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Q13155

- AIMP2_HUMAN

UniProt

Q13155 - AIMP2_HUMAN

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
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: IntAct

    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

    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-SubCell

    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

    ArrayExpressiQ13155.
    BgeeiQ13155.
    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. 61 interactions.
    DIPiDIP-34421N.
    IntActiQ13155. 37 interactions.
    MINTiMINT-5002775.
    STRINGi9606.ENSP00000223029.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MPMYQVKPYH GGGAPLRVEL PTCMYRLPNV HGRSYGPAPG AGHVQEESNL    50
    SLQALESRQD DILKRLYELK AAVDGLSKMI QTPDADLDVT NIIQADEPTT 100
    LTTNALDLNS VLGKDYGALK DIVINANPAS PPLSLLVLHR LLCEHFRVLS 150
    TVHTHSSVKS VPENLLKCFG EQNKKQPRQD YQLGFTLIWK NVPKTQMKFS 200
    IQTMCPIEGE GNIARFLFSL FGQKHNAVNA TLIDSWVDIA IFQLKEGSSK 250
    EKAAVFRSMN SALGKSPWLA GNELTVADVV LWSVLQQIGG CSVTVPANVQ 300
    RWMRSCENLA PFNTALKLLK 320
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 61 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.
    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

    GeneWikii Multisynthetase_complex_auxiliary_component_p38.
    GenomeRNAii 7965.
    NextBioi 30485.
    PROi Q13155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13155.
    Bgeei Q13155.
    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

    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: October 1, 2014
    This is version 123 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