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Q13155

- AIMP2_HUMAN

UniProt

Q13155 - AIMP2_HUMAN

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Protein

Aminoacyl tRNA synthase complex-interacting multifunctional protein 2

Gene

AIMP2

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

Functioni

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.1 Publication

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. negative regulation of cell proliferation Source: Ensembl
  4. positive regulation of protein ubiquitination Source: Ensembl
  5. tRNA aminoacylation for protein translation Source: Reactome
  6. Type II pneumocyte differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_15306. 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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:20609. AIMP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1642EN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication
Mutagenesisi172 – 1732QN → AA: Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication

Organism-specific databases

PharmGKBiPA165617609.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Aminoacyl tRNA synthase complex-interacting multifunctional protein 2PRO_0000221129Add
BLAST

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13155.
PaxDbiQ13155.
PeptideAtlasiQ13155.
PRIDEiQ13155.

PTM databases

PhosphoSiteiQ13155.

Expressioni

Gene expression databases

BgeeiQ13155.
ExpressionAtlasiQ13155. baseline and differential.
GenevestigatoriQ13155.

Organism-specific databases

HPAiHPA019098.
HPA020057.

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113684. 62 interactions.
DIPiDIP-34421N.
IntActiQ13155. 37 interactions.
MINTiMINT-5002775.
STRINGi9606.ENSP00000223029.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DPGX-ray2.84I/J/K/L1-48[»]
ProteinModelPortaliQ13155.
SMRiQ13155. Positions 2-32.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 31798GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 16281Interaction with PARK2Add
BLAST
Regioni162 – 22564Interaction with TP53Add
BLAST

Sequence similaritiesi

Contains 1 GST C-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG72943.
GeneTreeiENSGT00390000015826.
HOGENOMiHOG000233491.
InParanoidiQ13155.
KOiK15438.
OMAiTNIIQAD.
OrthoDBiEOG70PC0D.
PhylomeDBiQ13155.
TreeFamiTF326322.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
[Graphical view]
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 AAC50391.1 differs from that shown. Reason: Frameshift at position 312. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921I → V in a lung cancer cell line; reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity. 1 Publication
VAR_058392
Natural varianti97 – 993EPT → DLS in a lung cancer cell line; no effect on proapoptotic activity.
VAR_058393
Natural varianti129 – 1291A → G.1 Publication
Corresponds to variant rs17855441 [ dbSNP | Ensembl ].
VAR_025521
Natural varianti166 – 1661L → I.
Corresponds to variant rs34525431 [ dbSNP | Ensembl ].
VAR_050125
Natural varianti209 – 2091G → S in a lung cancer cell line; no effect on proapoptotic activity. 1 Publication
VAR_058394

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.
Hs.520205.

Genome annotation databases

EnsembliENST00000223029; ENSP00000223029; ENSG00000106305.
GeneIDi7965.
KEGGihsa:7965.
UCSCiuc003spo.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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 .
CCDSi CCDS5344.1.
RefSeqi NP_006294.2. NM_006303.3.
UniGenei Hs.301613.
Hs.520205.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DPG X-ray 2.84 I/J/K/L 1-48 [» ]
ProteinModelPortali Q13155.
SMRi Q13155. Positions 2-32.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113684. 62 interactions.
DIPi DIP-34421N.
IntActi Q13155. 37 interactions.
MINTi MINT-5002775.
STRINGi 9606.ENSP00000223029.

PTM databases

PhosphoSitei Q13155.

Proteomic databases

MaxQBi Q13155.
PaxDbi Q13155.
PeptideAtlasi Q13155.
PRIDEi Q13155.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000223029 ; ENSP00000223029 ; ENSG00000106305 .
GeneIDi 7965.
KEGGi hsa:7965.
UCSCi uc003spo.3. human.

Organism-specific databases

CTDi 7965.
GeneCardsi GC07P006016.
HGNCi HGNC:20609. AIMP2.
HPAi HPA019098.
HPA020057.
MIMi 600859. gene.
neXtProti NX_Q13155.
PharmGKBi PA165617609.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72943.
GeneTreei ENSGT00390000015826.
HOGENOMi HOG000233491.
InParanoidi Q13155.
KOi K15438.
OMAi TNIIQAD.
OrthoDBi EOG70PC0D.
PhylomeDBi Q13155.
TreeFami TF326322.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi AIMP2. human.
GeneWikii Multisynthetase_complex_auxiliary_component_p38.
GenomeRNAii 7965.
NextBioi 30485.
PROi Q13155.
SOURCEi Search...

Gene expression databases

Bgeei Q13155.
ExpressionAtlasi Q13155. baseline and differential.
Genevestigatori Q13155.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
[Graphical view ]
Pfami PF14497. GST_C_3. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAIMP2_HUMAN
AccessioniPrimary (citable) accession number: Q13155
Secondary accession number(s): Q75MR1, Q96CZ5, Q9P1L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: November 26, 2014
This is version 125 of the entry and version 2 of the sequence. [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

Miscellaneous

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

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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3