SCYE1

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

AIMP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1E7Z, 1EUJ, 1FL0, 4R3Z
Identifiers
Aliases	AIMP1, EMAP2, EMAPII, HLD3, SCYE1, p43, aminoacyl tRNA synthetase complex interacting multifunctional protein 1
External IDs	OMIM: 603605; MGI: 102774; HomoloGene: 31260; GeneCards: AIMP1; OMA:AIMP1 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q24 Start 106,315,544 bp End 106,349,456 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 G3 Start 132,366,242 bp End 132,390,131 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon rectum thoracic diaphragm endometrium monocyte gastrocnemius muscle islet of Langerhans cartilage tissue beta cell Descending thoracic aorta Top expressed in somite maxillary prominence mandibular prominence primitive streak epiblast hair follicle plantaris muscle renal corpuscle extensor digitorum longus muscle medullary collecting duct More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein binding RNA binding GTPase binding tRNA binding cytokine activity Cellular component Golgi apparatus membrane aminoacyl-tRNA synthetase multienzyme complex transport vesicle extracellular region cell surface endoplasmic reticulum cytoplasmic vesicle nucleus methionyl glutamyl tRNA synthetase complex extracellular space cytoplasm cytosol Biological process blood vessel morphogenesis protein biosynthesis cell-cell signaling negative regulation of endothelial cell proliferation chemotaxis cell adhesion defense response to virus response to wounding angiogenesis glucose metabolic process leukocyte migration signal transduction apoptotic process tRNA aminoacylation for protein translation inflammatory response carbohydrate metabolic process regulation of signaling receptor activity positive regulation of glucagon secretion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9255 13722 Ensembl ENSG00000164022 ENSMUSG00000028029 UniProt Q12904 P31230 RefSeq (mRNA) NM_004757 NM_001142415 NM_001142416 NM_007926 NM_001368626 RefSeq (protein) NP_001135887 NP_001135888 NP_004748 NP_001355555 NP_031952 Location (UCSC) Chr 4: 106.32 – 106.35 Mb Chr 3: 132.37 – 132.39 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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. 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.

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. doi:10.1016/S0021-9258(19)88692-1. 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. S2CID 34057814.
• 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. S2CID 25940947.
• 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. S2CID 20768076.
• 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/jcem.87.8.8719. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 31844938.
• 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. S2CID 39222196.
• 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. S2CID 41006480.
• 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. S2CID 7939914.
• 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. S2CID 21903526.
• 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. S2CID 31089927.