CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005959
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 
Protein Synonyms/Alias
 Multisynthase complex auxiliary component p43; Endothelial monocyte-activating polypeptide 2; EMAP-2; Endothelial monocyte-activating polypeptide II; EMAP-II; Small inducible cytokine subfamily E member 1 
Gene Name
 Aimp1 
Gene Synonyms/Alias
 Emap2; Scye1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
35QVALLKEKAILQATMubiquitination[1]
63KKEIEELKQELILAEacetylation[2]
63KKEIEELKQELILAEubiquitination[1]
146AAASTDSKPIDASRLacetylation[3]
212VVLLCNLKPAKMRGVacetylation[4]
260AFPGEPDKELNPKKKacetylation[2, 3]
267KELNPKKKIWEQIQPacetylation[3]
267KELNPKKKIWEQIQPsuccinylation[3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1- mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7 (By similarity). 
Sequence Annotation
 DOMAIN 149 250 tRNA-binding.
 REGION 6 46 Required for fibroblast proliferation (By
 REGION 54 192 Interaction with HSP90B1.
 REGION 101 115 Required for endothelial cell death (By
 REGION 115 190 Required for endothelial cell migration  
Keyword
 Angiogenesis; Apoptosis; Carbohydrate metabolism; Cell adhesion; Complete proteome; Cytokine; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum; Glucose metabolism; Golgi apparatus; Inflammatory response; Nucleus; Protein biosynthesis; Reference proteome; RNA-binding; Secreted; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 310 AA 
Protein Sequence
MATNDAVLKR LEQKGAEADQ IIEYLKQQVA LLKEKAILQA TMREEKKLRV ENAKLKKEIE 60
ELKQELILAE IHNGVEQVRV RLSTPLQTNC TASESVVQSP SVATTASPAT KEQIKAGEEK 120
KVKEKTEKKG EKKEKQQSAA ASTDSKPIDA SRLDLRIGCI VTAKKHPDAD SLYVEEVDVG 180
EAAPRTVVSG LVNHVPLEQM QNRMVVLLCN LKPAKMRGVL SQAMVMCASS PEKVEILAPP 240
NGSVPGDRIT FDAFPGEPDK ELNPKKKIWE QIQPDLHTNA ECVATYKGAP FEVKGKGVCR 300
AQTMANSGIK 310 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:HGNC.
 GO:0009986; C:cell surface; ISS:BHF-UCL.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
 GO:0005125; F:cytokine activity; IDA:HGNC.
 GO:0042803; F:protein homodimerization activity; ISS:HGNC.
 GO:0000049; F:tRNA binding; ISS:HGNC.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007267; P:cell-cell signaling; IEA:Compara.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
 GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
 GO:0050900; P:leukocyte migration; IDA:HGNC.
 GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:HGNC.
 GO:0006412; P:translation; IEA:UniProtKB-KW. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR002547; tRNA-bd_dom. 
Pfam
 PF01588; tRNA_bind 
SMART
  
PROSITE
 PS50886; TRBD 
PRINTS