AIMP2_MOUSE
ID AIMP2_MOUSE Reviewed; 320 AA.
AC Q8R010; E9QP67; Q8R2Y6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aminoacyl tRNA synthase complex-interacting multifunctional protein 2;
DE AltName: Full=Multisynthase complex auxiliary component p38 {ECO:0000303|PubMed:12060739};
DE AltName: Full=Protein JTV-1;
GN Name=Aimp2; Synonyms=Jtv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=12060739; DOI=10.1073/pnas.122110199;
RA Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H., Ko Y.-G.,
RA Kim S.;
RT "p38 is essential for the assembly and stability of macromolecular tRNA
RT synthetase complex: implications for its physiological significance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for assembly and stability of the aminoacyl-tRNA
CC synthase complex (PubMed:12060739). 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 (PubMed:12819782). Blocks MDM2-mediated ubiquitination
CC and degradation of p53/TP53 (PubMed:18695251). Functions as a
CC proapoptotic factor (PubMed:16135753). {ECO:0000269|PubMed:12060739,
CC ECO:0000269|PubMed:12819782, ECO:0000269|PubMed:16135753,
CC ECO:0000269|PubMed:18695251}.
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:12060739). Interacts (via
CC N-terminus) with KARS1. Interacts with EPRS1. Forms a linear complex
CC that contains MARS1, EEF1E1, EPRS1 and AIMP2 that is at the core of the
CC multisubunit complex. Binds FUBP1 (via C-terminus) (By similarity).
CC Interacts in both its unphosphorylated and phosphorylated forms with
CC p53/TP53 (via N-terminus) in the nucleus following UV irradiation.
CC Interacts (via N-terminus) with PRKN/parkin (via first RING-type
CC domain). Interacts with TARS3. {ECO:0000250|UniProtKB:Q13155,
CC ECO:0000269|PubMed:12060739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18695251}.
CC Nucleus {ECO:0000269|PubMed:18695251}. Note=Following DNA damage,
CC dissociates from the aminoacyl-tRNA synthase complex and translocates
CC from the cytoplasm to the nucleus. {ECO:0000269|PubMed:18695251}.
CC -!- PTM: Phosphorylated on serine residues in response to UV irradiation.
CC {ECO:0000269|PubMed:18695251}.
CC -!- PTM: Ubiquitinated by PRKN, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of component enzymes and
CC associated factors of the aminoacyl-tRNA synthase complex, lack of
CC complex formation and lethality within two days of birth. Neonates
CC display severe hyperplasia in a number of organs including lung,
CC intestine and liver, lung failure, and disturbed thymocyte
CC proliferation and differentiation. Embryonic fibroblasts deficient in
CC Aimp2 are resistant to apoptosis following UV irradiation.
CC {ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:12819782}.
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DR EMBL; AC121917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024410; AAH24410.1; -; mRNA.
DR EMBL; BC026958; AAH26958.1; -; mRNA.
DR EMBL; BC026972; AAH26972.1; -; mRNA.
DR CCDS; CCDS51692.1; -.
DR RefSeq; NP_001165617.1; NM_001172146.1.
DR AlphaFoldDB; Q8R010; -.
DR SMR; Q8R010; -.
DR BioGRID; 231187; 20.
DR STRING; 10090.ENSMUSP00000031613; -.
DR MoonProt; Q8R010; -.
DR iPTMnet; Q8R010; -.
DR PhosphoSitePlus; Q8R010; -.
DR SwissPalm; Q8R010; -.
DR EPD; Q8R010; -.
DR jPOST; Q8R010; -.
DR MaxQB; Q8R010; -.
DR PaxDb; Q8R010; -.
DR PeptideAtlas; Q8R010; -.
DR PRIDE; Q8R010; -.
DR ProteomicsDB; 285788; -.
DR Antibodypedia; 11563; 214 antibodies from 32 providers.
DR DNASU; 231872; -.
DR Ensembl; ENSMUST00000031613; ENSMUSP00000031613; ENSMUSG00000029610.
DR GeneID; 231872; -.
DR KEGG; mmu:231872; -.
DR UCSC; uc009akw.2; mouse.
DR CTD; 7965; -.
DR MGI; MGI:2385237; Aimp2.
DR VEuPathDB; HostDB:ENSMUSG00000029610; -.
DR eggNOG; ENOG502QUNJ; Eukaryota.
DR GeneTree; ENSGT00390000015826; -.
DR InParanoid; Q8R010; -.
DR OMA; LCQHYRV; -.
DR OrthoDB; 1382507at2759; -.
DR PhylomeDB; Q8R010; -.
DR TreeFam; TF326322; -.
DR BioGRID-ORCS; 231872; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Aimp2; mouse.
DR PRO; PR:Q8R010; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R010; protein.
DR Bgee; ENSMUSG00000029610; Expressed in triceps brachii and 277 other tissues.
DR ExpressionAtlas; Q8R010; baseline and differential.
DR Genevisible; Q8R010; MM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:CAFA.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:1903632; P:positive regulation of aminoacyl-tRNA ligase activity; IMP:CAFA.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:CAFA.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR GO; GO:0060510; P:type II pneumocyte differentiation; IMP:MGI.
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; PTHR13438; 1.
DR Pfam; PF16780; AIMP2_LysRS_bd; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF18569; Thioredoxin_16; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..320
FT /note="Aminoacyl tRNA synthase complex-interacting
FT multifunctional protein 2"
FT /id="PRO_0000316841"
FT DOMAIN 220..317
FT /note="GST C-terminal"
FT REGION 82..162
FT /note="Interaction with PRKN"
FT /evidence="ECO:0000250"
FT REGION 162..225
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 17
FT /note="H -> R (in Ref. 2; AAH26958)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="S -> N (in Ref. 2; AAH24410/AAH26958/AAH26972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35378 MW; 247EBE7067180170 CRC64;
MPMYQVKPYH GGSAPLHVEL PTCMYRLPNV HSKTTSPATD AGHVQETSEP SLQALESRQD
DILKRLYELK AAVDGLSKMI HTPDADLDVT NILQADEPTT LATNTLDLNS VLGKDYGALK
DIVINANPAS PPLSLLVLHR LLCERYRVLS TVHTHSSVKN VPENLVKCFG EQARKQSRHE
YQLGFTLIWK NVPKTQMKFS VQTMCPIEGE GNIARFLFSL FGQKHNAVTL TLIDSWVDIA
MFQLREGSSK EKAAVFRSMN SALGRSPWLV GNELTVADVV LWSVLQQTGG SSGAAPTNVQ
RWLKSCENLA PFSTALQLLK
