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AIMP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4DPG, 4YCU, 4YCW, 5A34, 5A1N, 5A5H
Identifiers
Aliases	AIMP2, JTV-1, JTV1, P38, PRO0992, Multisynthetase complex auxiliary component p38, aminoacyl tRNA synthetase complex interacting multifunctional protein 2, HLD17
External IDs	OMIM: 600859; MGI: 2385237; HomoloGene: 4594; GeneCards: AIMP2; OMA:AIMP2 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7p22.1 Start 6,009,255 bp End 6,023,834 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 G2 Start 143,839,522 bp End 143,846,665 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte tibialis anterior muscle vastus lateralis muscle deltoid muscle body of tongue muscle of arm biceps brachii gastrocnemius muscle triceps brachii muscle Top expressed in triceps brachii muscle quadriceps femoris muscle vastus lateralis muscle sternocleidomastoid muscle gastrocnemius muscle extensor digitorum longus muscle plantaris muscle temporal muscle medial head of gastrocnemius muscle tibialis anterior muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding molecular adaptor activity Cellular component cytoplasm membrane nucleus cytosol aminoacyl-tRNA synthetase multienzyme complex Biological process multicellular organism development cell differentiation type II pneumocyte differentiation positive regulation of neuron death positive regulation of protein ubiquitination tRNA aminoacylation for protein translation protein biosynthesis negative regulation of cell population proliferation apoptotic process positive regulation of aminoacyl-tRNA ligase activity protein-containing complex assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7965 231872 Ensembl ENSG00000106305 ENSMUSG00000029610 UniProt Q13155 Q8R010 RefSeq (mRNA) NM_006303 NM_001326606 NM_001326607 NM_001326609 NM_001326611 NM_018570 NM_001326610 NM_001362785 NM_001362787 NM_001172146 NM_146165 RefSeq (protein) NP_001313535 NP_001313536 NP_001313538 NP_001313539 NP_001313540 NP_006294 NP_001349714 NP_001349716 NP_001165617 NP_666277 Location (UCSC) Chr 7: 6.01 – 6.02 Mb Chr 5: 143.84 – 143.85 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 2 is an enzyme that in humans is encoded by the AIMP2 gene.

Function

The JTV1 gene is located on chromosome 7p22 flanked by two genes, HRI and PMS2. JTV1 and HRI overlap slightly and are arranged in a tail-to-tail fashion. JTV1 and PMS2 are separated by approximately 200 base pairs and are arranged head-to-head. JTV1 is transcribed in the opposite direction compared to HRI and PMS2. The function of the JTV1 gene product is unknown.

Interactions

Multisynthetase complex auxiliary component p38 has been shown to interact with Parkin (ligase), P53 and KARS.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000106305 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029610 – Ensembl, 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. Nicolaides NC, Kinzler KW, Vogelstein B (September 1995). "Analysis of the 5' region of PMS2 reveals heterogeneous transcripts and a novel overlapping gene". Genomics. 29 (2): 329–34. doi:10.1006/geno.1995.9997. PMID 8666379.
6. ^ Han JM, Park BJ, Park SG, Oh YS, Choi SJ, Lee SW, Hwang SK, Chang SH, Cho MH, Kim S (August 2008). "AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53". Proceedings of the National Academy of Sciences of the United States of America. 105 (32): 11206–11. Bibcode:2008PNAS..10511206H. doi:10.1073/pnas.0800297105. PMC 2516205. PMID 18695251.
7. ^ "Entrez Gene: JTV1 JTV1 gene".
8. Corti O, Hampe C, Koutnikova H, Darios F, Jacquier S, Prigent A, Robinson JC, Pradier L, Ruberg M, Mirande M, Hirsch E, Rooney T, Fournier A, Brice A (June 2003). "The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration". Human Molecular Genetics. 12 (12): 1427–37. doi:10.1093/hmg/ddg159. PMID 12783850.
9. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
10. Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (January 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.

Further reading

• Park SG, Ewalt KL, Kim S (October 2005). "Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers". Trends in Biochemical Sciences. 30 (10): 569–74. doi:10.1016/j.tibs.2005.08.004. PMID 16125937.
• Raszewski W (1978). "Protective action of series of new mono-pyridinium salts and their effect on "aging" of acetylcholine esterase inhibited by fluostigmine". Polish Journal of Pharmacology and Pharmacy. 29 (6): 603–7. PMID 600859.
• Norcum MT (August 1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". The Journal of Biological Chemistry. 266 (23): 15398–405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
• Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (January 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
• Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ, Kwon HJ, Kim S (October 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". The Journal of Biological Chemistry. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
• Ahn HC, Kim S, Lee BJ (May 2003). "Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43". FEBS Letters. 542 (1–3): 119–24. doi:10.1016/S0014-5793(03)00362-4. PMID 12729910. S2CID 39222196.
• Corti O, Hampe C, Koutnikova H, Darios F, Jacquier S, Prigent A, Robinson JC, Pradier L, Ruberg M, Mirande M, Hirsch E, Rooney T, Fournier A, Brice A (June 2003). "The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration". Human Molecular Genetics. 12 (12): 1427–37. doi:10.1093/hmg/ddg159. PMID 12783850.
• Kim MJ, Park BJ, Kang YS, Kim HJ, Park JH, Kang JW, Lee SW, Han JM, Lee HW, Kim S (July 2003). "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation". Nature Genetics. 34 (3): 330–6. doi:10.1038/ng1182. PMID 12819782. S2CID 41006480.
• Sampath P, Mazumder B, Seshadri V, Gerber CA, Chavatte L, Kinter M, Ting SM, Dignam JD, Kim S, Driscoll DM, Fox PL (October 2004). "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation". Cell. 119 (2): 195–208. doi:10.1016/j.cell.2004.09.030. PMID 15479637. S2CID 18944876.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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