
PaxDbiP00520
PeptideAtlasiP00520
PRIDEiP00520

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842 [P00520-1]
ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842 [P00520-4]
GeneIDi11350
KEGGimmu:11350
UCSCiuc008jdz.3 mouse [P00520-1]
uc033hmk.1 mouse [P00520-2]
uc033hml.1 mouse [P00520-3]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
25
MGIiMGI:87859 Abl1

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000153838
HOVERGENiHBG004162
InParanoidiP00520
KOiK06619
OMAiGAFRESG
OrthoDBi182823at2759
TreeFamiTF105081

Enzyme and pathway databases

BRENDAi2.7.10.2 3474
ReactomeiR-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-375170 CDO in myogenesis
R-MMU-428890 Role of ABL in ROBO-SLIT signaling
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-69231 Cyclin D associated events in G1
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Abl1 mouse
EvolutionaryTraceiP00520

Protein Ontology

More...
PROi
PR:P00520

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026842 Expressed in 297 organ(s), highest expression level in external carotid artery
ExpressionAtlasiP00520 baseline and differential
GenevisibleiP00520 MM

Family and domain databases

CDDicd09935 SH2_ABL, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR033221 ABL1
IPR035837 ABL_SH2
IPR015015 F-actin_binding
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PANTHERiPTHR24418:SF88 PTHR24418:SF88, 1 hit
PfamiView protein in Pfam
PF08919 F_actin_bind, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00808 FABD, 1 hit
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiABL1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00520
Secondary accession number(s): P97896
, Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: February 13, 2019
This is version 237 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

3D-structure, Complete proteome, Reference proteome

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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