1euj

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<StructureSection load='1euj' size='340' side='right'caption='[[1euj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1euj' size='340' side='right'caption='[[1euj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1euj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EUJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1euj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUJ FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1euj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euj OCA], [http://pdbe.org/1euj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1euj RCSB], [http://www.ebi.ac.uk/pdbsum/1euj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1euj ProSAT]</span></td></tr>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1euj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euj OCA], [https://pdbe.org/1euj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1euj RCSB], [https://www.ebi.ac.uk/pdbsum/1euj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1euj ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[http://omim.org/entry/260600 260600]]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>
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[[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[https://omim.org/entry/260600 260600]]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] 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.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>
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[[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] 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.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 06:32, 11 August 2021

A NOVEL ANTI-TUMOR CYTOKINE CONTAINS A RNA-BINDING MOTIF PRESENT IN AMINOACYL-TRNA SYNTHETASES

PDB ID 1euj

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