ABL2

V-abl Abelson murine leukemia viral oncogene homolog 2
PDB rendering based on 1ab2.
Available structures PDB 2ECD, 2KK1, 2XYN, 3GVU, 3HMI
Identifiers
Symbols	ABL2; ABLL; ARG; FLJ22224; FLJ31718; FLJ41441
External IDs	OMIM: 164690 MGI: 87860 HomoloGene: 5278 GeneCards: ABL2 Gene
EC number	2.7.10.2
Gene Ontology Molecular function • nucleotide binding • magnesium ion binding • protein kinase activity • protein tyrosine kinase activity • non-membrane spanning protein tyrosine kinase activity • protein binding • ATP binding • manganese ion binding Cellular component • cytoplasm • cytosol • cytoskeleton Biological process • protein modification process • protein phosphorylation • cell adhesion • signal transduction • axon guidance • peptidyl-tyrosine phosphorylation • positive regulation of oxidoreductase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	27	11352
Ensembl	ENSG00000143322	ENSMUSG00000026596
UniProt	P42684	Q61055
RefSeq (mRNA)	NM_001136000.2	NM_009595
RefSeq (protein)	NP_001129472.1	NP_033725
Location (UCSC)	Chr 1: 179.07 – 179.2 Mb	Chr 1: 158.49 – 158.57 Mb
PubMed search	[1]	[2]

Tyrosine-protein kinase ABL2 also known as Abelson-related gene (Arg) is an enzyme that in humans is encoded by the ABL2 gene.^[1][2]

Function

ABL2 is a cytoplasmic tyrosine kinase which is closely related to but distinct from ABL1. The similarity of the proteins includes the tyrosine kinase domains and extends amino-terminal to include the SH2 and SH3 domains. ABL2 is expressed in both normal and tumor cells. The ABL2 gene product is expressed as two variants bearing different amino termini, both approximately 12-kb in length.^[2]

Interactions

ABL2 has been shown to interact with:

• Abl gene^[3]
• catalase,^[4] and
• SORBS2.^[5]

References

Further reading

External links

• MeSH Genes,+abl
• MeSH Abelson+Leukemia+Virus
• ABL2 Info with links in the Cell Migration Gateway

v d e PDB gallery 1ab2: THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL   1abo: CRYSTAL STRUCTURE OF THE COMPLEX OF THE ABL TYROSINE KINASE SH3 DOMAIN WITH 3BP-1 SYNTHETIC PEPTIDE   1abq: CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN   1bbz: CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS   1fpu: CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR   1iep: CRYSTAL STRUCTURE OF THE C-ABL KINASE DOMAIN IN COMPLEX WITH STI-571.   1ju5: Ternary complex of an Crk SH2 domain, Crk-derived phophopeptide, and Abl SH3 domain by NMR spectroscopy   1m52: Crystal Structure of the c-Abl Kinase domain in complex with PD173955   1opj: Structural basis for the auto-inhibition of c-Abl tyrosine kinase   2e2b: Crystal structure of the c-Abl kinase domain in complex with INNO-406   2f4j: Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680   2g1t: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain   2g2f: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain   2g2h: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain   2g2i: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain   2gqg: X-ray Crystal Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain   2hiw: Crystal Structure of Inactive Conformation Abl Kinase Catalytic Domain Complexed with Type II Inhibitor   2hyy: Human Abl kinase domain in complex with imatinib (STI571, Glivec)   2hz0: Abl kinase domain in complex with NVP-AEG082   2hz4: Abl kinase domain unligated and in complex with tetrahydrostaurosporine   2hzi: Abl kinase domain in complex with PD180970   2hzn: Abl kinase domain in complex with NVP-AFG210

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