CPLM-011941

Genbank Nucleotide ID

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

Homo sapiens (Human)

Position	Peptide	Type	References
24	IFCRLLAKMANNDAV	ubiquitination	[1, 2, 3, 4, 5, 6, 7]

[1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] 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]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] 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]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[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.

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.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR012340; NA-bd_OB-fold.
IPR002547; tRNA-bd_dom.