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Q13155 (AIMP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Alternative name(s):
Multisynthase complex auxiliary component p38
Protein JTV-1
Gene names
Name:AIMP2
Synonyms:JTV1
ORF Names:PRO0992
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for assembly and stability of the aminoacyl-tRNA synthase complex. 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. Ref.10

Subunit structure

Component of the aminoacyl-tRNA synthase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18, AIMP2/p38 and AIMP1/p43. 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 KARS and PARK2/parkin (via first RING-type domain). Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity. Note: Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus By similarity.

Post-translational modification

Phosphorylated on serine residues in response to UV irradiation By similarity.

Ubiquitinated by PARK2, leading to its degradation by the proteasome. Mutant PARK2 fails to ubiquitinate AIMP2 efficiently, allowing its accumulation which may contribute to neurodegeneration associated with Parkinson disease. Ref.10

Miscellaneous

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

Sequence similarities

Contains 1 GST C-terminal domain.

Sequence caution

The sequence AAC50391.1 differs from that shown. Reason: Frameshift at position 312.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C19orf57Q0VDD75EBI-745226,EBI-741210
FUBP1Q96AE44EBI-745226,EBI-711404
gagP045913EBI-745226,EBI-6179719From a different organism.
KARSQ150463EBI-745226,EBI-356367

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
PRO_0000221129

Regions

Domain220 – 31798GST C-terminal
Region82 – 16281Interaction with PARK2
Region162 – 22564Interaction with TP53

Natural variations

Natural variant921I → V in a lung cancer cell line; reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. Ref.12
VAR_058392
Natural variant97 – 993EPT → DLS in a lung cancer cell line; no effect on proapoptotic activity.
VAR_058393
Natural variant1291A → G. Ref.5
Corresponds to variant rs17855441 [ dbSNP | Ensembl ].
VAR_025521
Natural variant1661L → I.
Corresponds to variant rs34525431 [ dbSNP | Ensembl ].
VAR_050125
Natural variant2091G → S in a lung cancer cell line; no effect on proapoptotic activity. Ref.12
VAR_058394

Experimental info

Mutagenesis163 – 1642EN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. Ref.12
Mutagenesis172 – 1732QN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Q13155 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: F253726B63C12BAB

FASTA32035,349
        10         20         30         40         50         60 
MPMYQVKPYH GGGAPLRVEL PTCMYRLPNV HGRSYGPAPG AGHVQEESNL SLQALESRQD 

        70         80         90        100        110        120 
DILKRLYELK AAVDGLSKMI QTPDADLDVT NIIQADEPTT LTTNALDLNS VLGKDYGALK 

       130        140        150        160        170        180 
DIVINANPAS PPLSLLVLHR LLCEHFRVLS TVHTHSSVKS VPENLLKCFG EQNKKQPRQD 

       190        200        210        220        230        240 
YQLGFTLIWK NVPKTQMKFS IQTMCPIEGE GNIARFLFSL FGQKHNAVNA TLIDSWVDIA 

       250        260        270        280        290        300 
IFQLKEGSSK EKAAVFRSMN SALGKSPWLA GNELTVADVV LWSVLQQIGG CSVTVPANVQ 

       310        320 
RWMRSCENLA PFNTALKLLK 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the 5' region of PMS2 reveals heterogeneous transcripts and a novel overlapping gene."
Nicolaides N.C., Kinzler K.W., Vogelstein B.
Genomics 29:329-334(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-129.
Tissue: Lymph and Placenta.
[6]"Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-320.
Tissue: Fetal liver.
[7]"Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein."
Quevillon S., Robinson J.-C., Berthonneau E., Siatecka M., Mirande M.
J. Mol. Biol. 285:183-195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KARS.
[8]"Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation."
Kim M.J., Park B.-J., Kang Y.-S., Kim H.J., Park J.-H., Kang J.W., Lee S.W., Han J.M., Lee H.-W., Kim S.
Nat. Genet. 34:330-336(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FUBP1.
[9]"Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly."
Halwani R., Cen S., Javanbakht H., Saadatmand J., Kim S., Shiba K., Kleiman L.
J. Virol. 78:7553-7564(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KARS.
[10]"Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death."
Ko H.S., von Coelln R., Sriram S.R., Kim S.W., Chung K.K.K., Pletnikova O., Troncoso J., Johnson B., Saffary R., Goh E.L., Song H., Park B.-J., Kim M.J., Kim S., Dawson V.L., Dawson T.M.
J. Neurosci. 25:7968-7978(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARK2, UBIQUITINATION.
[11]"Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro."
Guzzo C.M., Yang D.C.H.
Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KARS.
[12]"AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53."
Han J.M., Park B.-J., Park S.G., Oh Y.S., Choi S.J., Lee S.W., Hwang S.-K., Chang S.-H., Cho M.-H., Kim S.
Proc. Natl. Acad. Sci. U.S.A. 105:11206-11211(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53, VARIANTS VAL-92; 97-ASP--SER-99 AND SER-209, MUTAGENESIS OF 163-GLU-ASN-164 AND 172-GLN-ASN-173.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006294.2. NM_006303.3.
UniGeneHs.301613.
Hs.520205.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DPGX-ray2.84I/J/K/L1-48[»]
ProteinModelPortalQ13155.
SMRQ13155. Positions 2-32.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113684. 64 interactions.
DIPDIP-34421N.
IntActQ13155. 37 interactions.
MINTMINT-5002775.
STRING9606.ENSP00000223029.

PTM databases

PhosphoSiteQ13155.

Proteomic databases

PaxDbQ13155.
PeptideAtlasQ13155.
PRIDEQ13155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223029; ENSP00000223029; ENSG00000106305.
GeneID7965.
KEGGhsa:7965.
UCSCuc003spo.3. human.

Organism-specific databases

CTD7965.
GeneCardsGC07P006016.
HGNCHGNC:20609. AIMP2.
HPAHPA019098.
HPA020057.
MIM600859. gene.
neXtProtNX_Q13155.
PharmGKBPA165617609.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72943.
HOGENOMHOG000233491.
InParanoidQ13155.
KOK15438.
OMATNIIQAD.
OrthoDBEOG70PC0D.
PhylomeDBQ13155.
TreeFamTF326322.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ13155.
BgeeQ13155.
GenevestigatorQ13155.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
ProtoNetSearch...

Other

GeneWikiMultisynthetase_complex_auxiliary_component_p38.
GenomeRNAi7965.
NextBio30485.
PROQ13155.
SOURCESearch...

Entry information

Entry nameAIMP2_HUMAN
AccessionPrimary (citable) accession number: Q13155
Secondary accession number(s): Q75MR1, Q96CZ5, Q9P1L2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM