Abl1
entrez
11350
canonical
uniprot
P00520
canonical
ensembl
ENSMUSG00000026842
resolver
ensp
ENSMUSP00000028190
resolver
ensp
ENSMUSP00000075167
resolver
ensp
ENSMUSP00000286651
resolver
genesymbol
Abl1
resolver
genesymbol_syn
Abl
resolver
uniprot
P97896
resolver
uniprot
Q3SYK5
resolver
uniprot
Q61252
resolver
uniprot
Q61253
resolver
uniprot
Q61254
resolver
uniprot
Q61255
resolver
uniprot
Q61256
resolver
uniprot
Q61257
resolver
uniprot
Q61258
resolver
uniprot
Q61259
resolver
uniprot
Q61260
resolver
uniprot
Q61261
resolver
uniprot
Q6PCM5
resolver
uniprot
Q8C1X4
resolver
uniprot_entry
ABL1_MOUSE
resolver
uniprot_entry
Q3SYK5_MOUSE
resolver
uniprot_sec
P97896
resolver
uniprot_sec
Q61252
resolver
uniprot_sec
Q61253
resolver
uniprot_sec
Q61254
resolver
uniprot_sec
Q61255
resolver
uniprot_sec
Q61256
resolver
uniprot_sec
Q61257
resolver
uniprot_sec
Q61258
resolver
uniprot_sec
Q61259
resolver
uniprot_sec
Q61260
resolver
uniprot_sec
Q61261
resolver
uniprot_sec
Q6PCM5
resolver
uniprot_sec
Q8C1X4
resolver
activity_regulation
ACTIVITY REGULATION: 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, also inhibits the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec). {ECO:0000250, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12654251, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:20072125, ECO:0000269|PubMed:9109492}.
uniprot
proteins
amino_acid_sequence
MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKRGTRGGAGSMLQAPELPTKTRTCRRAAEQKDAPDTPELLHTKGLGESDALDSEPAVSPLLPRKERGPPDGSLNEDERLLPRDRKTNLFSALIKKKKKMAPTPPKRSSSFREMDGQPDRRGASEDDSRELCNGPPALTSDAAEPTKSPKASNGAGVPNGAFREPGNSGFRSPHMWKKSSTLTGSRLAAAEEESGMSSSKRFLRSCSASCMPHGARDTEWRSVTLPRDLPSAGKQFDSSTFGGHKSEKPALPRKRTSESRSEQVAKSTAMPPPRLVKKNEEAAEEGFKDTESSPGSSPPSLTPKLLRRQVTASPSSGLSHKEEATKGSASGMGTPATAEPAPPSNKVGLSKASSEEMRVRRHKHSSESPGRDKGRLAKLKPAPPPPPACTGKAGKPAQSPSQEAGEAGGPTKTKCTSLAMDAVNTDPTKAGPPGEGLRKPVPPSVPKPQSTAKPPGTPTSPVSTPSTAPAPSPLAGDQQPSSAAFIPLISTRVSLRKTRQPPERIASGTITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLESNLRELQICPATASSGPAATQDFSKLLSSVKEISDIVRR
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717' (By similarity). ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Regulates T-cell differentiation in a TBX21-dependent manner (PubMed:21690296). Positively regulates chemokine-mediated T-cell migration, polarization, and homing to lymph nodes and immune-challenged tissues, potentially via activation of NEDD9/HEF1 and RAP1 (PubMed:22810897). Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity (PubMed:21690296). {ECO:0000250|UniProtKB:P00519, ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11279131, ECO:0000269|PubMed:11350980, ECO:0000269|PubMed:12107171, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:19878872, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:7780740, ECO:0000269|PubMed:8194526, ECO:0000269|PubMed:9109492}.
uniprot
proteins
mass_dalton
122673
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="P->S: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 128; /note="Y->D: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 139; /note="Y->C: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 226; /note="Y->F: Minimal reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 229; /note="S->P: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 271; /note="K->M: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 315; /note="T->I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 393; /note="Y->F: Minimal reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 446; /note="S->A: No effect on basal activity, but abolishes ionizing radiation-induced activation."; /evidence="ECO:0000269|PubMed:9109492"; MUTAGEN 464; /note="C->Y: Loss of inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 465; /note="P->S: Loss of inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 497; /note="F->L: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 505; /note="E->K: Loss of inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 506; /note="V->L: Strongly reduced inhibition by GNF-2."; /evidence="ECO:0000269|PubMed:20072125"; MUTAGEN 1083; /note="L->A: Loss of nuclear export."; /evidence="ECO:0000269|PubMed:9636171
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation. {ECO:0000250}.; PTM: 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. {ECO:0000250, ECO:0000269|PubMed:10988075, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:1566087, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:2183353, ECO:0000269|PubMed:9109492}.; PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity). {ECO:0000250}.; PTM: Isoform IV is myristoylated on Gly-2. {ECO:0000269|PubMed:12654251}.
uniprot
proteins
protein_family
ABL subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10896159
uniprot
proteins
pubmed
10988075
uniprot
proteins
pubmed
11114745
uniprot
proteins
pubmed
11163214
uniprot
proteins
pubmed
11279004
uniprot
proteins
pubmed
11279131
uniprot
proteins
pubmed
11350980
uniprot
proteins
pubmed
12021275
uniprot
proteins
pubmed
12107171
uniprot
proteins
pubmed
12654251
uniprot
proteins
pubmed
12748290
uniprot
proteins
pubmed
12775773
uniprot
proteins
pubmed
14993293
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1566087
uniprot
proteins
pubmed
15686624
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17718712
uniprot
proteins
pubmed
19878872
uniprot
proteins
pubmed
19895503
uniprot
proteins
pubmed
19903482
uniprot
proteins
pubmed
20072125
uniprot
proteins
pubmed
2065352
uniprot
proteins
pubmed
2065353
uniprot
proteins
pubmed
20841568
uniprot
proteins
pubmed
21690296
uniprot
proteins
pubmed
2183353
uniprot
proteins
pubmed
22810897
uniprot
proteins
pubmed
3283651
uniprot
proteins
pubmed
3317402
uniprot
proteins
pubmed
6319018
uniprot
proteins
pubmed
7664083
uniprot
proteins
pubmed
7665185
uniprot
proteins
pubmed
7780740
uniprot
proteins
pubmed
8194526
uniprot
proteins
pubmed
9109492
uniprot
proteins
pubmed
9636171
uniprot
proteins
sequence_length
1123
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 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. {ECO:0000250}.
uniprot
proteins