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Protein

Tyrosine-protein kinase ABL1

Gene

ABL1

Organism
Homo sapiens (Human)
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' (PubMed:28428613). 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-153' 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. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (By similarity).By similarity23 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+By similarity

<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. Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage. Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity (By similarity). Activated by 5-(1,3-diaryl-1H-pyrazol-4-yl)hydantoin, 5-[3-(4-fluorophenyl)-1-phenyl-1H-pyrazol-4-yl]-2,4-imidazolidinedione (DPH) (PubMed:28428613). Inhibited by ABI1, whose activity is controlled by ABL1 itself through tyrosine phosphorylation. Also inhibited by imatinib mesylate (Gleevec) which is used for the treatment of chronic myeloid leukemia (CML), and by VX-680, an inhibitor that acts also on imatinib-resistant mutants (PubMed:28428613).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 sitei271ATP1
<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 – 256ATP9
Nucleotide bindingi316 – 322ATP7

<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

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BRENDAi
2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-375170 CDO in myogenesis
R-HSA-428890 Role of ABL in ROBO-SLIT signaling
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-69231 Cyclin D associated events in G1
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P00519

SIGNOR Signaling Network Open Resource

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SIGNORi
P00519

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P00519 Predicted

<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:2.7.10.22 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, JTK7
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000097007.17

Human Gene Nomenclature Database

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HGNCi
HGNC:76 ABL1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
189980 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P00519

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Leukemia, chronic myeloid (CML)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts.
See also OMIM:608232
A chromosomal aberration involving ABL1 has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL).
Congenital heart defects and skeletal malformations syndrome (CHDSKM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by congenital heart disease with atrial and ventricular septal defects, variable skeletal abnormalities, and failure to thrive. Skeletal defects include pectus excavatum, scoliosis, and finger contractures. Some patient exhibit joint laxity.
See also OMIM:617602
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_079482226Y → C in CHDSKM; increases kinase activity; no effect on protein levels. 1 PublicationCorresponds to variant dbSNP:rs1060499547Ensembl.1
Natural variantiVAR_079483337A → T in CHDSKM; increases kinase activity; no effect on protein levels. 1 PublicationCorresponds to variant dbSNP:rs1060499548Ensembl.1

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>Mutagenesisi735T → A: Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei26 – 27Breakpoint for translocation to form BCR-ABL oncogene2

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
25

MalaCards human disease database

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MalaCardsi
ABL1
MIMi608232 phenotype
617602 phenotype

Open Targets

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OpenTargetsi
ENSG00000097007

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
521 Chronic myeloid leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24413

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1862

Drug and drug target database

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DrugBanki
DB08043 1-[4-(PYRIDIN-4-YLOXY)PHENYL]-3-[3-(TRIFLUOROMETHYL)PHENYL]UREA
DB00171 Adenosine triphosphate
DB06616 Bosutinib
DB01254 Dasatinib
DB00619 Imatinib
DB08231 MYRISTIC ACID
DB03878 N-[4-Methyl-3-[[4-(3-Pyridinyl)-2-Pyrimidinyl]Amino]Phenyl]-3-Pyridinecarboxamide
DB04868 Nilotinib
DB08901 Ponatinib
DB12323 Radotinib
DB08896 Regorafenib
DB05184 XL228

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1923

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ABL1

Domain mapping of disease mutations (DMDM)

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DMDMi
85681908

<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_00000880501 – 1130Tyrosine-protein kinase ABL1Add BLAST1130

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 residuei50PhosphoserineCombined sources1 Publication1
Modified residuei70Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei115Phosphotyrosine1 Publication1
Modified residuei128Phosphotyrosine1 Publication1
Modified residuei139Phosphotyrosine1 Publication1
Modified residuei172Phosphotyrosine1 Publication1
Modified residuei185Phosphotyrosine1 Publication1
Modified residuei215Phosphotyrosine1 Publication1
Modified residuei226Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei229PhosphoserineBy similarity1
Modified residuei253PhosphotyrosineCombined sources1
Modified residuei257PhosphotyrosineCombined sources1
Modified residuei393Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases1 Publication1
Modified residuei413PhosphotyrosineCombined sources1
Modified residuei446PhosphoserineBy similarity1
Modified residuei559PhosphoserineCombined sources1
Modified residuei569PhosphoserineCombined sources1
Modified residuei618Phosphoserine; by PAK21 Publication1
Modified residuei619Phosphoserine; by PAK21 Publication1
Modified residuei620PhosphoserineCombined sources1
Modified residuei659PhosphoserineCombined sources1
Modified residuei683PhosphoserineCombined sources1
Modified residuei711N6-acetyllysine; by EP3001 Publication1
Modified residuei718PhosphoserineCombined sources1
Modified residuei735Phosphothreonine1 Publication1
Modified residuei751PhosphothreonineCombined sources1
Modified residuei781PhosphothreonineCombined sources1
Modified residuei814PhosphothreonineCombined sources1
Modified residuei823PhosphothreonineCombined sources1
Modified residuei844PhosphothreonineCombined sources1
Modified residuei852PhosphothreonineCombined sources1
Modified residuei855PhosphoserineCombined sources1
Modified residuei917PhosphoserineCombined sources1
Modified residuei977PhosphoserineCombined sources1
Isoform IB (identifier: P00519-2)
<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

<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-711 by EP300 which promotes the cytoplasmic translocation.1 Publication
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. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation (By similarity). Phosphorylation at Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division (By similarity). Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1. Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation. Phosphorylated by PRKDC (By similarity).By similarity
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P00519

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00519

MaxQB - The MaxQuant DataBase

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MaxQBi
P00519

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

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PaxDbi
P00519

PeptideAtlas

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PeptideAtlasi
P00519

PRoteomics IDEntifications database

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PRIDEi
P00519

ProteomicsDB human proteome resource

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ProteomicsDBi
51259
51260 [P00519-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00519

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

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PhosphoSitePlusi
P00519

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P00519

<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

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Bgeei
ENSG00000097007 Expressed in 229 organ(s), highest expression level in frontal pole

CleanEx database of gene expression profiles

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CleanExi
HS_ABL1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00519 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00519 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB002686
HPA027251
HPA027280
HPA028409

<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 SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16, ITGB1 and HCK (By similarity). Interacts with STX17; probably phosphorylates STX17. Interacts with INPPL1/SHIP2. 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-735 and, sequesters ABL1 into the cytoplasm. Interacts with ABI1, ABI2, BCR, CRK, FGR, FYN, HCK, 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 (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases. Interacts with TBX21 (By similarity).By similarity23 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
106543, 195 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P00519

Database of interacting proteins

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DIPi
DIP-1042N

Protein interaction database and analysis system

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IntActi
P00519, 230 interactors

Molecular INTeraction database

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MINTi
P00519

STRING: functional protein association networks

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STRINGi
9606.ENSP00000361423

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00519

<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

11130
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
1AB2NMR-A120-220[»]
1ABLmodel-A65-121[»]
1AWONMR-A65-119[»]
1BBZX-ray1.65A/C/E/G64-121[»]
1JU5NMR-C62-122[»]
1OPLX-ray3.42A/B27-512[»]
1ZZPNMR-A1007-1130[»]
2ABLX-ray2.50A57-218[»]
2E2BX-ray2.20A/B229-515[»]
2F4JX-ray1.91A229-513[»]
2FO0X-ray2.27A38-512[»]
2G1TX-ray1.80A/B/C/D229-512[»]
2G2FX-ray2.70A/B229-512[»]
2G2HX-ray2.00A/B229-512[»]
2G2IX-ray3.12A/B229-512[»]
2GQGX-ray2.40A/B229-500[»]
2HIWX-ray2.20A/B230-512[»]
2HYYX-ray2.40A/B/C/D228-500[»]
2HZ0X-ray2.10A/B228-497[»]
2HZ4X-ray2.80A/B/C228-500[»]
2HZIX-ray1.70A/B229-500[»]
2O88X-ray1.75A/B64-121[»]
2V7AX-ray2.50A/B229-512[»]
3CS9X-ray2.21A/B/C/D229-500[»]
3EG0X-ray2.30A60-121[»]
3EG1X-ray1.85A/B60-121[»]
3EG2X-ray1.80A60-121[»]
3EG3X-ray1.40A60-121[»]
3EGUX-ray2.25A60-121[»]
3K2MX-ray1.75A/B121-232[»]
3PYYX-ray1.85A/B229-512[»]
3QRIX-ray2.10A/B229-499[»]
3QRJX-ray1.82A/B229-499[»]
3QRKX-ray2.30A229-499[»]
3T04X-ray2.10A112-232[»]
3UE4X-ray2.42A/B229-512[»]
3UYOX-ray1.83A112-232[»]
4J9BX-ray1.70A60-121[»]
4J9CX-ray1.05A60-121[»]
4J9DX-ray1.50A/C/E60-121[»]
4J9EX-ray1.40A/C/E60-121[»]
4J9FX-ray1.09A/C/E60-121[»]
4J9GX-ray1.80A/C/E60-121[»]
4J9HX-ray1.70A/B/C/D/E/F60-121[»]
4J9IX-ray2.20A/C/E60-121[»]
4JJBX-ray1.65A60-121[»]
4JJCX-ray1.60A60-121[»]
4JJDX-ray1.60A60-121[»]
4TWPX-ray2.40A/B233-503[»]
4WA9X-ray2.20A/B246-512[»]
4XEYX-ray2.89A/B119-515[»]
4YC8X-ray2.90A/B229-512[»]
4ZOGX-ray2.30A/B229-511[»]
5DC0X-ray2.23B112-232[»]
5DC4X-ray1.48A112-232[»]
5DC9X-ray1.56A112-232[»]
5HU9X-ray1.53A229-500[»]
5MO4X-ray2.17A27-515[»]
5NP2X-ray1.60A/B64-120[»]
5OAZX-ray1.03A/B60-121[»]
6AMVNMR-A26-236[»]
6AMWNMR-A26-236[»]
6BL8X-ray2.50A/B233-504[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00519

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

More...
SMRi
P00519

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00519

<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
Regioni869 – 968DNA-bindingBy similarityAdd BLAST100
Regioni953 – 1130F-actin-bindingAdd BLAST178

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
Motifi709 – 715Nuclear localization signal 2Sequence analysis7
Motifi762 – 769Nuclear localization signal 3Sequence analysis8
Motifi1090 – 1100Nuclear export signalBy similarityAdd 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 biasi782 – 1019Pro-richAdd BLAST238
Compositional biasi897 – 903Poly-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

More...
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
P00519

KEGG Orthology (KO)

More...
KOi
K06619

Identification of Orthologs from Complete Genome Data

More...
OMAi
GAFRESG

Database of Orthologous Groups

More...
OrthoDBi
182823at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00519

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

More...
Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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 (2+)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.

This entry describes 2 <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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform IA (identifier: P00519-1) [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 NKPTVYGVSP NYDKWEMERT DITMKHKLGG
260 270 280 290 300
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
310 320 330 340 350
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL 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 GKQGVRGAVS TLLQAPELPT KTRTSRRAAE HRDTTDVPEM
560 570 580 590 600
PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF
610 620 630 640 650
SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP
660 670 680 690 700
LDTADPAKSP KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT
710 720 730 740 750
GEEEGGGSSS KRFLRSCSAS CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS
760 770 780 790 800
TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV TPPPRLVKKN EEAADEVFKD
810 820 830 840 850
IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS ALGTPAAAEP
860 870 880 890 900
VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP
910 920 930 940 950
PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ
960 970 980 990 1000
PGEGLKKPVL PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST
1010 1020 1030 1040 1050
AFIPLISTRV SLRKTRQPPE RIASGAITKG VVLDSTEALC LAISRNSEQM
1060 1070 1080 1090 1100
ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC
1110 1120 1130
PATAGSGPAA TQDFSKLLSS VKEISDIVQR
Length:1,130
Mass (Da):122,873
Last modified:January 24, 2006 - v4
<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:i85FE6C1C0E483EA2
GO
Isoform IB (identifier: P00519-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,149
Mass (Da):124,955
Checksum:iDF9D4512F78FFE52
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
R4GRW0R4GRW0_HUMAN
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>

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 conflicti159G → S in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti424 – 425AF → GK (PubMed:6191223).Curated2
Sequence conflicti445L → R in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti459E → K in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti520S → T in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti719A → V in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti837G → E in CAA34438 (PubMed:2687768).Curated1
Sequence conflicti837G → W in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti863G → R in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti894R → K in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti917 – 919SPS → RPG in AAA51561 (PubMed:3021337).Curated3
Sequence conflicti952G → A in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti967 – 968QS → HP in AAA51561 (PubMed:3021337).Curated2
Sequence conflicti982P → PL in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti1022Missing in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti1045R → G in AAA51561 (PubMed:3021337).Curated1
Sequence conflicti1103T → S in AAA51561 (PubMed:3021337).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03267647R → G in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_051692140L → P1 PublicationCorresponds to variant dbSNP:rs1064152Ensembl.1
Natural variantiVAR_032677166R → K in a melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_079482226Y → C in CHDSKM; increases kinase activity; no effect on protein levels. 1 PublicationCorresponds to variant dbSNP:rs1060499547Ensembl.1
Natural variantiVAR_051693247K → R. Corresponds to variant dbSNP:rs34549764Ensembl.1
Natural variantiVAR_079483337A → T in CHDSKM; increases kinase activity; no effect on protein levels. 1 PublicationCorresponds to variant dbSNP:rs1060499548Ensembl.1
Natural variantiVAR_025043706G → V2 PublicationsCorresponds to variant dbSNP:rs34634745Ensembl.1
Natural variantiVAR_032678810P → L1 PublicationCorresponds to variant dbSNP:rs2229071Ensembl.1
Natural variantiVAR_025044852T → P1 Publication1
Natural variantiVAR_025045900P → S1 PublicationCorresponds to variant dbSNP:rs35266696Ensembl.1
Natural variantiVAR_051694968S → P. Corresponds to variant dbSNP:rs1064165Ensembl.1
Natural variantiVAR_025046972S → L2 PublicationsCorresponds to variant dbSNP:rs2229067Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0049571 – 26MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKKESSRHGGPHCN VFVEH in isoform IB. 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
M14752 mRNA Translation: AAA51561.1
X16416 mRNA Translation: CAA34438.1
U07563 Genomic DNA Translation: AAB60394.1
U07563, U07561 Genomic DNA Translation: AAB60393.1
DQ145721 Genomic DNA Translation: AAZ38718.1
AL359092 Genomic DNA No translation available.
AL161733 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW87948.1
BC117451 mRNA Translation: AAI17452.1
S69223 Genomic DNA Translation: AAD14034.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS35165.1 [P00519-2]
CCDS35166.1 [P00519-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S08519 TVHUA

NCBI Reference Sequences

More...
RefSeqi
NP_005148.2, NM_005157.5 [P00519-1]
NP_009297.2, NM_007313.2 [P00519-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.431048

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000318560; ENSP00000323315; ENSG00000097007 [P00519-1]
ENST00000372348; ENSP00000361423; ENSG00000097007 [P00519-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:25

UCSC genome browser

More...
UCSCi
uc004bzv.4 human [P00519-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14752 mRNA Translation: AAA51561.1
X16416 mRNA Translation: CAA34438.1
U07563 Genomic DNA Translation: AAB60394.1
U07563, U07561 Genomic DNA Translation: AAB60393.1
DQ145721 Genomic DNA Translation: AAZ38718.1
AL359092 Genomic DNA No translation available.
AL161733 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW87948.1
BC117451 mRNA Translation: AAI17452.1
S69223 Genomic DNA Translation: AAD14034.1
CCDSiCCDS35165.1 [P00519-2]
CCDS35166.1 [P00519-1]
PIRiS08519 TVHUA
RefSeqiNP_005148.2, NM_005157.5 [P00519-1]
NP_009297.2, NM_007313.2 [P00519-2]
UniGeneiHs.431048

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AB2NMR-A120-220[»]
1ABLmodel-A65-121[»]
1AWONMR-A65-119[»]
1BBZX-ray1.65A/C/E/G64-121[»]
1JU5NMR-C62-122[»]
1OPLX-ray3.42A/B27-512[»]
1ZZPNMR-A1007-1130[»]
2ABLX-ray2.50A57-218[»]
2E2BX-ray2.20A/B229-515[»]
2F4JX-ray1.91A229-513[»]
2FO0X-ray2.27A38-512[»]
2G1TX-ray1.80A/B/C/D229-512[»]
2G2FX-ray2.70A/B229-512[»]
2G2HX-ray2.00A/B229-512[»]
2G2IX-ray3.12A/B229-512[»]
2GQGX-ray2.40A/B229-500[»]
2HIWX-ray2.20A/B230-512[»]
2HYYX-ray2.40A/B/C/D228-500[»]
2HZ0X-ray2.10A/B228-497[»]
2HZ4X-ray2.80A/B/C228-500[»]
2HZIX-ray1.70A/B229-500[»]
2O88X-ray1.75A/B64-121[»]
2V7AX-ray2.50A/B229-512[»]
3CS9X-ray2.21A/B/C/D229-500[»]
3EG0X-ray2.30A60-121[»]
3EG1X-ray1.85A/B60-121[»]
3EG2X-ray1.80A60-121[»]
3EG3X-ray1.40A60-121[»]
3EGUX-ray2.25A60-121[»]
3K2MX-ray1.75A/B121-232[»]
3PYYX-ray1.85A/B229-512[»]
3QRIX-ray2.10A/B229-499[»]
3QRJX-ray1.82A/B229-499[»]
3QRKX-ray2.30A229-499[»]
3T04X-ray2.10A112-232[»]
3UE4X-ray2.42A/B229-512[»]
3UYOX-ray1.83A112-232[»]
4J9BX-ray1.70A60-121[»]
4J9CX-ray1.05A60-121[»]
4J9DX-ray1.50A/C/E60-121[»]
4J9EX-ray1.40A/C/E60-121[»]
4J9FX-ray1.09A/C/E60-121[»]
4J9GX-ray1.80A/C/E60-121[»]
4J9HX-ray1.70A/B/C/D/E/F60-121[»]
4J9IX-ray2.20A/C/E60-121[»]
4JJBX-ray1.65A60-121[»]
4JJCX-ray1.60A60-121[»]
4JJDX-ray1.60A60-121[»]
4TWPX-ray2.40A/B233-503[»]
4WA9X-ray2.20A/B246-512[»]
4XEYX-ray2.89A/B119-515[»]
4YC8X-ray2.90A/B229-512[»]
4ZOGX-ray2.30A/B229-511[»]
5DC0X-ray2.23B112-232[»]
5DC4X-ray1.48A112-232[»]
5DC9X-ray1.56A112-232[»]
5HU9X-ray1.53A229-500[»]
5MO4X-ray2.17A27-515[»]
5NP2X-ray1.60A/B64-120[»]
5OAZX-ray1.03A/B60-121[»]
6AMVNMR-A26-236[»]
6AMWNMR-A26-236[»]
6BL8X-ray2.50A/B233-504[»]
ProteinModelPortaliP00519
SMRiP00519
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106543, 195 interactors
CORUMiP00519
DIPiDIP-1042N
IntActiP00519, 230 interactors
MINTiP00519
STRINGi9606.ENSP00000361423

Chemistry databases

BindingDBiP00519
ChEMBLiCHEMBL1862
DrugBankiDB08043 1-[4-(PYRIDIN-4-YLOXY)PHENYL]-3-[3-(TRIFLUOROMETHYL)PHENYL]UREA
DB00171 Adenosine triphosphate
DB06616 Bosutinib
DB01254 Dasatinib
DB00619 Imatinib
DB08231 MYRISTIC ACID
DB03878 N-[4-Methyl-3-[[4-(3-Pyridinyl)-2-Pyrimidinyl]Amino]Phenyl]-3-Pyridinecarboxamide
DB04868 Nilotinib
DB08901 Ponatinib
DB12323 Radotinib
DB08896 Regorafenib
DB05184 XL228
GuidetoPHARMACOLOGYi1923

Protein family/group databases

MoonDBiP00519 Predicted

PTM databases

iPTMnetiP00519
PhosphoSitePlusiP00519

Polymorphism and mutation databases

BioMutaiABL1
DMDMi85681908

Proteomic databases

EPDiP00519
jPOSTiP00519
MaxQBiP00519
PaxDbiP00519
PeptideAtlasiP00519
PRIDEiP00519
ProteomicsDBi51259
51260 [P00519-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
25
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318560; ENSP00000323315; ENSG00000097007 [P00519-1]
ENST00000372348; ENSP00000361423; ENSG00000097007 [P00519-2]
GeneIDi25
KEGGihsa:25
UCSCiuc004bzv.4 human [P00519-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
25
DisGeNETi25
EuPathDBiHostDB:ENSG00000097007.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ABL1
HGNCiHGNC:76 ABL1
HPAiCAB002686
HPA027251
HPA027280
HPA028409
MalaCardsiABL1
MIMi189980 gene
608232 phenotype
617602 phenotype
neXtProtiNX_P00519
OpenTargetsiENSG00000097007
Orphaneti521 Chronic myeloid leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia
PharmGKBiPA24413

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000153838
HOVERGENiHBG004162
InParanoidiP00519
KOiK06619
OMAiGAFRESG
OrthoDBi182823at2759
PhylomeDBiP00519
TreeFamiTF105081

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-375170 CDO in myogenesis
R-HSA-428890 Role of ABL in ROBO-SLIT signaling
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-69231 Cyclin D associated events in G1
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8940973 RUNX2 regulates osteoblast differentiation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP00519
SIGNORiP00519

Miscellaneous databases

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

More...
ChiTaRSi
ABL1 human
EvolutionaryTraceiP00519

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ABL_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
25
PMAP-CutDBiP00519

Protein Ontology

More...
PROi
PR:P00519

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000097007 Expressed in 229 organ(s), highest expression level in frontal pole
CleanExiHS_ABL1
ExpressionAtlasiP00519 baseline and differential
GenevisibleiP00519 HS

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_HUMAN
<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: P00519
Secondary accession number(s): A3KFJ3
, Q13869, Q13870, Q16133, Q17R61, Q45F09
<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: January 24, 2006
Last modified: January 16, 2019
This is version 253 of the entry and version 4 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
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