Q4JIM5
uniprot
Q4JIM5
canonical
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 (By similarity). Inhibited by imatinib mesylate (Gleevec). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits the tyrosine kinase activity. {ECO:0000250, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.
uniprot
proteins
amino_acid_sequence
MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTADAGFNVFTQHDHFASCVEDGFEGDKTGGSSPEVLHRPFGCDAESQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTTDSKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTFKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECSREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRTASSSSVVPYLPRLPLLPSKTRTLRKQGENKENLDGGLDAAESLASSSAPAGFIRSTQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSPVASLQNADGFSVAPSQQEPNLVPAKCYGGSFAQRNLCADDDSGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEEGAAPARERPKAKLLPRGATALPLRAPDPAITESDSPGVGVAGVAAAPKGKERNGGTRLGVAGVPEDGEQLGWSSPAKAVAVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSTCSDPEEEPTAPPAGQHTPETQEGGKKAAPGPVPSSGKPGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSAITEPVPNSQLVDTGHQLLDYCSGYVDSIPQTRNKFAFREAVSKLELSLQELQVSSTAAGVPGTNPVLNNLLSCVQEISDVVQR
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, receptor endocytosis, autophagy, DNA damage response and apoptosis. 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 or DOK1. Required for adhesion-dependent phosphorylation of ARHGAP35 which 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. 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 (PubMed:22810897). {ECO:0000269|PubMed:11279004, ECO:0000269|PubMed:11752434, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293, ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:17892306, ECO:0000269|PubMed:22810897, ECO:0000269|PubMed:9883720}.
uniprot
proteins
mass_dalton
128196
uniprot
proteins
mutagenesis
MUTAGEN 272; /note="Y->F: Minimal reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 317; /note="K->M: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 439; /note="Y->F: Partial reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 568; /note="Y->F: No reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290"; MUTAGEN 684; /note="Y->F: Minimal reduction in ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:12748290
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress (By similarity). Phosphorylated by PDGFRB. {ECO:0000250, ECO:0000269|PubMed:12748290, ECO:0000269|PubMed:14993293}.; PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
ABL subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11279004
uniprot
proteins
pubmed
11752434
uniprot
proteins
pubmed
12748290
uniprot
proteins
pubmed
12775773
uniprot
proteins
pubmed
14729179
uniprot
proteins
pubmed
14993293
uniprot
proteins
pubmed
16971514
uniprot
proteins
pubmed
17892306
uniprot
proteins
pubmed
18182299
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20841568
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22810897
uniprot
proteins
pubmed
9883720
uniprot
proteins
sequence_length
1182
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11752434}.
uniprot
proteins