SCYE1

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1

PDB rendering based on 1e7z.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsAIMP1 ; EMAP2; EMAPII; HLD3; SCYE1; p43
External IDsOMIM: 603605 MGI: 102774 HomoloGene: 31260 GeneCards: AIMP1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez925513722
EnsemblENSG00000164022ENSMUSG00000028029
UniProtQ12904P31230
RefSeq (mRNA)NM_001142415NM_007926
RefSeq (protein)NP_001135887NP_031952
Location (UCSC)Chr 4:
107.24 – 107.27 Mb		Chr 3:
132.66 – 132.68 Mb
PubMed search

Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 is a protein that in humans is encoded by the AIMP1 gene.[1][2][3]

The protein encoded by this gene is a cytokine that may be induced by apoptosis and is also released from professional antigen-presenting cells such as dendritic cells. The release of this cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor of SCYE1 (pro-SCYE1) is identical to the p43 subunit, which is associated with the multiaminoacyl-tRNA synthetase complex (mARS). Pro-SCYE1 may function in binding RNA as part of the tRNA synthetase complex in normal cells and in stimulating inflammatory responses after proteolytic cleavage in tumor cells.[3] As an inflammatory cytokine, AIMp1/p43 has demonstrated the ability to skew T-helper polarization in the direction of Th-1, and its homozygous deletion leads to a hyper-polarized Th-2 phenotype.

Interactions

SCYE1 has been shown to interact with SMURF2.[4]

References

  1. ↑ Kao J, Houck K, Fan Y, Haehnel I, Libutti SK, Kayton ML, Grikscheit T, Chabot J, Nowygrod R, Greenberg S et al. (Nov 1994). "Characterization of a novel tumor-derived cytokine. Endothelial-monocyte activating polypeptide II". J Biol Chem 269 (40): 25106–19. PMID 7929199.
  2. ↑ Kao J, Fan YG, Haehnel I, Brett J, Greenberg S, Clauss M, Kayton M, Houck K, Kisiel W, Seljelid R et al. (May 1994). "A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response". J Biol Chem 269 (13): 9774–82. PMID 7545917.
  3. ↑ 3.0 3.1 "Entrez Gene: SCYE1 small inducible cytokine subfamily E, member 1 (endothelial monocyte-activating)".
  4. ↑ Lee, Yeon Sook; Han Jung Min; Son Sung Hwa; Choi Jin Woo; Jeon Eun Ju; Bae Suk-Chul; Park Young In; Kim Sunghoon (Jul 2008). "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2". Biochem. Biophys. Res. Commun. (United States) 371 (3): 395–400. doi:10.1016/j.bbrc.2008.04.099. PMID 18448069.

Further reading

  • Kao J, Ryan J, Brett G et al. (1992). "Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms". J. Biol. Chem. 267 (28): 20239–47. PMID 1400342.
  • Quevillon S, Agou F, Robinson JC, Mirande M (1998). "The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine". J. Biol. Chem. 272 (51): 32573–9. doi:10.1074/jbc.272.51.32573. PMID 9405472.
  • Quevillon S, Robinson JC, Berthonneau E et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
  • Park SG, Jung KH, Lee JS et al. (1999). "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". J. Biol. Chem. 274 (24): 16673–6. doi:10.1074/jbc.274.24.16673. PMID 10358004.
  • Kim Y, Shin J, Li R et al. (2000). "A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (35): 27062–8. doi:10.1074/jbc.C000216200. PMID 10852899.
  • Renault L, Kerjan P, Pasqualato S et al. (2001). "Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry". EMBO J. 20 (3): 570–8. doi:10.1093/emboj/20.3.570. PMC 133484. PMID 11157763.
  • Shalak V, Kaminska M, Mitnacht-Kraus R et al. (2001). "The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component". J. Biol. Chem. 276 (26): 23769–76. doi:10.1074/jbc.M100489200. PMID 11306575.
  • Chang SY, Park SG, Kim S, Kang CY (2002). "Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation". J. Biol. Chem. 277 (10): 8388–94. doi:10.1074/jbc.M108792200. PMID 11741979.
  • Battersby S, Boddy SC, Critchley HO, Jabbour HN (2002). "Expression and localization of endothelial monocyte-activating polypeptide II in the human endometrium across the menstrual cycle: regulation of expression by prostaglandin E(2)". J. Clin. Endocrinol. Metab. 87 (8): 3928–35. doi:10.1210/jc.87.8.3928. PMID 12161535.
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Park H, Park SG, Kim J et al. (2003). "Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43". Cytokine 20 (4): 148–53. doi:10.1006/cyto.2002.1992. PMID 12543078.
  • Ahn HC, Kim S, Lee BJ (2003). "Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43". FEBS Lett. 542 (1–3): 119–24. doi:10.1016/S0014-5793(03)00362-4. PMID 12729910.
  • Kim MJ, Park BJ, Kang YS et al. (2003). "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation". Nat. Genet. 34 (3): 330–6. doi:10.1038/ng1182. PMID 12819782.
  • Wolfe CL, Warrington JA, Davis S et al. (2004). "Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII". Protein Sci. 12 (10): 2282–90. doi:10.1110/ps.03147903. PMC 2366922. PMID 14500886.
  • Mueller CA, Schluesener HJ, Conrad S et al. (2004). "Spinal cord injury induces lesional expression of the proinflammatory and antiangiogenic cytokine EMAP II". J. Neurotrauma 20 (10): 1007–15. doi:10.1089/089771503770195858. PMID 14588117.
  • Murray JC, Symonds P, Ward W et al. (2004). "Colorectal cancer cells induce lymphocyte apoptosis by an endothelial monocyte-activating polypeptide-II-dependent mechanism". J. Immunol. 172 (1): 274–81. doi:10.4049/jimmunol.172.1.274. PMID 14688335.
  • Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Murray JC, Heng YM, Symonds P et al. (2004). "Endothelial monocyte-activating polypeptide-II (EMAP-II): a novel inducer of lymphocyte apoptosis". J. Leukoc. Biol. 75 (5): 772–6. doi:10.1189/jlb.1003487. PMID 14982944.