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Reviewed, UniProtKB/Swiss-Prot Q13155 (AIMP2_HUMAN)

Last modified November 24, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for assembly and stability of the aminoacyl-tRNA synthetase 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 TP53/p53. Functions as a proapoptotic factor. Ref.8

Subunit structure

Component of the aminoacyl-tRNA synthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and aspartyl-tRNA synthetases, 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 TP53/p53 (via N-terminus) in the nucleus following UV irradiation. Interacts (via N-terminus) with PARK2/parkin (via first RING-type domain). Ref.8 Ref.7 Ref.9

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity. Note: Following DNA damage, dissociates from the aminoacyl-tRNA synthetase 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.8

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.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Protein biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C19orf57Q0VDD73EBI-745226,EBI-741210

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320Aminoacyl tRNA synthetase 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.9
VAR_058392
Natural variant97 – 993EPT → DLS in a lung cancer cell line; no effect on proapoptotic activity.
VAR_058393
Natural variant1291A → G: dbSNP rs17855441. Ref.5
VAR_025521
Natural variant1661L → I: dbSNP rs34525431.
VAR_050125
Natural variant2091G → S in a lung cancer cell line; no effect on proapoptotic activity. Ref.9
VAR_058394

Experimental info

Mutagenesis163 – 1642EN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. Ref.9
Mutagenesis172 – 1732QN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q13155-1 [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: 8666379] [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: 12853948] [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: 12690205] [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: 15489334] [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]"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: 12819782] [Abstract]
Cited for: INTERACTION WITH FUBP1.
[8]"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: 16135753] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARK2, UBIQUITINATION.
[9]"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: 18695251] [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.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00011916.
RefSeqNP_006294.2.
UniGeneHs.301613
Hs.520205
Hs.632637

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ13155. 10 interactions.
STRINGQ13155.

PTM databases

PhosphoSiteQ13155.

Proteomic databases

PeptideAtlasQ13155.
PRIDEQ13155.

Genome annotation databases

EnsemblENST00000223029; ENSP00000223029; ENSG00000106305; Homo sapiens. [Genome view]
GeneID7965.
KEGGhsa:7965.
UCSCuc003spo.1. human.

Organism-specific databases

CTD7965.
GeneCardsGC07P006015.
H-InvDBHIX0006460.
HGNCHGNC:20609. AIMP2.
HPAHPA019098.
HPA020057.
MIM600859. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ13155.
HOVERGENQ13155.
OMALFGQKHN
OrthoDBEOG9QJV6T

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ13155.
BgeeQ13155.
GenevestigatorQ13155.
GermOnlineENSG00000106305. Homo sapiens.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
PROSITEPS50405. GST_CTER. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio30485.
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: November 24, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents