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Protein

Aminoacyl tRNA synthase complex-interacting multifunctional protein 2

Gene

AIMP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.2 Publications

Miscellaneous

Accumulates in brains affected by autosomal-recessive juvenile parkinsonism, idiopathic Parkinson disease and diffuse Lewy body disease.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein
Biological processApoptosis, Differentiation, Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Alternative name(s):
Multisynthase complex auxiliary component p38
Protein JTV-1
Gene namesi
Name:AIMP2
Synonyms:JTV1
ORF Names:PRO0992
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000106305.9.
HGNCiHGNC:20609. AIMP2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163 – 164EN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication2
Mutagenesisi172 – 173QN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication2
Mutagenesisi215R → A: Nearly abolishes interaction with EPRS. 1 Publication1
Mutagenesisi238D → R: Nearly abolishes interaction with EPRS. 1 Publication1

Organism-specific databases

DisGeNETi7965.
OpenTargetsiENSG00000106305.
PharmGKBiPA165617609.

Polymorphism and mutation databases

BioMutaiAIMP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002211291 – 320Aminoacyl tRNA synthase complex-interacting multifunctional protein 2Add BLAST320

Post-translational modificationi

Phosphorylated on serine residues in response to UV irradiation.By similarity
Ubiquitinated by PRKN, leading to its degradation by the proteasome. Mutant PRKN fails to ubiquitinate AIMP2 efficiently, allowing its accumulation which may contribute to neurodegeneration associated with Parkinson disease.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13155.
MaxQBiQ13155.
PaxDbiQ13155.
PeptideAtlasiQ13155.
PRIDEiQ13155.

PTM databases

iPTMnetiQ13155.
PhosphoSitePlusiQ13155.
SwissPalmiQ13155.

Expressioni

Gene expression databases

BgeeiENSG00000106305.
ExpressionAtlasiQ13155. baseline and differential.
GenevisibleiQ13155. HS.

Organism-specific databases

HPAiHPA019098.
HPA020057.

Interactioni

Subunit structurei

Part of a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464). Interacts (via N-terminus) with KARS (PubMed:9878398, PubMed:15220430, PubMed:18029264, PubMed:23159739, PubMed:26074468). Interacts with EPRS (PubMed:26472928). Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex (PubMed:26472928). Binds FUBP1 (via C-terminus). Interacts in both its unphosphorylated and phosphorylated forms with p53/TP53 (via N-terminus) in the nucleus following UV irradiation. Interacts (via N-terminus) with PRKN/parkin (via first RING-type domain) (PubMed:16135753).11 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113684. 86 interactors.
CORUMiQ13155.
DIPiDIP-34421N.
IntActiQ13155. 82 interactors.
MINTiMINT-5002775.
STRINGi9606.ENSP00000223029.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Helixi108 – 112Combined sources5
Helixi113 – 115Combined sources3
Helixi116 – 119Combined sources4
Beta strandi120 – 126Combined sources7
Beta strandi128 – 130Combined sources3
Helixi133 – 143Combined sources11
Beta strandi148 – 154Combined sources7
Helixi163 – 166Combined sources4
Turni167 – 169Combined sources3
Beta strandi182 – 189Combined sources8
Beta strandi196 – 198Combined sources3
Beta strandi202 – 204Combined sources3
Beta strandi207 – 209Combined sources3
Helixi210 – 219Combined sources10
Helixi227 – 242Combined sources16
Turni243 – 246Combined sources4
Helixi249 – 262Combined sources14
Turni263 – 265Combined sources3
Beta strandi266 – 268Combined sources3
Beta strandi271 – 273Combined sources3
Helixi276 – 286Combined sources11
Helixi297 – 307Combined sources11
Helixi310 – 318Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DPGX-ray2.84I/J/K/L1-48[»]
4YCUX-ray2.10C1-36[»]
4YCWX-ray2.90C/D/G/H1-36[»]
5A1NX-ray2.10B90-320[»]
5A34X-ray2.60B/D/F/H90-320[»]
5A5HX-ray2.32B/D/F/H90-320[»]
ProteinModelPortaliQ13155.
SMRiQ13155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini220 – 317GST C-terminalAdd BLAST98

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 162Interaction with PRKN1 PublicationAdd BLAST81
Regioni162 – 225Interaction with TP531 PublicationAdd BLAST64

Phylogenomic databases

eggNOGiENOG410II5D. Eukaryota.
ENOG4110B04. LUCA.
GeneTreeiENSGT00390000015826.
HOGENOMiHOG000233491.
InParanoidiQ13155.
KOiK15438.
OMAiRVELPTC.
OrthoDBiEOG091G0Q05.
PhylomeDBiQ13155.
TreeFamiTF326322.

Family and domain databases

InterProiView protein in InterPro
IPR031889. AIMP2_LysRS-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
PfamiView protein in Pfam
PF16780. AIMP2_LysRS_bd. 1 hit.
PF00043. GST_C. 1 hit.
SUPFAMiSSF47616. SSF47616. 1 hit.

Sequencei

Sequence statusi: Complete.

Q13155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMYQVKPYH GGGAPLRVEL PTCMYRLPNV HGRSYGPAPG AGHVQEESNL
60 70 80 90 100
SLQALESRQD DILKRLYELK AAVDGLSKMI QTPDADLDVT NIIQADEPTT
110 120 130 140 150
LTTNALDLNS VLGKDYGALK DIVINANPAS PPLSLLVLHR LLCEHFRVLS
160 170 180 190 200
TVHTHSSVKS VPENLLKCFG EQNKKQPRQD YQLGFTLIWK NVPKTQMKFS
210 220 230 240 250
IQTMCPIEGE GNIARFLFSL FGQKHNAVNA TLIDSWVDIA IFQLKEGSSK
260 270 280 290 300
EKAAVFRSMN SALGKSPWLA GNELTVADVV LWSVLQQIGG CSVTVPANVQ
310 320
RWMRSCENLA PFNTALKLLK
Length:320
Mass (Da):35,349
Last modified:January 11, 2001 - v2
Checksum:iF253726B63C12BAB
GO

Sequence cautioni

The sequence AAC50391 differs from that shown. Reason: Frameshift at position 312.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05839292I → V in a lung cancer cell line; reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication1
Natural variantiVAR_05839397 – 99EPT → DLS in a lung cancer cell line; no effect on proapoptotic activity. 3
Natural variantiVAR_025521129A → G1 PublicationCorresponds to variant dbSNP:rs17855441Ensembl.1
Natural variantiVAR_050125166L → I. Corresponds to variant dbSNP:rs34525431Ensembl.1
Natural variantiVAR_058394209G → S in a lung cancer cell line; no effect on proapoptotic activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24169 mRNA. Translation: AAC50391.1. Frameshift.
AC005995 Genomic DNA. Translation: AAS00389.1.
CH236963 Genomic DNA. Translation: EAL23713.1.
CH878731 Genomic DNA. Translation: EAW55053.1.
BC002853 mRNA. Translation: AAH02853.1.
BC010156 mRNA. Translation: AAH10156.1.
BC013630 mRNA. Translation: AAH13630.1.
AF116615 mRNA. Translation: AAF71039.1.
CCDSiCCDS5344.1.
RefSeqiNP_006294.2. NM_006303.3.
UniGeneiHs.301613.

Genome annotation databases

EnsembliENST00000223029; ENSP00000223029; ENSG00000106305.
GeneIDi7965.
KEGGihsa:7965.
UCSCiuc003spo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAIMP2_HUMAN
AccessioniPrimary (citable) accession number: Q13155
Secondary accession number(s): Q75MR1, Q96CZ5, Q9P1L2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: September 27, 2017
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references