AIMP2_CRIGR
ID AIMP2_CRIGR Reviewed; 320 AA.
AC Q9WVM7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
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).
CC -!- FUNCTION: Required for assembly and stability of the aminoacyl-tRNA
CC synthase complex. Mediates ubiquitination and degradation of FUBP1, a
CC transcriptional activator of MYC, leading to MYC down-regulation which
CC is required for aveolar type II cell differentiation. Blocks MDM2-
CC mediated ubiquitination and degradation of p53/TP53. Functions as a
CC proapoptotic factor. {ECO:0000250|UniProtKB:Q13155}.
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. Interacts (via N-terminus) with
CC KARS1. Interacts with EPRS1. Forms a linear complex that contains
CC MARS1, EEF1E1, EPRS1 and AIMP2 that is at the core of the multisubunit
CC complex. Binds FUBP1 (via C-terminus). Interacts in both its
CC unphosphorylated and phosphorylated forms with p53/TP53 (via N-
CC terminus) in the nucleus following UV irradiation. Interacts (via N-
CC terminus) with PRKN/parkin (via first RING-type domain). Interacts with
CC TARS3. {ECO:0000250|UniProtKB:Q13155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8R010}. Nucleus {ECO:0000250|UniProtKB:Q8R010}.
CC Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase
CC complex and translocates from the cytoplasm to the nucleus.
CC {ECO:0000250|UniProtKB:Q8R010}.
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. {ECO:0000250}.
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DR EMBL; AF072727; AAD38422.1; -; mRNA.
DR RefSeq; NP_001230912.1; NM_001243983.1.
DR AlphaFoldDB; Q9WVM7; -.
DR SMR; Q9WVM7; -.
DR IntAct; Q9WVM7; 1.
DR STRING; 10029.NP_001230912.1; -.
DR Ensembl; ENSCGRT00001021211; ENSCGRP00001016967; ENSCGRG00001017144.
DR GeneID; 100682533; -.
DR KEGG; cge:100682533; -.
DR CTD; 7965; -.
DR eggNOG; ENOG502QUNJ; Eukaryota.
DR GeneTree; ENSGT00390000015826; -.
DR OrthoDB; 1382507at2759; -.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:1903632; P:positive regulation of aminoacyl-tRNA ligase activity; 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 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; PF14497; GST_C_3; 1.
DR Pfam; PF18569; Thioredoxin_16; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Developmental protein; Differentiation; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Ubl conjugation.
FT CHAIN 1..320
FT /note="Aminoacyl tRNA synthase complex-interacting
FT multifunctional protein 2"
FT /id="PRO_0000221128"
FT DOMAIN 220..317
FT /note="GST C-terminal"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q8R010"
SQ SEQUENCE 320 AA; 35433 MW; 6D24E033ABEC810A CRC64;
MPMYQVKSYH GGSAPLRVEL PTCMYRLPNV HSKTTSPATD AGHVQETSEP SLQALESRQD
DILKRLYELK AAVDGLSKMI HTPDADLDVT NILQADEPVP LTTNALDLNL VLGKDYGALK
DIVINANPAS PPISLLVLHR LLCERYRVLS TVHTHSSVKN VPENLLKCFG EQARKQSRHE
YQLGFTLIWK NVPKTQMKFS VQTMCPIEGE GNIARFLFSL FGQKHSAVNL TLIDSWVDIA
MFQLKEGSSK ERAAVFRSMN SALGKSPWLV GNELTVADVV LWSVLQQTGD GSGVAPANVQ
RWLKSCENLV PFSTALQLLK
