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)
End	36,272,157 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	24,834,632 bp
RNA expression pattern
	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
	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
	55034
	68591
	ENSG00000075643
	ENSMUSG00000039616
	Q96EN8
	Q14CH1
	NM_017947
	NM_026779
	NP_060417
	NP_081055
	Wikidata
View/Edit Human	View/Edit Mouse

Molybdenum cofactor sulfurase is an enzyme that in humans is encoded by the MOCOS gene.⁵⁶

MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH) and aldehyde oxidase (AOX1), which is required for their enzymatic activities.⁵

References

GRCh38: Ensembl release 89: ENSG00000075643 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000039616 – Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T (April 2001). "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II". Biochemical and Biophysical Research Communications. 282 (5): 1194–200. Bibcode:2001BBRC..282.1194I. doi:10.1006/bbrc.2001.4719. PMID 11302742.
"Entrez Gene: MOCOS molybdenum cofactor sulfurase".

Further reading

Maruyama K, Sugano S (January 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, Suyama A, Sugano S (October 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.
Yamamoto T, Moriwaki Y, Takahashi S, Tsutsumi Z, Tuneyoshi K, Matsui K, et al. (November 2003). "Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II". Metabolism. 52 (11): 1501–4. doi:10.1016/s0026-0495(03)00272-5. PMID 14624414.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
Peretz H, Naamati MS, Levartovsky D, Lagziel A, Shani E, Horn I, et al. (May 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". Molecular Genetics and Metabolism. 91 (1): 23–9. doi:10.1016/j.ymgme.2007.02.005. PMID 17368066.