CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011940
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9ANNDAVLKRLEQKGAubiquitination[1]
26DQIIEYLKQQVSLLKubiquitination[2]
33KQQVSLLKEKAILQAacetylation[3]
33KQQVSLLKEKAILQAubiquitination[4]
35QVSLLKEKAILQATLubiquitination[1]
148IAGSADSKPIDVSRLacetylation[5]
262AFPGEPDKELNPKKKacetylation[5]
312TMSNSGIK*******ubiquitination[6, 7]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
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. 
Sequence Annotation
 DOMAIN 151 252 tRNA-binding.
 REGION 6 46 Required for fibroblast proliferation.
 REGION 54 194 Interaction with HSP90B1 (By similarity).
 REGION 101 114 Required for endothelial cell death.
 REGION 114 192 Required for endothelial cell migration.  
Keyword
 3D-structure; Alternative splicing; Angiogenesis; Apoptosis; Carbohydrate metabolism; Cell adhesion; Complete proteome; Cytokine; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Glucose metabolism; Golgi apparatus; Inflammatory response; Leukodystrophy; Nucleus; Polymorphism; Protein biosynthesis; Reference proteome; RNA-binding; Secreted; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 312 AA 
Protein Sequence
MANNDAVLKR LEQKGAEADQ IIEYLKQQVS LLKEKAILQA TLREEKKLRV ENAKLKKEIE 60
ELKQELIQAE IQNGVKQIPF PSGTPLHANS MVSENVIQST AVTTVSSGTK EQIKGGTGDE 120
KKAKEKIEKK GEKKEKKQQS IAGSADSKPI DVSRLDLRIG CIITARKHPD ADSLYVEEVD 180
VGEIAPRTVV SGLVNHVPLE QMQNRMVILL CNLKPAKMRG VLSQAMVMCA SSPEKIEILA 240
PPNGSVPGDR ITFDAFPGEP DKELNPKKKI WEQIQPDLHT NDECVATYKG VPFEVKGKGV 300
CRAQTMSNSG IK 312 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:HGNC.
 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; TAS:ProtInc.
 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; ISS:HGNC.
 GO:0042803; F:protein homodimerization activity; IDA:HGNC.
 GO:0000049; F:tRNA binding; IDA: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; IDA:HGNC.
 GO:0006935; P:chemotaxis; TAS:ProtInc.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
 GO:0006954; P:inflammatory response; TAS:ProtInc.
 GO:0050900; P:leukocyte migration; IDA:HGNC.
 GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:HGNC.
 GO:0007165; P:signal transduction; NAS:ProtInc.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR002547; tRNA-bd_dom. 
Pfam
 PF01588; tRNA_bind 
SMART
  
PROSITE
 PS50886; TRBD 
PRINTS