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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-Experimental evidence at protein leveli

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. 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, ABI1.22 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Cofactori

Enzyme 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). 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.By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei271ATP1
Active sitei363Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi248 – 256ATP9
Nucleotide bindingi316 – 322ATP7

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: BHF-UCL
  • nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • proline-rich region binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein kinase activity Source: MGI
  • protein kinase C binding Source: ParkinsonsUK-UCL
  • protein tyrosine kinase activity Source: UniProtKB
  • SH3 domain binding Source: UniProtKB
  • syntaxin binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament branching Source: Ensembl
  • activated T cell proliferation Source: Ensembl
  • activation of protein kinase C activity Source: ParkinsonsUK-UCL
  • alpha-beta T cell differentiation Source: Ensembl
  • autophagy Source: UniProtKB-KW
  • B-1 B cell homeostasis Source: Ensembl
  • B cell proliferation involved in immune response Source: Ensembl
  • B cell receptor signaling pathway Source: Ensembl
  • Bergmann glial cell differentiation Source: Ensembl
  • cell cycle arrest Source: ParkinsonsUK-UCL
  • cellular protein modification process Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to dopamine Source: ParkinsonsUK-UCL
  • cellular response to hydrogen peroxide Source: ParkinsonsUK-UCL
  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to oxidative stress Source: ParkinsonsUK-UCL
  • cerebellum morphogenesis Source: Ensembl
  • collateral sprouting Source: Ensembl
  • DNA damage induced protein phosphorylation Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: Ensembl
  • establishment of protein localization Source: UniProtKB
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • innate immune response Source: GO_Central
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  • microspike assembly Source: Ensembl
  • mismatch repair Source: ProtInc
  • mitochondrial depolarization Source: ParkinsonsUK-UCL
  • mitotic nuclear division Source: ParkinsonsUK-UCL
  • negative regulation of BMP signaling pathway Source: Ensembl
  • negative regulation of cell-cell adhesion Source: Ensembl
  • negative regulation of cellular senescence Source: Ensembl
  • negative regulation of endothelial cell apoptotic process Source: Ensembl
  • negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • negative regulation of mitotic cell cycle Source: Ensembl
  • negative regulation of phospholipase C activity Source: MGI
  • negative regulation of protein serine/threonine kinase activity Source: BHF-UCL
  • negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  • neuromuscular process controlling balance Source: Ensembl
  • peptidyl-tyrosine autophosphorylation Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of actin filament binding Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of interferon-gamma secretion Source: Ensembl
  • positive regulation of interleukin-2 secretion Source: Ensembl
  • positive regulation of microtubule binding Source: UniProtKB
  • positive regulation of mitotic cell cycle Source: Ensembl
  • positive regulation of muscle cell differentiation Source: Reactome
  • positive regulation of neuron death Source: Ensembl
  • positive regulation of osteoblast proliferation Source: Ensembl
  • positive regulation of oxidoreductase activity Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  • positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
  • protein autophosphorylation Source: ParkinsonsUK-UCL
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of actin cytoskeleton reorganization Source: UniProtKB
  • regulation of autophagy Source: UniProtKB
  • regulation of axon extension Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell proliferation Source: GO_Central
  • regulation of endocytosis Source: UniProtKB
  • regulation of extracellular matrix organization Source: Ensembl
  • regulation of microtubule polymerization Source: UniProtKB
  • regulation of response to DNA damage stimulus Source: UniProtKB
  • regulation of transcription, DNA-templated Source: ProtInc
  • response to oxidative stress Source: MGI
  • signal transduction in response to DNA damage Source: UniProtKB
  • spleen development Source: Ensembl
  • substrate adhesion-dependent cell spreading Source: Ensembl
  • thymus development Source: Ensembl
  • transitional one stage B cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Autophagy, Cell adhesion, DNA damage, DNA repair, Endocytosis

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01874-MONOMER.
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-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP00519.
SIGNORiP00519.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase ABL1 (EC:2.7.10.2)
Alternative name(s):
Abelson murine leukemia viral oncogene homolog 1
Abelson tyrosine-protein kinase 1
Proto-oncogene c-Abl
p150
Gene namesi
Name:ABL1
Synonyms:ABL, JTK7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:76. ABL1.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Nucleus
  • Mitochondrion By similarity

  • Note: Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress (By similarity).By similarity
Isoform IB :

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell leading edge Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • mitochondrion Source: ParkinsonsUK-UCL
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleolus Source: MGI
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

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).

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Sitei26 – 27Breakpoint for translocation to form BCR-ABL oncogene2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi25.
MalaCardsiABL1.
MIMi608232. phenotype.
OpenTargetsiENSG00000097007.
Orphaneti521. Chronic myeloid leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA24413.

Chemistry databases

ChEMBLiCHEMBL1862.
DrugBankiDB00171. Adenosine triphosphate.
DB06616. Bosutinib.
DB01254. Dasatinib.
DB00619. Imatinib.
DB04868. Nilotinib.
DB08901. Ponatinib.
DB08896. Regorafenib.
GuidetoPHARMACOLOGYi1923.

Polymorphism and mutation databases

BioMutaiABL1.
DMDMi85681908.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000880502 – 1130Tyrosine-protein kinase ABL1Add BLAST1129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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)
Lipidationi2N-myristoyl glycine1

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

EPDiP00519.
MaxQBiP00519.
PaxDbiP00519.
PeptideAtlasiP00519.
PRIDEiP00519.

PTM databases

iPTMnetiP00519.
PhosphoSitePlusiP00519.

Miscellaneous databases

PMAP-CutDBP00519.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000097007.
CleanExiHS_ABL1.
ExpressionAtlasiP00519. baseline and differential.
GenevisibleiP00519. HS.

Organism-specific databases

HPAiCAB002686.
HPA027251.
HPA027280.
HPA028409.

Interactioni

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.By similarity23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP011EBI-375543,EBI-375446
ABI2Q9NYB92EBI-375543,EBI-743598
ARP102752EBI-375543,EBI-608057
CDONQ4KMG02EBI-375543,EBI-7016840
CdonO351584EBI-375543,EBI-7016767From a different organism.
CRKP461082EBI-375543,EBI-886
CRKLP461092EBI-375543,EBI-910
CTNNB1P352222EBI-375543,EBI-491549
EGFRP005332EBI-375543,EBI-297353
ERBB2P046262EBI-375543,EBI-641062
FLNCQ143152EBI-375543,EBI-489954
ITGB2P051074EBI-375543,EBI-300173
KITP107212EBI-375543,EBI-1379503
LRRK1Q38SD23EBI-375543,EBI-1050422
MAP4K1Q929183EBI-375543,EBI-881
MAVSQ7Z4346EBI-375543,EBI-995373
MSH5O4319610EBI-375543,EBI-6092730
MUC1P159418EBI-375543,EBI-2804728
NCK1P163332EBI-375543,EBI-389883
PRICKLE3O439002EBI-375543,EBI-1751761
RAPGEF1Q139054EBI-375543,EBI-976876
RIMS1Q86UR52EBI-375543,EBI-1043236
RIN1Q136714EBI-375543,EBI-366017
SFNP319472EBI-375543,EBI-476295
SHBQ154645EBI-375543,EBI-4402156
SLC22A3O757512EBI-375543,EBI-1752674
SNCAP378406EBI-5278159,EBI-985879
SORBS1Q9BX662EBI-375543,EBI-433642
SORBS3O60504-25EBI-375543,EBI-1222956
SOS2Q078902EBI-375543,EBI-298181
SRCP129312EBI-375543,EBI-621482
TLN2Q9Y4G63EBI-375543,EBI-1220811
TOP1P113877EBI-375543,EBI-876302
VAV1P154985EBI-375543,EBI-625518
YWHAZP631043EBI-375543,EBI-347088

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: BHF-UCL
  • proline-rich region binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein kinase C binding Source: ParkinsonsUK-UCL
  • SH3 domain binding Source: UniProtKB
  • syntaxin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106543. 185 interactors.
DIPiDIP-1042N.
IntActiP00519. 223 interactors.
MINTiMINT-7236141.
STRINGi9606.ENSP00000361423.

Chemistry databases

BindingDBiP00519.

Structurei

Secondary structure

11130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi49 – 53Combined sources5
Helixi58 – 60Combined sources3
Beta strandi65 – 70Combined sources6
Beta strandi76 – 79Combined sources4
Beta strandi87 – 93Combined sources7
Beta strandi97 – 104Combined sources8
Beta strandi107 – 112Combined sources6
Helixi113 – 115Combined sources3
Beta strandi116 – 118Combined sources3
Helixi122 – 124Combined sources3
Beta strandi128 – 131Combined sources4
Helixi134 – 140Combined sources7
Turni141 – 143Combined sources3
Beta strandi148 – 153Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi161 – 167Combined sources7
Beta strandi170 – 175Combined sources6
Beta strandi177 – 179Combined sources3
Turni180 – 182Combined sources3
Beta strandi184 – 187Combined sources4
Beta strandi190 – 194Combined sources5
Helixi195 – 202Combined sources8
Beta strandi209 – 211Combined sources3
Beta strandi226 – 228Combined sources3
Beta strandi229 – 231Combined sources3
Turni233 – 235Combined sources3
Helixi239 – 241Combined sources3
Beta strandi242 – 247Combined sources6
Helixi248 – 251Combined sources4
Beta strandi254 – 261Combined sources8
Helixi262 – 264Combined sources3
Beta strandi266 – 271Combined sources6
Turni275 – 277Combined sources3
Helixi280 – 290Combined sources11
Beta strandi301 – 305Combined sources5
Beta strandi307 – 310Combined sources4
Beta strandi312 – 316Combined sources5
Beta strandi319 – 322Combined sources4
Helixi323 – 329Combined sources7
Turni332 – 334Combined sources3
Helixi337 – 356Combined sources20
Beta strandi359 – 361Combined sources3
Helixi366 – 368Combined sources3
Beta strandi369 – 371Combined sources3
Helixi373 – 375Combined sources3
Beta strandi377 – 379Combined sources3
Helixi381 – 383Combined sources3
Helixi384 – 387Combined sources4
Helixi390 – 392Combined sources3
Beta strandi393 – 396Combined sources4
Beta strandi399 – 401Combined sources3
Helixi403 – 405Combined sources3
Helixi408 – 413Combined sources6
Helixi418 – 433Combined sources16
Helixi445 – 447Combined sources3
Helixi448 – 453Combined sources6
Helixi466 – 475Combined sources10
Helixi480 – 482Combined sources3
Helixi486 – 496Combined sources11
Beta strandi498 – 500Combined sources3
Helixi503 – 506Combined sources4
Turni510 – 512Combined sources3
Helixi1029 – 1045Combined sources17
Turni1046 – 1048Combined sources3
Helixi1053 – 1070Combined sources18
Helixi1071 – 1073Combined sources3
Helixi1080 – 1097Combined sources18
Beta strandi1101 – 1104Combined sources4
Beta strandi1106 – 1108Combined sources3
Helixi1115 – 1128Combined sources14

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[»]
ProteinModelPortaliP00519.
SMRiP00519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 121SH3PROSITE-ProRule annotationAdd BLAST61
Domaini127 – 217SH2PROSITE-ProRule annotationAdd BLAST91
Domaini242 – 493Protein kinasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 60CAPAdd BLAST59
Regioni869 – 968DNA-bindingBy similarityAdd BLAST100
Regioni953 – 1130F-actin-bindingAdd BLAST178

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Compositional biasi18 – 22Poly-Ser5
Compositional biasi605 – 609Poly-Lys5
Compositional biasi782 – 1019Pro-richAdd BLAST238
Compositional biasi897 – 903Poly-Pro7

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP00519.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG091G0D46.
PhylomeDBiP00519.
TreeFamiTF105081.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033221. ABL1.
IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF88. PTHR24418:SF88. 1 hit.
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 → P.1 PublicationCorresponds to variant rs1064152dbSNPEnsembl.1
Natural variantiVAR_032677166R → K in a melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_051693247K → R.Corresponds to variant rs34549764dbSNPEnsembl.1
Natural variantiVAR_025043706G → V.2 PublicationsCorresponds to variant rs34634745dbSNPEnsembl.1
Natural variantiVAR_032678810P → L.1 PublicationCorresponds to variant rs2229071dbSNPEnsembl.1
Natural variantiVAR_025044852T → P.1 Publication1
Natural variantiVAR_025045900P → S.1 PublicationCorresponds to variant rs35266696dbSNPEnsembl.1
Natural variantiVAR_051694968S → P.Corresponds to variant rs1064165dbSNPEnsembl.1
Natural variantiVAR_025046972S → L.2 PublicationsCorresponds to variant rs2229067dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0049571 – 26MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKKESSRHGGPHCN VFVEH in isoform IB. 1 PublicationAdd BLAST26

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, AL161733 Genomic DNA. Translation: CAM45752.1.
AL161733 Genomic DNA. Translation: CAM45754.1.
AL161733, AL359092 Genomic DNA. Translation: CAM45756.1.
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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

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

Abl entry

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, AL161733 Genomic DNA. Translation: CAM45752.1.
AL161733 Genomic DNA. Translation: CAM45754.1.
AL161733, AL359092 Genomic DNA. Translation: CAM45756.1.
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[»]
ProteinModelPortaliP00519.
SMRiP00519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106543. 185 interactors.
DIPiDIP-1042N.
IntActiP00519. 223 interactors.
MINTiMINT-7236141.
STRINGi9606.ENSP00000361423.

Chemistry databases

BindingDBiP00519.
ChEMBLiCHEMBL1862.
DrugBankiDB00171. Adenosine triphosphate.
DB06616. Bosutinib.
DB01254. Dasatinib.
DB00619. Imatinib.
DB04868. Nilotinib.
DB08901. Ponatinib.
DB08896. Regorafenib.
GuidetoPHARMACOLOGYi1923.

PTM databases

iPTMnetiP00519.
PhosphoSitePlusiP00519.

Polymorphism and mutation databases

BioMutaiABL1.
DMDMi85681908.

Proteomic databases

EPDiP00519.
MaxQBiP00519.
PaxDbiP00519.
PeptideAtlasiP00519.
PRIDEiP00519.

Protocols and materials databases

DNASUi25.
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

CTDi25.
DisGeNETi25.
GeneCardsiABL1.
HGNCiHGNC:76. ABL1.
HPAiCAB002686.
HPA027251.
HPA027280.
HPA028409.
MalaCardsiABL1.
MIMi189980. gene.
608232. phenotype.
neXtProtiNX_P00519.
OpenTargetsiENSG00000097007.
Orphaneti521. Chronic myeloid leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA24413.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP00519.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG091G0D46.
PhylomeDBiP00519.
TreeFamiTF105081.

Enzyme and pathway databases

BioCyciZFISH:HS01874-MONOMER.
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-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP00519.
SIGNORiP00519.

Miscellaneous databases

ChiTaRSiABL1. human.
EvolutionaryTraceiP00519.
GeneWikiiABL_(gene).
GenomeRNAii25.
PMAP-CutDBP00519.
PROiP00519.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000097007.
CleanExiHS_ABL1.
ExpressionAtlasiP00519. baseline and differential.
GenevisibleiP00519. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR033221. ABL1.
IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF88. PTHR24418:SF88. 1 hit.
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiABL1_HUMAN
AccessioniPrimary (citable) accession number: P00519
Secondary accession number(s): A3KFJ3
, Q13869, Q13870, Q16133, Q17R61, Q45F09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 231 of the entry and version 4 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.