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UBA4 Uba4p

MOCS3, Uba4, Uba4p
Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase). The protein encoded by this gene adenylates and activates MPT synthase. This gene contains no introns. A pseudogene of this gene is present on chromosome 14. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Urm1, Ubiquitin, CAN, Gephyrin, ACID
Papers using MOCS3 antibodies
The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
Suzuki Tsutomu et al., In Nucleic Acids Research, 1996
... A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis ...
Papers on MOCS3
Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man.
Schaffrath et al., Kassel, Germany. In Febs Lett, May 2015
The ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways.
Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans.
Leimkühler et al., Potsdam, Germany. In J Biol Chem, 2015
The studies showed that TUM1 interacts with the l-cysteine desulfurase NFS1 and the rhodanese-like protein MOCS3, suggesting a dual function of TUM1 both in sulfur transfer for the biosynthesis of the molybdenum cofactor, and for the thiolation of tRNA.
Loss of anticodon wobble uridine modifications affects tRNA(Lys) function and protein levels in Saccharomyces cerevisiae.
Schaffrath et al., Kassel, Germany. In Plos One, 2014
While mutations in subunits of the Elongator complex (Elp1-Elp6), which disable mcm5 side chain formation, or removal of components of the thiolation pathway (Ncs2/Ncs6, Urm1, Uba4) are individually tolerated, the combination of both modification defects has been reported to have lethal effects on Saccharomyces cerevisiae.
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
Leimkühler et al., Potsdam, Germany. In Plos One, 2012
We have previously demonstrated that purified NFS1 is able to transfer sulfur to the C-terminal domain of MOCS3, a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation.
Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.
Leimkühler et al., Potsdam, Germany. In J Biol Chem, 2012
extension of the C terminus with an additional glycine of MOCS2A and URM1 altered the localization of MOCS3 from the cytosol to the nucleus.
The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier.
Ji et al., Shanghai, China. In Protein Cell, 2011
The ubiquitin-related modifier Urm1 can be covalently conjugated to lysine residues of other proteins, such as yeast Ahp1 and human MOCS3, through a mechanism involving the E1-like protein Uba4 (MOCS3 in humans).
Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.
Jentsch et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2011
First, Urm1 is appended to lysine residues of three components that function in its own pathway (i.e., MOCS3, ATPBD3, and CTU2).
Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegans.
Han et al., Boulder, United States. In Genetics, 2010
In yeast, the ELP complex has been shown to genetically interact with Uba4p/Urm1p and Kti11-13p for a function in tRNA modification.
Functional deficiencies of sulfite oxidase: Differential diagnoses in neonates presenting with intractable seizures and cystic encephalomalacia.
Camelo Junior et al., Freiburg, Germany. In Brain Dev, 2010
Defects in the synthesis of the molybdenum cofactor are caused by mutations in one of the genes MOCS1, MOCS2, MOCS3 and GEPH and result in combined deficiencies of the enzymes sulfite oxidase, xanthine dehydrogenase and aldehyde oxidase.
Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA.
Peter et al., Zürich, Switzerland. In Nature, 2009
Moreover, we identify Uba4p, Ncs2p, Ncs6p and Yor251cp as components of this conserved pathway.
Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions.
Suzuki et al., Tokyo, Japan. In Nucleic Acids Res, 2009
We have identified five genes in Saccharomyces cerevisiae, YIL008w (URM1), YHR111w (UBA4), YOR251c (TUM1), YNL119w (NCS2) and YGL211w (NCS6), that are required for 2-thiolation of mcm(5)s(2)U.
Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.
Hayashi et al., Takatsuki, Japan. In J Biol Chem, 2008
ubiquitin-like protein Urm1 and ubiquitin-activating enzyme-like protein Uba4, as well as Tuc1 and Tuc2, were strictly required for tRNA thio-modification
A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae.
Byström et al., Umeå, Sweden. In Rna, 2008
In addition to earlier described mutants, formation of the s(2) group was also abolished in urm1, uba4, and ncs2 mutants and decreased in the yor251c mutant.
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.
Leimkühler et al., Potsdam, Germany. In J Biol Chem, 2008
Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins.
Leimkühler et al., Potsdam, Germany. In Biochemistry, 2008
The UBA4-URM1 system represents the evolutionary link between protein conjugation and protein modification by sulfur carrier proteins.
Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs.
Leimkühler et al., Potsdam, Germany. In Febs J, 2007
in humans & most eukaryotes thiosulfate is not physiologic sulfur donor for MOCS3, whereas in bacterial homologs, which have arginine at last position of active site loop, thiosulfate can be used as a sulfur source for molybdenum cofactor biosynthesis.
Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH.
Johnson et al., Göttingen, Germany. In Hum Mutat, 2003
The cofactor is an unstable reduced pterin with a unique four-carbon side chain, synthesized by a complex pathway that requires the products of at least four different genes (MOCS1, MOCS2, MOCS3, and GEPH).
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