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AIMP2_BOVIN
ID   AIMP2_BOVIN             Reviewed;         320 AA.
AC   Q0II26;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC122837; AAI22838.1; -; mRNA.
DR   RefSeq; NP_001069281.1; NM_001075813.2.
DR   AlphaFoldDB; Q0II26; -.
DR   SMR; Q0II26; -.
DR   STRING; 9913.ENSBTAP00000009687; -.
DR   PaxDb; Q0II26; -.
DR   PeptideAtlas; Q0II26; -.
DR   PRIDE; Q0II26; -.
DR   Ensembl; ENSBTAT00000009687; ENSBTAP00000009687; ENSBTAG00000007367.
DR   GeneID; 520979; -.
DR   KEGG; bta:520979; -.
DR   CTD; 7965; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007367; -.
DR   VGNC; VGNC:25766; AIMP2.
DR   eggNOG; ENOG502QUNJ; Eukaryota.
DR   GeneTree; ENSGT00390000015826; -.
DR   HOGENOM; CLU_076114_0_0_1; -.
DR   InParanoid; Q0II26; -.
DR   OMA; LCQHYRV; -.
DR   OrthoDB; 1382507at2759; -.
DR   TreeFam; TF326322; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000007367; Expressed in biceps femoris and 104 other tissues.
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; IBA:GO_Central.
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   PANTHER; PTHR13438; PTHR13438; 1.
DR   Pfam; PF16780; AIMP2_LysRS_bd; 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; Reference proteome; Ubl conjugation.
FT   CHAIN           1..320
FT                   /note="Aminoacyl tRNA synthase complex-interacting
FT                   multifunctional protein 2"
FT                   /id="PRO_0000316840"
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:0000250|UniProtKB:Q8R010"
SQ   SEQUENCE   320 AA;  35178 MW;  13D1A507989F0E34 CRC64;
     MPMYQVKPYH EGSGSLRVEL PTCMYRLPNV HGRTGSPAPS ADHVQEASDP SLQALESHQD
     DILKRLYELK AAVDGLSKMI QTPDADLDVT NIIQADEPAA LSTSTVDLNA MLGQDHGALK
     DIVINANPAS PPLSLLVLHR LLCDHYKVLS SVHTHSAVRS VPANLLQCFG EQTRQQPRHE
     YQLGFTLIWK DVPKTQMKFS VQTMCPIEGE GNIARFLFSL FGQKQDAVNL TLIDSWVDIA
     IFQLKEGSSK EKAAVFRSMN SALGKTPWLV GDELTVADVV LWSVLRQTGG CGGMAPANVQ
     KWMQACENLA PFHTALKLLQ
 
 
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