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MOCS3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3I2V
Identifiers
Aliases	MOCS3, UBA4, molybdenum cofactor synthesis 3
External IDs	OMIM: 609277; MGI: 1916622; HomoloGene: 6108; GeneCards: MOCS3; OMA:MOCS3 - orthologs
Gene location (Human) Chr. Chromosome 20 (human) Band 20q13.13 Start 50,958,818 bp End 50,963,929 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 H3 Start 168,072,542 bp End 168,074,514 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm testicle stromal cell of endometrium gonad ventricular zone ganglionic eminence islet of Langerhans gastrocnemius muscle nasal epithelium prefrontal cortex Top expressed in seminiferous tubule spermatid spermatocyte muscle of thigh right kidney granulocyte embryo primary visual cortex proximal tubule mesenteric lymph nodes More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding thiosulfate sulfurtransferase activity molybdopterin-synthase sulfurtransferase activity metal ion binding URM1 activating enzyme activity protein binding catalytic activity ubiquitin-like modifier activating enzyme activity ATP binding molybdopterin-synthase adenylyltransferase activity nucleotidyltransferase activity sulfurtransferase activity Cellular component cytoplasm cytosol Biological process molybdopterin cofactor biosynthetic process tRNA processing Mo-molybdopterin cofactor biosynthetic process metabolism tRNA wobble uridine modification tRNA thio-modification tRNA wobble position uridine thiolation protein urmylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27304 69372 Ensembl ENSG00000124217 ENSMUSG00000074576 UniProt O95396 A2BDX3 RefSeq (mRNA) NM_014484 NM_001160330 RefSeq (protein) NP_055299 NP_001153802 Location (UCSC) Chr 20: 50.96 – 50.96 Mb Chr 2: 168.07 – 168.07 Mb PubMed search
Wikidata
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Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene.

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, encoded by MOCS2/Mocs2 in mammals). 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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000124217 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000074576 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Matthies A, Nimtz M, Leimkuhler S (May 2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20. doi:10.1021/bi0503448. PMID 15910006.
6. ^ "Entrez Gene: MOCS3 molybdenum cofactor synthesis 3".

Further reading

• Reiss J, Johnson JL (2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH". Hum. Mutat. 21 (6): 569–76. doi:10.1002/humu.10223. PMID 12754701. S2CID 41013043.
• Johnson JL, Coyne KE, Rajagopalan KV, et al. (2002). "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency". Am. J. Med. Genet. 104 (2): 169–73. doi:10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8. PMID 11746050.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
• Cortese MS, Caplan AB, Crawford RL (2003). "Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)". BMC Evol. Biol. 2: 8. doi:10.1186/1471-2148-2-8. PMC 115864. PMID 11972321.
• 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.
• Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5946–51. Bibcode:2004PNAS..101.5946M. doi:10.1073/pnas.0308191101. PMC 395903. PMID 15073332.
• Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Krepinsky K, Leimkühler S (2007). "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". FEBS J. 274 (11): 2778–87. doi:10.1111/j.1742-4658.2007.05811.x. PMID 17459099. S2CID 82541137.

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