ABL2 - Abelson tyrosine-protein kinase 2 - human protein (Function)
 
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ABL2 »  Abelson tyrosine-protein kinase 2   [ EC 2.7.10.2 ]
 
Protein also known as:  Abelson murine leukemia viral oncogene homolog 2.
Gene name:  ABL2
Entry whose protein(s) existence is based on evidence at protein level
extend overview
1 83 9
GENE REF ISO

Function

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Overview 
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 acts also 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.  
5
  • CuratedUniProtKB
GO molecular function 
Actin filament bindingdefinition[GO:0051015]  
1
  • TASUniProtKB
Actin monomer bindingdefinition[GO:0003785]  
1
  • TASUniProtKB
ATP bindingdefinition[GO:0005524]  
  • IEAUniProtKB KW
Magnesium ion bindingdefinition[GO:0000287]  
1
  • IDAUniProtKB
Manganese ion bindingdefinition[GO:0030145]  
1
  • IDAUniProtKB
Non-membrane spanning protein tyrosine kinase activitydefinition[GO:0004715]  
1
  • TASUniProtKB
Protein bindingdefinition[GO:0005515]  
6
  • IPIIntAct
  • IPIBHF-UCL
Protein kinase activitydefinition[GO:0004672]  
1
  • TASPINC
Protein tyrosine kinase activitydefinition[GO:0004713]  
1
  • IDAUniProtKB
GO biological process 
Actin filament bundle assemblydefinition[GO:0051017] silver  
  • IEAOrtholog Compara
Cell adhesiondefinition[GO:0007155]  
  • IEAUniProtKB KW
Cellular protein modification processdefinition[GO:0006464]  
1
  • TASPINC
Cellular response to retinoic aciddefinition[GO:0071300]  
1
  • IMPBHF-UCL
Peptidyl-tyrosine phosphorylationdefinition[GO:0018108]  
1
  • IDAUniProtKB
Positive regulation of neuron projection developmentdefinition[GO:0010976]  
1
  • IMPBHF-UCL
Positive regulation of oxidoreductase activitydefinition[GO:0051353]  
1
  • IDABHF-UCL
Regulation of actin cytoskeleton reorganizationdefinition[GO:2000249]  
1
  • TASUniProtKB
Regulation of autophagydefinition[GO:0010506]  
1
  • TASUniProtKB
Regulation of cell adhesiondefinition[GO:0030155]  
1
  • TASUniProtKB
Regulation of cell motilitydefinition[GO:2000145]  
1
  • TASUniProtKB
Regulation of endocytosisdefinition[GO:0030100]  
1
  • TASUniProtKB
Signal transductiondefinition[GO:0007165]  
1
  • TASPINC
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reaction
EC 2.7.10.2: ATP + a [protein]-L-tyrosine ADP + a [protein]-L-tyrosine phosphate.  
  • CuratedUniProtKB
It requires the following cofactor
Magnesium or manganese.  
  • CuratedUniProtKB
It is regulated in the following manner
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).  
2
  • CuratedUniProtKB
 
More information is available from:
Pathways 
According to KEGG, this protein belongs to the following pathways:
ErbB signaling pathway  hsa04012+27  
Viral myocarditis  hsa05416+27  
According to Reactome, this protein belongs to the following pathway:
Developmental Biology  REACT_111045  
 

Keywords

Biological process 
Cell adhesion  definition   [KW-0130]
Molecular function 
Kinase  definition   [KW-0418]
Transferase  definition   [KW-0808]
Tyrosine-protein kinase  definition   [KW-0829]
Technical term 
Reference proteome  definition   [KW-1185]
 

Further external links

Other
GeneWiki: ABL2
GenomeRNAi: 27
PRO: PR:P42684
Chemistry
GuidetoPHARMACOLOGY: 1924