ID AIMP2_HUMAN Reviewed; 320 AA. AC Q13155; F8W950; Q75MR1; Q96CZ5; Q9P1L2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 2; DE AltName: Full=Multisynthase complex auxiliary component p38; DE AltName: Full=Protein JTV-1; GN Name=AIMP2; Synonyms=JTV1; ORFNames=PRO0992; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8666379; DOI=10.1006/geno.1995.9997; RA Nicolaides N.C., Kinzler K.W., Vogelstein B.; RT "Analysis of the 5' region of PMS2 reveals heterogeneous transcripts and a RT novel overlapping gene."; RL Genomics 29:329-334(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-129. RC TISSUE=Lymph, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-17 AND 34-58, ALTERNATIVE SPLICING, IDENTIFICATION IN RP THE MSC COMPLEX, INTERACTION WITH TARS3, AND IDENTIFICATION BY MASS RP SPECTROMETRY (ISOFORMS 1 AND 2). RX PubMed=24312579; DOI=10.1371/journal.pone.0081734; RA Kim K., Park S.J., Na S., Kim J.S., Choi H., Kim Y.K., Paek E., Lee C.; RT "Reinvestigation of aminoacyl-tRNA synthetase core complex by affinity RT purification-mass spectrometry reveals TARSL2 as a potential member of the RT complex."; RL PLoS ONE 8:E81734-E81734(2013). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-320. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., RA Liu M., He F.; RT "Functional prediction of the coding sequences of 121 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH KARS1. RX PubMed=9878398; DOI=10.1006/jmbi.1998.2316; RA Quevillon S., Robinson J.-C., Berthonneau E., Siatecka M., Mirande M.; RT "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of RT protein-protein interactions and characterization of a core protein."; RL J. Mol. Biol. 285:183-195(1999). RN [9] RP INTERACTION WITH FUBP1. RX PubMed=12819782; DOI=10.1038/ng1182; RA Kim M.J., Park B.-J., Kang Y.-S., Kim H.J., Park J.-H., Kang J.W., RA Lee S.W., Han J.M., Lee H.-W., Kim S.; RT "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase RT cofactor p38 is required for lung cell differentiation."; RL Nat. Genet. 34:330-336(2003). RN [10] RP INTERACTION WITH KARS1. RX PubMed=15220430; DOI=10.1128/jvi.78.14.7553-7564.2004; RA Halwani R., Cen S., Javanbakht H., Saadatmand J., Kim S., Shiba K., RA Kleiman L.; RT "Cellular distribution of Lysyl-tRNA synthetase and its interaction with RT Gag during human immunodeficiency virus type 1 assembly."; RL J. Virol. 78:7553-7564(2004). RN [11] RP FUNCTION, INTERACTION WITH PRKN, AND UBIQUITINATION. RX PubMed=16135753; DOI=10.1523/jneurosci.2172-05.2005; RA Ko H.S., von Coelln R., Sriram S.R., Kim S.W., Chung K.K.K., Pletnikova O., RA Troncoso J., Johnson B., Saffary R., Goh E.L., Song H., Park B.-J., RA Kim M.J., Kim S., Dawson V.L., Dawson T.M.; RT "Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase RT cofactor, p38/JTV-1, leads to catecholaminergic cell death."; RL J. Neurosci. 25:7968-7978(2005). RN [12] RP INTERACTION WITH KARS1. RX PubMed=18029264; DOI=10.1016/j.bbrc.2007.11.028; RA Guzzo C.M., Yang D.C.H.; RT "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase RT and p38 in vitro."; RL Biochem. Biophys. Res. Commun. 365:718-723(2008). RN [13] RP INTERACTION WITH TP53, VARIANTS VAL-92; 97-GLU--THR-99 DELINS ASP-LEU-SER RP AND SER-209, AND MUTAGENESIS OF 163-GLU-ASN-164 AND 172-GLN-ASN-173. RX PubMed=18695251; DOI=10.1073/pnas.0800297105; RA Han J.M., Park B.-J., Park S.G., Oh Y.S., Choi S.J., Lee S.W., Hwang S.-K., RA Chang S.-H., Cho M.-H., Kim S.; RT "AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to RT genotoxic stresses via p53."; RL Proc. Natl. Acad. Sci. U.S.A. 105:11206-11211(2008). RN [14] RP FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19131329; DOI=10.1074/jbc.m809636200; RA Kaminska M., Havrylenko S., Decottignies P., Gillet S., Le Marechal P., RA Negrutskii B., Mirande M.; RT "Dissection of the structural organization of the aminoacyl-tRNA synthetase RT complex."; RL J. Biol. Chem. 284:6053-6060(2009). RN [15] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=19289464; DOI=10.1074/jbc.m900480200; RA Kaminska M., Havrylenko S., Decottignies P., Le Marechal P., Negrutskii B., RA Mirande M.; RT "Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the RT Cytoplasm of Human Cells."; RL J. Biol. Chem. 284:13746-13754(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] {ECO:0007744|PDB:4DPG} RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 1-48 IN COMPLEX WITH KARS1, AND RP SUBUNIT. RX PubMed=23159739; DOI=10.1016/j.molcel.2012.10.010; RA Ofir-Birin Y., Fang P., Bennett S.P., Zhang H.M., Wang J., Rachmin I., RA Shapiro R., Song J., Dagan A., Pozo J., Kim S., Marshall A.G., Schimmel P., RA Yang X.L., Nechushtan H., Razin E., Guo M.; RT "Structural switch of lysyl-tRNA synthetase between translation and RT transcription."; RL Mol. Cell 49:30-42(2013). RN [19] {ECO:0007744|PDB:4YCU, ECO:0007744|PDB:4YCW} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-36 IN COMPLEX WITH KARS1. RX PubMed=26074468; DOI=10.1016/j.chembiol.2015.05.007; RA Fang P., Han H., Wang J., Chen K., Chen X., Guo M.; RT "Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP RT Competitive Inhibitor."; RL Chem. Biol. 22:734-744(2015). RN [20] {ECO:0007744|PDB:5A34} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 90-320 IN COMPLEX WITH EPRS1, RP SUBUNIT, AND MUTAGENESIS OF ARG-215 AND ASP-238. RX PubMed=26472928; DOI=10.1074/jbc.m115.690867; RA Cho H.Y., Maeng S.J., Cho H.J., Choi Y.S., Chung J.M., Lee S., Kim H.K., RA Kim J.H., Eom C.Y., Kim Y.G., Guo M., Jung H.S., Kang B.S., Kim S.; RT "Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione RT Transferase-homology Domains."; RL J. Biol. Chem. 290:29313-29328(2015). RN [21] RP INVOLVEMENT IN HLD17, AND VARIANT HLD17 35-TYR--LYS-320 DEL. RX PubMed=29215095; DOI=10.1038/s10038-017-0363-1; RA Shukla A., Das Bhowmik A., Hebbar M., Rajagopal K.V., Girisha K.M., RA Gupta N., Dalal A.; RT "Homozygosity for a nonsense variant in AIMP2 is associated with a RT progressive neurodevelopmental disorder with microcephaly, seizures, and RT spastic quadriparesis."; RL J. Hum. Genet. 63:19-25(2018). CC -!- FUNCTION: Required for assembly and stability of the aminoacyl-tRNA CC synthase complex (PubMed:19131329). Mediates ubiquitination and CC degradation of FUBP1, a transcriptional activator of MYC, leading to CC MYC down-regulation which is required for aveolar type II cell CC differentiation. Blocks MDM2-mediated ubiquitination and degradation of CC p53/TP53. Functions as a proapoptotic factor. CC {ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:19131329}. CC -!- SUBUNIT: Part of the multisynthetase complex (MSC), a multisubunit CC complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln CC (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the CC bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits CC AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:24312579, PubMed:19131329, CC PubMed:19289464). Interacts (via N-terminus) with KARS1 CC (PubMed:9878398, PubMed:15220430, PubMed:18029264, PubMed:23159739, CC PubMed:26074468). Interacts with EPRS1 (PubMed:26472928). Forms a CC linear complex that contains MARS1, EEF1E1, EPRS1 and AIMP2 that is at CC the core of the multisubunit complex (PubMed:26472928). Binds FUBP1 CC (via C-terminus). Interacts in both its unphosphorylated and CC phosphorylated forms with p53/TP53 (via N-terminus) in the nucleus CC following UV irradiation. Interacts (via N-terminus) with PRKN/parkin CC (via first RING-type domain) (PubMed:16135753). Interacts with TARS3 CC (PubMed:24312579). {ECO:0000269|PubMed:12819782, CC ECO:0000269|PubMed:15220430, ECO:0000269|PubMed:16135753, CC ECO:0000269|PubMed:18029264, ECO:0000269|PubMed:18695251, CC ECO:0000269|PubMed:19131329, ECO:0000269|PubMed:19289464, CC ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:24312579, CC ECO:0000269|PubMed:26074468, ECO:0000269|PubMed:26472928, CC ECO:0000269|PubMed:9878398}. CC -!- INTERACTION: CC Q13155; Q12904: AIMP1; NbExp=4; IntAct=EBI-745226, EBI-1045802; CC Q13155; Q12904-2: AIMP1; NbExp=5; IntAct=EBI-745226, EBI-12412735; CC Q13155; P05067: APP; NbExp=3; IntAct=EBI-745226, EBI-77613; CC Q13155; O75934: BCAS2; NbExp=12; IntAct=EBI-745226, EBI-1050106; CC Q13155; Q0VDD7: BRME1; NbExp=8; IntAct=EBI-745226, EBI-741210; CC Q13155; Q13895: BYSL; NbExp=5; IntAct=EBI-745226, EBI-358049; CC Q13155; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-745226, EBI-747505; CC Q13155; Q8NA61-2: CBY2; NbExp=5; IntAct=EBI-745226, EBI-11524851; CC Q13155; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-745226, EBI-11974185; CC Q13155; Q96L14: CEP170P1; NbExp=5; IntAct=EBI-745226, EBI-743488; CC Q13155; P14868: DARS1; NbExp=10; IntAct=EBI-745226, EBI-358730; CC Q13155; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-745226, EBI-11988027; CC Q13155; Q8IYI6: EXOC8; NbExp=5; IntAct=EBI-745226, EBI-742102; CC Q13155; Q13643: FHL3; NbExp=13; IntAct=EBI-745226, EBI-741101; CC Q13155; Q96AE4: FUBP1; NbExp=4; IntAct=EBI-745226, EBI-711404; CC Q13155; P13807: GYS1; NbExp=3; IntAct=EBI-745226, EBI-740553; CC Q13155; Q15046: KARS1; NbExp=21; IntAct=EBI-745226, EBI-356367; CC Q13155; Q15046-1: KARS1; NbExp=2; IntAct=EBI-745226, EBI-21457670; CC Q13155; Q15323: KRT31; NbExp=3; IntAct=EBI-745226, EBI-948001; CC Q13155; Q14525: KRT33B; NbExp=3; IntAct=EBI-745226, EBI-1049638; CC Q13155; O76011: KRT34; NbExp=3; IntAct=EBI-745226, EBI-1047093; CC Q13155; O76013-2: KRT36; NbExp=3; IntAct=EBI-745226, EBI-11958506; CC Q13155; P25791: LMO2; NbExp=3; IntAct=EBI-745226, EBI-739696; CC Q13155; P25791-3: LMO2; NbExp=6; IntAct=EBI-745226, EBI-11959475; CC Q13155; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-745226, EBI-739832; CC Q13155; Q9NYP9: MIS18A; NbExp=6; IntAct=EBI-745226, EBI-1104552; CC Q13155; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-745226, EBI-928842; CC Q13155; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-745226, EBI-10172876; CC Q13155; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-745226, EBI-741158; CC Q13155; P22061: PCMT1; NbExp=3; IntAct=EBI-745226, EBI-353343; CC Q13155; O15212: PFDN6; NbExp=3; IntAct=EBI-745226, EBI-356973; CC Q13155; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-745226, EBI-742388; CC Q13155; P54646: PRKAA2; NbExp=3; IntAct=EBI-745226, EBI-1383852; CC Q13155; Q15276: RABEP1; NbExp=3; IntAct=EBI-745226, EBI-447043; CC Q13155; P0C264: SBK3; NbExp=3; IntAct=EBI-745226, EBI-17181801; CC Q13155; O95391: SLU7; NbExp=3; IntAct=EBI-745226, EBI-750559; CC Q13155; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-745226, EBI-11334239; CC Q13155; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-745226, EBI-17721485; CC Q13155; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-745226, EBI-750109; CC Q13155; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-745226, EBI-12090309; CC Q13155; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-745226, EBI-1105213; CC Q13155; P04637: TP53; NbExp=6; IntAct=EBI-745226, EBI-366083; CC Q13155; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-745226, EBI-16428984; CC Q13155; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-745226, EBI-3439227; CC Q13155; Q8N5A5-2: ZGPAT; NbExp=12; IntAct=EBI-745226, EBI-10183064; CC Q13155; PRO_0000038593 [P04591]: gag; Xeno; NbExp=3; IntAct=EBI-745226, EBI-6179719; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. CC Nucleus {ECO:0000250|UniProtKB:Q8R010}. Note=Following DNA damage, CC dissociates from the aminoacyl-tRNA synthase complex and translocates CC from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q8R010}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13155-1; Sequence=Displayed; CC Name=2; Synonyms=DX2 {ECO:0000303|PubMed:24312579}; CC IsoId=Q13155-2; Sequence=VSP_059914; CC -!- PTM: Phosphorylated on serine residues in response to UV irradiation. CC {ECO:0000250}. CC -!- PTM: Ubiquitinated by PRKN, leading to its degradation by the CC proteasome. Mutant PRKN fails to ubiquitinate AIMP2 efficiently, CC allowing its accumulation which may contribute to neurodegeneration CC associated with Parkinson disease. {ECO:0000269|PubMed:16135753}. CC -!- DISEASE: Leukodystrophy, hypomyelinating, 17 (HLD17) [MIM:618006]: An CC autosomal recessive neurodevelopmental disorder characterized by CC atrophy of cerebral cortex, spinal cord and cerebellum, thin corpus CC callosum, abnormal signals in the basal ganglia, and features CC suggesting hypo- or demyelination observed on brain imaging. Clinical CC manifestations include lack of development, absent speech, CC microcephaly, spasticity, seizures, and contractures. CC {ECO:0000269|PubMed:29215095}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Accumulates in brains affected by autosomal-recessive CC juvenile parkinsonism, idiopathic Parkinson disease and diffuse Lewy CC body disease. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50391.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U24169; AAC50391.1; ALT_FRAME; mRNA. DR EMBL; AC005995; AAS00389.1; -; Genomic_DNA. DR EMBL; CH236963; EAL23713.1; -; Genomic_DNA. DR EMBL; CH878731; EAW55053.1; -; Genomic_DNA. DR EMBL; BC002853; AAH02853.1; -; mRNA. DR EMBL; BC010156; AAH10156.1; -; mRNA. DR EMBL; BC013630; AAH13630.1; -; mRNA. DR EMBL; AF116615; AAF71039.1; -; mRNA. DR CCDS; CCDS5344.1; -. [Q13155-1] DR CCDS; CCDS87475.1; -. [Q13155-2] DR RefSeq; NP_001313536.1; NM_001326607.1. [Q13155-2] DR RefSeq; NP_006294.2; NM_006303.3. [Q13155-1] DR PDB; 4DPG; X-ray; 2.84 A; I/J/K/L=1-48. DR PDB; 4YCU; X-ray; 2.10 A; C=1-36. DR PDB; 4YCW; X-ray; 2.90 A; C/D/G/H=1-36. DR PDB; 5A1N; X-ray; 2.10 A; B=90-320. DR PDB; 5A34; X-ray; 2.60 A; B/D/F/H=90-320. DR PDB; 5A5H; X-ray; 2.32 A; B/D/F/H=90-320. DR PDB; 5Y6L; X-ray; 2.90 A; D=89-320. DR PDB; 6ILD; X-ray; 1.88 A; C=1-36. DR PDB; 6IY6; X-ray; 3.60 A; C/D/I/J=115-320. DR PDB; 6JPV; X-ray; 2.15 A; A/B=24-32. DR PDB; 6K39; X-ray; 1.40 A; A/B=25-32. DR PDBsum; 4DPG; -. DR PDBsum; 4YCU; -. DR PDBsum; 4YCW; -. DR PDBsum; 5A1N; -. DR PDBsum; 5A34; -. DR PDBsum; 5A5H; -. DR PDBsum; 5Y6L; -. DR PDBsum; 6ILD; -. DR PDBsum; 6IY6; -. DR PDBsum; 6JPV; -. DR PDBsum; 6K39; -. DR AlphaFoldDB; Q13155; -. DR SMR; Q13155; -. DR BioGRID; 113684; 443. DR ComplexPortal; CPX-2469; Multiaminoacyl-tRNA synthetase complex. DR CORUM; Q13155; -. DR DIP; DIP-34421N; -. DR IntAct; Q13155; 100. DR MINT; Q13155; -. DR STRING; 9606.ENSP00000223029; -. DR BindingDB; Q13155; -. DR ChEMBL; CHEMBL4523285; -. DR GlyGen; Q13155; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13155; -. DR PhosphoSitePlus; Q13155; -. DR SwissPalm; Q13155; -. DR BioMuta; AIMP2; -. DR EPD; Q13155; -. DR jPOST; Q13155; -. DR MassIVE; Q13155; -. DR MaxQB; Q13155; -. DR PaxDb; 9606-ENSP00000223029; -. DR PeptideAtlas; Q13155; -. DR ProteomicsDB; 30261; -. DR ProteomicsDB; 59195; -. DR Pumba; Q13155; -. DR ABCD; Q13155; 1 sequenced antibody. DR Antibodypedia; 11563; 237 antibodies from 32 providers. DR DNASU; 7965; -. DR Ensembl; ENST00000223029.8; ENSP00000223029.3; ENSG00000106305.10. [Q13155-1] DR Ensembl; ENST00000395236.2; ENSP00000378658.2; ENSG00000106305.10. [Q13155-2] DR GeneID; 7965; -. DR KEGG; hsa:7965; -. DR MANE-Select; ENST00000223029.8; ENSP00000223029.3; NM_006303.4; NP_006294.2. DR UCSC; uc003spo.4; human. [Q13155-1] DR AGR; HGNC:20609; -. DR CTD; 7965; -. DR DisGeNET; 7965; -. DR GeneCards; AIMP2; -. DR HGNC; HGNC:20609; AIMP2. DR HPA; ENSG00000106305; Tissue enhanced (skeletal). DR MalaCards; AIMP2; -. DR MIM; 600859; gene. DR MIM; 618006; phenotype. DR neXtProt; NX_Q13155; -. DR OpenTargets; ENSG00000106305; -. DR PharmGKB; PA165617609; -. DR VEuPathDB; HostDB:ENSG00000106305; -. DR eggNOG; ENOG502QUNJ; Eukaryota. DR GeneTree; ENSGT00390000015826; -. DR HOGENOM; CLU_076114_0_0_1; -. DR InParanoid; Q13155; -. DR OMA; LCQHYRV; -. DR OrthoDB; 4146269at2759; -. DR PhylomeDB; Q13155; -. DR TreeFam; TF326322; -. DR PathwayCommons; Q13155; -. DR Reactome; R-HSA-2408522; Selenoamino acid metabolism. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR SignaLink; Q13155; -. DR SIGNOR; Q13155; -. DR BioGRID-ORCS; 7965; 17 hits in 1160 CRISPR screens. DR ChiTaRS; AIMP2; human. DR GeneWiki; Multisynthetase_complex_auxiliary_component_p38; -. DR GenomeRNAi; 7965; -. DR Pharos; Q13155; Tchem. DR PRO; PR:Q13155; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q13155; Protein. DR Bgee; ENSG00000106305; Expressed in oocyte and 219 other cell types or tissues. DR ExpressionAtlas; Q13155; baseline and differential. DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl. DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR GO; GO:0060510; P:type II pneumocyte differentiation; IEA:Ensembl. DR CDD; cd03200; GST_C_AIMP2; 1. DR Gene3D; 1.20.1050.130; -; 1. DR InterPro; IPR042360; AIMP2. DR InterPro; IPR031889; AIMP2_LysRS-bd. DR InterPro; IPR041503; AIMP2_thioredoxin. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR004046; GST_C. DR PANTHER; PTHR13438; AMINOACYL TRNA SYNTHASE COMPLEX-INTERACTING MULTIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR13438:SF2; AMINOACYL TRNA SYNTHASE COMPLEX-INTERACTING MULTIFUNCTIONAL PROTEIN 2; 1. DR Pfam; PF16780; AIMP2_LysRS_bd; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF18569; Thioredoxin_16; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR Genevisible; Q13155; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; KW Developmental protein; Differentiation; Direct protein sequencing; KW Disease variant; Leukodystrophy; Nucleus; Phosphoprotein; KW Protein biosynthesis; Reference proteome; Ubl conjugation. FT CHAIN 1..320 FT /note="Aminoacyl tRNA synthase complex-interacting FT multifunctional protein 2" FT /id="PRO_0000221129" FT DOMAIN 220..317 FT /note="GST C-terminal" FT REGION 82..162 FT /note="Interaction with PRKN" FT /evidence="ECO:0000269|PubMed:16135753" FT REGION 162..225 FT /note="Interaction with TP53" FT /evidence="ECO:0000269|PubMed:18695251" FT VAR_SEQ 46..114 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000269|PubMed:24312579" FT /id="VSP_059914" FT VARIANT 35..320 FT /note="Missing (in HLD17)" FT /evidence="ECO:0000269|PubMed:29215095" FT /id="VAR_081108" FT VARIANT 92 FT /note="I -> V (in a lung cancer cell line; reduced FT interaction with TP53, loss of TP53 activation and loss of FT proapoptotic activity)" FT /evidence="ECO:0000269|PubMed:18695251" FT /id="VAR_058392" FT VARIANT 97..99 FT /note="EPT -> DLS (in a lung cancer cell line; no effect on FT proapoptotic activity)" FT /evidence="ECO:0000269|PubMed:18695251" FT /id="VAR_058393" FT VARIANT 129 FT /note="A -> G (in dbSNP:rs17855441)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_025521" FT VARIANT 166 FT /note="L -> I (in dbSNP:rs34525431)" FT /id="VAR_050125" FT VARIANT 209 FT /note="G -> S (in a lung cancer cell line; no effect on FT proapoptotic activity; dbSNP:rs982080297)" FT /evidence="ECO:0000269|PubMed:18695251" FT /id="VAR_058394" FT MUTAGEN 163..164 FT /note="EN->AA: Reduced interaction with TP53, loss of TP53 FT activation and loss of proapoptotic activity." FT /evidence="ECO:0000269|PubMed:18695251" FT MUTAGEN 172..173 FT /note="QN->AA: Reduced interaction with TP53, loss of TP53 FT activation and loss of proapoptotic activity." FT /evidence="ECO:0000269|PubMed:18695251" FT MUTAGEN 215 FT /note="R->A: Nearly abolishes interaction with EPRS1." FT /evidence="ECO:0000269|PubMed:26472928" FT MUTAGEN 238 FT /note="D->R: Nearly abolishes interaction with EPRS1." FT /evidence="ECO:0000269|PubMed:26472928" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:6ILD" FT HELIX 108..112 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5A34" FT HELIX 133..143 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:5A1N" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:5A5H" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:5A5H" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:5A5H" FT HELIX 210..219 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 227..242 FT /evidence="ECO:0007829|PDB:5A1N" FT TURN 243..246 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 249..262 FT /evidence="ECO:0007829|PDB:5A1N" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 276..286 FT /evidence="ECO:0007829|PDB:5A1N" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:5Y6L" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:5A1N" FT HELIX 310..318 FT /evidence="ECO:0007829|PDB:5A1N" SQ SEQUENCE 320 AA; 35349 MW; F253726B63C12BAB CRC64; MPMYQVKPYH GGGAPLRVEL PTCMYRLPNV HGRSYGPAPG AGHVQEESNL SLQALESRQD DILKRLYELK AAVDGLSKMI QTPDADLDVT NIIQADEPTT LTTNALDLNS VLGKDYGALK DIVINANPAS PPLSLLVLHR LLCEHFRVLS TVHTHSSVKS VPENLLKCFG EQNKKQPRQD YQLGFTLIWK NVPKTQMKFS IQTMCPIEGE GNIARFLFSL FGQKHNAVNA TLIDSWVDIA IFQLKEGSSK EKAAVFRSMN SALGKSPWLA GNELTVADVV LWSVLQQIGG CSVTVPANVQ RWMRSCENLA PFNTALKLLK //