Details for: AIMP1

Gene ID: 9255

Symbol: AIMP1

Ensembl ID: ENSG00000164022

Description: aminoacyl tRNA synthetase complex interacting multifunctional protein 1

Associated with

Other Information

Genular Protein ID: 1297069949

Symbol: AIMP1_HUMAN

Name: Aminoacyl tRNA synthase complex-interacting multifunctional protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7929199

Title: Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II.

PubMed ID: 7929199

DOI: 10.1016/s0021-9258(17)31505-3

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 24312579

Title: Reinvestigation of aminoacyl-tRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex.

PubMed ID: 24312579

DOI: 10.1371/journal.pone.0081734

PubMed ID: 10358004

Title: Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase.

PubMed ID: 10358004

DOI: 10.1074/jbc.274.24.16673

PubMed ID: 10850427

Title: Prostate adenocarcinoma cells release the novel proinflammatory polypeptide EMAP-II in response to stress.

PubMed ID: 10850427

PubMed ID: 11306575

Title: The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component.

PubMed ID: 11306575

DOI: 10.1074/jbc.m100489200

PubMed ID: 12237313

Title: Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis.

PubMed ID: 12237313

DOI: 10.1074/jbc.m207934200

PubMed ID: 11818442

Title: Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase-associated factor, p43: identification of the related adhesion molecules and signal pathways.

PubMed ID: 11818442

PubMed ID: 14500886

Title: Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII.

PubMed ID: 14500886

DOI: 10.1110/ps.03147903

PubMed ID: 16472771

Title: Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1.

PubMed ID: 16472771

DOI: 10.1016/j.bbrc.2006.01.117

PubMed ID: 17443684

Title: Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines.

PubMed ID: 17443684

DOI: 10.1002/jcp.21083

PubMed ID: 19362550

Title: Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome.

PubMed ID: 19362550

DOI: 10.1016/j.yexcr.2009.03.021

PubMed ID: 19131329

Title: Dissection of the structural organization of the aminoacyl-tRNA synthetase complex.

PubMed ID: 19131329

DOI: 10.1074/jbc.m809636200

PubMed ID: 19289464

Title: Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells.

PubMed ID: 19289464

DOI: 10.1074/jbc.m900480200

PubMed ID: 21092922

Title: Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous mutation.

PubMed ID: 21092922

DOI: 10.1016/j.ajhg.2010.10.016

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 10852899

Title: A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases.

PubMed ID: 10852899

DOI: 10.1074/jbc.c000216200

PubMed ID: 11157763

Title: Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry.

PubMed ID: 11157763

DOI: 10.1093/emboj/20.3.570

PubMed ID: 25288775

Title: Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.

PubMed ID: 25288775

DOI: 10.1073/pnas.1408836111

Sequence Information:

  • Length: 312
  • Mass: 34353
  • Checksum: 5F0BF73E58810C60
  • Sequence:
  • MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 
    ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 
    KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD 
    VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA 
    PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 
    CRAQTMSNSG IK

Genular Protein ID: 2569808679

Symbol: B4DNK3_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 269
  • Mass: 29745
  • Checksum: E96411349E003198
  • Sequence:
  • MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 
    ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 
    KKAKEKIEKK GEKKEKKQQS IAPRTVVSGL VNHVPLEQMQ NRMVILLCNL KPAKMRGVLS 
    QAMVMCASSP EKIEILAPPN GSVPGDRITF DAFPGEPDKE LNPKKKIWEQ IQPDLHTNDE 
    CVATYKGVPF EVKGKGVCRA QTMSNSGIK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.