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Protein

Tyrosine-protein kinase ABL1

Gene

Abl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks.11 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation3 Publications

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 (By similarity). Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage (By similarity). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei271ATPPROSITE-ProRule annotation1
Active sitei363Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi248 – 256ATPCurated9
Nucleotide bindingi316 – 322ATPCurated7

GO - Molecular functioni

  • actin filament binding Source: MGI
  • ATP binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • kinase activity Source: MGI
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • mitogen-activated protein kinase binding Source: MGI
  • non-membrane spanning protein tyrosine kinase activity Source: MGI
  • proline-rich region binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • protein domain specific binding Source: MGI
  • protein kinase activity Source: MGI
  • protein kinase C binding Source: MGI
  • protein tyrosine kinase activity Source: UniProtKB
  • SH3 domain binding Source: MGI
  • syntaxin binding Source: MGI

GO - Biological processi

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

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-375170. CDO in myogenesis.
R-MMU-428890. Role of Abl in Robo-Slit signaling.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:87859. Abl1.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Nucleus
  • Mitochondrion

  • Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins (By similarity). Localizes to mitochondria in response to oxidative stress.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112P → S: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi128Y → D: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi139Y → C: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi226Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi229S → P: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi271K → M: Loss of kinase activity. 1 Publication1
Mutagenesisi315T → I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi393Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication1
Mutagenesisi446S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. 1 Publication1
Mutagenesisi464C → Y: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi465P → S: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi497F → L: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi505E → K: Loss of inhibition by GNF-2. 1 Publication1
Mutagenesisi506V → L: Strongly reduced inhibition by GNF-2. 1 Publication1
Mutagenesisi1083L → A: Loss of nuclear export. 1

Keywords - Diseasei

Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL3099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000880512 – 1123Tyrosine-protein kinase ABL1Add BLAST1122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50PhosphoserineBy similarity1
Modified residuei70Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei115PhosphotyrosineBy similarity1
Modified residuei128PhosphotyrosineBy similarity1
Modified residuei139PhosphotyrosineBy similarity1
Modified residuei172PhosphotyrosineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei215PhosphotyrosineBy similarity1
Modified residuei226Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei229PhosphoserineBy similarity1
Modified residuei253PhosphotyrosineBy similarity1
Modified residuei257PhosphotyrosineBy similarity1
Modified residuei393Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases2 Publications1
Modified residuei413PhosphotyrosineBy similarity1
Modified residuei446Phosphoserine1 Publication1
Modified residuei547Phosphothreonine1 Publication1
Modified residuei559PhosphoserineBy similarity1
Modified residuei569Phosphoserine1 Publication1
Modified residuei618Phosphoserine; by PAK2By similarity1
Modified residuei619Phosphoserine; by PAK2By similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei658PhosphoserineBy similarity1
Modified residuei682PhosphoserineBy similarity1
Modified residuei710N6-acetyllysine; by EP300By similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei734PhosphothreonineBy similarity1
Modified residuei750PhosphothreonineBy similarity1
Modified residuei812PhosphothreonineBy similarity1
Modified residuei821PhosphothreonineBy similarity1
Modified residuei844PhosphothreonineBy similarity1
Modified residuei909PhosphoserineBy similarity1
Modified residuei970PhosphoserineBy similarity1

Post-translational modificationi

Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation.By similarity
Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity (By similarity). Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity (By similarity). DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation (By similarity). Phosphorylated by PDGFRB and PRKDC.By similarity7 Publications
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity).By similarity
Isoform IV is myristoylated on Gly-2.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00520.
PaxDbiP00520.
PeptideAtlasiP00520.
PRIDEiP00520.

PTM databases

iPTMnetiP00520.
PhosphoSitePlusiP00520.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSMUSG00000026842.
CleanExiMM_ABL1.
ExpressionAtlasiP00520. baseline and differential.
GenevisibleiP00520. MM.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP0-45EBI-8593082,EBI-8593095From a different organism.
CDKN1BP465272EBI-914519,EBI-519280From a different organism.
CdonQ32MD92EBI-914519,EBI-7017034
Dok1P974654EBI-914519,EBI-914917
EPHB2P28693-25EBI-914519,EBI-6725926From a different organism.
Nck1Q99M512EBI-914519,EBI-642202
Pstpip1P978145EBI-914519,EBI-7484574
Ptpn18P706022EBI-914519,EBI-7484661From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi197906. 20 interactors.
IntActiP00520. 22 interactors.
MINTiMINT-85127.
STRINGi10090.ENSMUSP00000075167.

Chemistry databases

BindingDBiP00520.

Structurei

Secondary structure

11123
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi65 – 70Combined sources6
Beta strandi76 – 79Combined sources4
Beta strandi87 – 93Combined sources7
Beta strandi97 – 103Combined sources7
Beta strandi108 – 112Combined sources5
Helixi113 – 115Combined sources3
Beta strandi116 – 121Combined sources6
Helixi122 – 124Combined sources3
Beta strandi128 – 131Combined sources4
Helixi134 – 140Combined sources7
Helixi141 – 143Combined sources3
Beta strandi148 – 153Combined sources6
Beta strandi155 – 157Combined sources3
Beta strandi161 – 167Combined sources7
Beta strandi170 – 175Combined sources6
Beta strandi184 – 187Combined sources4
Beta strandi192 – 194Combined sources3
Helixi195 – 202Combined sources8
Beta strandi209 – 211Combined sources3
Beta strandi226 – 228Combined sources3
Beta strandi230 – 233Combined sources4
Helixi239 – 241Combined sources3
Beta strandi242 – 248Combined sources7
Helixi249 – 251Combined sources3
Beta strandi255 – 261Combined sources7
Helixi262 – 264Combined sources3
Beta strandi266 – 273Combined sources8
Beta strandi275 – 278Combined sources4
Helixi280 – 292Combined sources13
Beta strandi301 – 305Combined sources5
Beta strandi307 – 316Combined sources10
Helixi323 – 329Combined sources7
Turni332 – 334Combined sources3
Helixi337 – 357Combined sources21
Beta strandi359 – 362Combined sources4
Helixi366 – 368Combined sources3
Beta strandi369 – 371Combined sources3
Helixi373 – 375Combined sources3
Beta strandi377 – 379Combined sources3
Helixi384 – 386Combined sources3
Beta strandi390 – 396Combined sources7
Beta strandi399 – 401Combined sources3
Helixi403 – 405Combined sources3
Helixi408 – 413Combined sources6
Helixi418 – 433Combined sources16
Beta strandi439 – 442Combined sources4
Helixi445 – 447Combined sources3
Helixi448 – 453Combined sources6
Helixi466 – 475Combined sources10
Helixi480 – 482Combined sources3
Helixi486 – 509Combined sources24

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00520.

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
Regioni863 – 961DNA-bindingAdd BLAST99
Regioni945 – 1123F-actin-bindingBy similarityAdd BLAST179

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi381 – 405Kinase activation loopAdd BLAST25
Motifi605 – 609Nuclear localization signal 1Sequence analysis5
Motifi708 – 714Nuclear localization signal 2Sequence analysis7
Motifi761 – 768Nuclear localization signal 3Sequence analysis8
Motifi1083 – 1093Nuclear export signalAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi18 – 22Poly-Ser5
Compositional biasi605 – 609Poly-Lys5
Compositional biasi804 – 1012Pro-richAdd BLAST209
Compositional biasi891 – 897Poly-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.
InParanoidiP00520.
KOiK06619.
OMAiGAFRESG.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform I (identifier: P00520-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS
60 70 80 90 100
KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC
110 120 130 140 150
EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL
160 170 180 190 200
VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH
210 220 230 240 250
HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT DITMKHKLGG
260 270 280 290 300
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
310 320 330 340 350
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA
360 370 380 390 400
MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK
410 420 430 440 450
FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE
460 470 480 490 500
LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES
510 520 530 540 550
SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE QKDAPDTPEL
560 570 580 590 600
LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
610 620 630 640 650
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS
660 670 680 690 700
DAAEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA
710 720 730 740 750
EEESGMSSSK RFLRSCSASC MPHGARDTEW RSVTLPRDLP SAGKQFDSST
760 770 780 790 800
FGGHKSEKPA LPRKRTSESR SEQVAKSTAM PPPRLVKKNE EAAEEGFKDT
810 820 830 840 850
ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS GMGTPATAEP
860 870 880 890 900
APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
910 920 930 940 950
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP
960 970 980 990 1000
VPPSVPKPQS TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS
1010 1020 1030 1040 1050
TRVSLRKTRQ PPERIASGTI TKGVVLDSTE ALCLAISRNS EQMASHSAVL
1060 1070 1080 1090 1100
EAGKNLYTFC VSYVDSIQQM RNKFAFREAI NKLESNLREL QICPATASSG
1110 1120
PAATQDFSKL LSSVKEISDI VRR
Length:1,123
Mass (Da):122,673
Last modified:February 15, 2005 - v3
Checksum:iBD48ADE8557AE95C
GO
Isoform II (identifier: P00520-2) [UniParc]FASTAAdd to basket

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

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

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

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

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184 – 187LYVS → VGDW in AAB60451 (PubMed:7665185).Curated4
Sequence conflicti184 – 187LYVS → VGDW in AAB60450 (PubMed:7665185).Curated4
Sequence conflicti782 – 786PPRLV → LPGWL in AAA88241 (PubMed:3317402).Curated5
Sequence conflicti987D → G in BAC41088 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0049591 – 26MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II. CuratedAdd BLAST26
Alternative sequenceiVSP_0049581 – 26MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III. CuratedAdd BLAST26
Alternative sequenceiVSP_0049601 – 26MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV. 1 PublicationAdd BLAST26

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi197906. 20 interactors.
IntActiP00520. 22 interactors.
MINTiMINT-85127.
STRINGi10090.ENSMUSP00000075167.

Chemistry databases

BindingDBiP00520.
ChEMBLiCHEMBL3099.

PTM databases

iPTMnetiP00520.
PhosphoSitePlusiP00520.

Proteomic databases

MaxQBiP00520.
PaxDbiP00520.
PeptideAtlasiP00520.
PRIDEiP00520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi25.
MGIiMGI:87859. Abl1.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP00520.
KOiK06619.
OMAiGAFRESG.
TreeFamiTF105081.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-375170. CDO in myogenesis.
R-MMU-428890. Role of Abl in Robo-Slit signaling.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP00520.
PROiP00520.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026842.
CleanExiMM_ABL1.
ExpressionAtlasiP00520. baseline and differential.
GenevisibleiP00520. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P00520
Secondary accession number(s): P97896
, Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: November 30, 2016
This is version 216 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.