MOCOS

MOCOS
Identifiers
Aliases	MOCOS, hMCS, MCS, MOS, molybdenum cofactor sulfurase
External IDs	OMIM: 613274; MGI: 1915841; HomoloGene: 9931; GeneCards: MOCOS; OMA:MOCOS - orthologs
Gene location (Human) Chr. Chromosome 18 (human) Band 18q12.2 Start 36,187,497 bp End 36,272,157 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 A2 Start 24,786,748 bp End 24,834,632 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte right lobe of liver palpebral conjunctiva right adrenal gland right adrenal cortex jejunal mucosa left adrenal gland left adrenal cortex buccal mucosa cell duodenum Top expressed in granulocyte left lobe of liver esophagus primary oocyte jejunum gastrula respiratory epithelium olfactory system olfactory epithelium duodenum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity molybdenum ion binding pyridoxal phosphate binding protein binding catalytic activity Mo-molybdopterin cofactor sulfurase activity molybdenum cofactor sulfurtransferase activity lyase activity Cellular component cytosol cellular component Biological process Mo-molybdopterin cofactor biosynthetic process molybdopterin cofactor biosynthetic process molybdopterin cofactor metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 55034 68591 Ensembl ENSG00000075643 ENSMUSG00000039616 UniProt Q96EN8 Q14CH1 RefSeq (mRNA) NM_017947 NM_026779 RefSeq (protein) NP_060417 NP_081055 Location (UCSC) Chr 18: 36.19 – 36.27 Mb Chr 18: 24.79 – 24.83 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene.

MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde oxidase (AOX1), which is required for their enzymatic activities.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Strausberg RL, Feingold EA, Grouse LH (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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Yamamoto T, Moriwaki Y, Takahashi S (2003). "Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II". Metab. Clin. Exp. 52 (11): 1501–4. doi:10.1016/s0026-0495(03)00272-5. PMID 14624414.
• Beausoleil SA, Jedrychowski M, Schwartz D (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Gerhard DS, Wagner L, Feingold EA (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.
• Beausoleil SA, Villén J, Gerber SA (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Peretz H, Naamati MS, Levartovsky D (2007). "Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the Human Molybdenum Cofactor Sulfurase (HMCS) associated with type II classical xanthinuria". Mol. Genet. Metab. 91 (1): 23–9. doi:10.1016/j.ymgme.2007.02.005. PMID 17368066.