ABL2
entrez
27
canonical
uniprot
P42684
canonical
ensembl
ENSG00000143322
resolver
ensp
ENSP00000339209
resolver
ensp
ENSP00000356595
resolver
ensp
ENSP00000423413
resolver
ensp
ENSP00000423578
resolver
ensp
ENSP00000424697
resolver
ensp
ENSP00000426831
resolver
ensp
ENSP00000427562
resolver
genesymbol
ABL2
resolver
genesymbol_syn
ABLL
resolver
genesymbol_syn
ARG
resolver
hgnc
HGNC:77
resolver
uniprot
A0M8X0
resolver
uniprot
B7UEF2
resolver
uniprot
B7UEF3
resolver
uniprot
B7UEF4
resolver
uniprot
B7UEF5
resolver
uniprot
Q5T0X6
resolver
uniprot
Q5W0C5
resolver
uniprot
Q6NZY6
resolver
uniprot
Q7Z301
resolver
uniprot_entry
ABL2_HUMAN
resolver
uniprot_sec
A0M8X0
resolver
uniprot_sec
B7UEF2
resolver
uniprot_sec
B7UEF3
resolver
uniprot_sec
B7UEF4
resolver
uniprot_sec
B7UEF5
resolver
uniprot_sec
Q5T0X6
resolver
uniprot_sec
Q5W0C5
resolver
uniprot_sec
Q6NZY6
resolver
uniprot_sec
Q7Z301
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. Activated by RIN1 binding to the SH2 and SH3 domains. Inhibited by imatinib mesylate (Gleevec) which is used for the treatment of chronic myeloid leukemia (CML). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits the tyrosine kinase activity (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQHDHFASCVEDGFEGDKTGGSSPEALHRPYGCDVEPQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTADGKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECNREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRAASSSSVVPYLPRLPILPSKTRTLKKQVENKENIEGAQDATENSASSLAPGFIRGAQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSSVASLQHADGFSFTPAQQEANLVPPKCYGGSFAQRNLCNDDGGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEESAAPSRERPKAKLLPRGATALPLRTPSGDLAITEKDPPGVGVAGVAAAPKGKEKNGGARLGMAGVPEDGEQPGWPSPAKAAPVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSICSDPTEEPTALTAGQSTSETQEGGKKAALGAVPISGKAGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSLQELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 also acts as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 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. 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 (By similarity). {ECO:0000250|UniProtKB:Q4JIM5, ECO:0000269|PubMed:15735735, ECO:0000269|PubMed:15886098, ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:17306540, ECO:0000269|PubMed:18945674}.
uniprot
proteins
mass_dalton
128343
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress. Phosphorylated by PDGFRB (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation. {ECO:0000269|PubMed:15735735}.
uniprot
proteins
protein_family
ABL subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
12748290
uniprot
proteins
pubmed
12775773
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14729179
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15735735
uniprot
proteins
pubmed
15886098
uniprot
proteins
pubmed
16678104
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17306540
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18182299
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18810762
uniprot
proteins
pubmed
18945674
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19381274
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20841568
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21417343
uniprot
proteins
pubmed
2198571
uniprot
proteins
pubmed
22297987
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
3787260
uniprot
proteins
sequence_length
1182
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q4JIM5}.
uniprot
proteins