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ABL2

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Protein-coding gene in the species Homo sapiens

ABL2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2ECD, 2KK1, 2XYN, 3GVU, 3HMI, 3ULR, 4EIH

Identifiers
AliasesABL2, ABLL, ARG, ABL proto-oncogene 2, non-receptor tyrosine kinase
External IDsOMIM: 164690; MGI: 87860; HomoloGene: 5278; GeneCards: ABL2; OMA:ABL2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for ABL2Genomic location for ABL2
Band1q25.2Start179,099,330 bp
End179,229,684 bp
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)
Chromosome 1 (mouse)Genomic location for ABL2Genomic location for ABL2
Band1 G3|1 67.71 cMStart156,386,356 bp
End156,477,138 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • tendon of biceps brachii

  • buccal mucosa cell

  • sural nerve

  • visceral pleura

  • parietal pleura

  • middle temporal gyrus

  • Brodmann area 23

  • tibia

  • secondary oocyte

  • cerebellar vermis
Top expressed in
  • Rostral migratory stream

  • secondary oocyte

  • primary oocyte

  • otolith organ

  • zygote

  • utricle

  • endothelial cell of lymphatic vessel

  • hand

  • lumbar subsegment of spinal cord

  • foot
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

27

11352

Ensembl

ENSG00000143322

ENSMUSG00000026596

UniProt

P42684

Q4JIM5

RefSeq (mRNA)
NM_001136000
NM_001136001
NM_001168236
NM_001168237
NM_001168238

NM_001168239
NM_005158
NM_007314

NM_001136104
NM_009595

RefSeq (protein)
NP_001129472
NP_001129473
NP_001161708
NP_001161709
NP_001161710

NP_001161711
NP_005149
NP_009298

n/a

Location (UCSC)Chr 1: 179.1 – 179.23 MbChr 1: 156.39 – 156.48 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

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

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 expression of ABL2 gene is higher in KRAS mutant non-small cell lung cancer. The ABL2 gene product is expressed as two variants bearing different amino termini, both approximately 12-kb in length.

Interactions

ABL2 has been shown to interact with three proteins: Abl gene, catalase, and SORBS2. The protein Abl gene is also known as abelson murine leukemia viral oncogene homolog 1 and is a protein that is encoded by the human ABL1 gene. Catalase is a common enzyme that catalyzes the decomposition of hydrogen peroxide to water and oxygen. SORBS2 is also known as Sorbin and SH3 domain-containing protein 2 and is a protein encoded by the SORBS2 gene in humans.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000143322Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000026596Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Kruh GD, King CR, Kraus MH, Popescu NC, Amsbaugh SC, McBride WO, Aaronson SA (Jan 1987). "A novel human gene closely related to the abl proto-oncogene". Science. 234 (4783): 1545–8. doi:10.1126/science.3787260. PMID 3787260.
  6. ^ "Entrez Gene: ABL2 v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene)".
  7. Nagy Á, Pongor LS, Szabó A, Santarpia M, Győrffy B (2017-02-15). "KRAS driven expression signature has prognostic power superior to mutation status in non-small cell lung cancer". International Journal of Cancer. 140 (4): 930–937. doi:10.1002/ijc.30509. ISSN 1097-0215. PMC 5299512. PMID 27859136.
  8. Cao C, Leng Y, Li C, Kufe D (April 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". J. Biol. Chem. 278 (15): 12961–7. doi:10.1074/jbc.M300058200. PMID 12569093.
  9. Cao C, Leng Y, Kufe D (August 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". J. Biol. Chem. 278 (32): 29667–75. doi:10.1074/jbc.M301292200. PMID 12777400.
  10. ^ Wang B, Golemis EA, Kruh GD (July 1997). "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". J. Biol. Chem. 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. hdl:20.500.12613/9174. PMID 9211900.
  11. Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D, Gewirtz AM, Calabretta B (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science. 253 (5019): 562–5. Bibcode:1991Sci...253..562S. doi:10.1126/science.1857987. PMID 1857987.
  12. Chelikani P, Fita I, Loewen PC (January 2004). "Diversity of structures and properties among catalases". Cell. Mol. Life Sci. 61 (2): 192–208. doi:10.1007/s00018-003-3206-5. hdl:10261/111097. PMID 14745498. S2CID 4411482.
  13. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Apr 1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.

Further reading

External links

PDB gallery
  • 1ab2: THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL 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 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 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 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 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. 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 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 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 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 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 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 2g1t: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
  • 2g2f: 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 2g2h: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
  • 2g2i: 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 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 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) 2hyy: Human Abl kinase domain in complex with imatinib (STI571, Glivec)
  • 2hz0: Abl kinase domain in complex with NVP-AEG082 2hz0: Abl kinase domain in complex with NVP-AEG082
  • 2hz4: Abl kinase domain unligated and in complex with tetrahydrostaurosporine 2hz4: Abl kinase domain unligated and in complex with tetrahydrostaurosporine
  • 2hzi: Abl kinase domain in complex with PD180970 2hzi: Abl kinase domain in complex with PD180970
  • 2hzn: Abl kinase domain in complex with NVP-AFG210 2hzn: Abl kinase domain in complex with NVP-AFG210
Protein kinases: tyrosine kinases (EC 2.7.10)
Receptor tyrosine kinases (EC 2.7.10.1)
Growth factor receptors
EGF receptor family
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PTK7 receptor family
RYK receptor family
MuSK receptor family
ROS receptor family
AATYK receptor family
AXL receptor family
RET receptor family
uncategorised
Non-receptor tyrosine kinases (EC 2.7.10.2)
ABL family
ACK family
CSK family
FAK family
FES family
FRK family
JAK family
SRC-A family
SRC-B family
TEC family
SYK family
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