SCYE1: Difference between revisions

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*{{cite journal  |author1=Chang SY |author2=Park SG |author3=Kim S |author4=Kang CY |title=Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8388–94 |year= 2002 |pmid= 11741979 |doi= 10.1074/jbc.M108792200 }}
*{{cite journal  |author1=Chang SY |author2=Park SG |author3=Kim S |author4=Kang CY |title=Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8388–94 |year= 2002 |pmid= 11741979 |doi= 10.1074/jbc.M108792200 }}
*{{cite journal  |author1=Battersby S |author2=Boddy SC |author3=Critchley HO |author4=Jabbour HN |title=Expression and localization of endothelial monocyte-activating polypeptide II in the human endometrium across the menstrual cycle: regulation of expression by prostaglandin E(2) |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 8 |pages= 3928–35 |year= 2002 |pmid= 12161535 |doi=10.1210/jc.87.8.3928  }}
*{{cite journal  |author1=Battersby S |author2=Boddy SC |author3=Critchley HO |author4=Jabbour HN |title=Expression and localization of endothelial monocyte-activating polypeptide II in the human endometrium across the menstrual cycle: regulation of expression by prostaglandin E(2) |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 8 |pages= 3928–35 |year= 2002 |pmid= 12161535 |doi=10.1210/jc.87.8.3928  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=Park H, Park SG, Kim J, etal |title=Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43 |journal=Cytokine |volume=20 |issue= 4 |pages= 148–53 |year= 2003 |pmid= 12543078 |doi=10.1006/cyto.2002.1992  }}
*{{cite journal  |vauthors=Park H, Park SG, Kim J, etal |title=Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43 |journal=Cytokine |volume=20 |issue= 4 |pages= 148–53 |year= 2003 |pmid= 12543078 |doi=10.1006/cyto.2002.1992  }}
*{{cite journal  |author1=Ahn HC |author2=Kim S |author3=Lee BJ |title=Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43 |journal=FEBS Lett. |volume=542 |issue= 1–3 |pages= 119–24 |year= 2003 |pmid= 12729910 |doi=10.1016/S0014-5793(03)00362-4  }}
*{{cite journal  |author1=Ahn HC |author2=Kim S |author3=Lee BJ |title=Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43 |journal=FEBS Lett. |volume=542 |issue= 1–3 |pages= 119–24 |year= 2003 |pmid= 12729910 |doi=10.1016/S0014-5793(03)00362-4  }}

Latest revision as of 12:00, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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