MOCS1

MOCS1

Identifiers

MOCS1, MIG11, MOCOD, MOCODA, molybdenum cofactor synthesis 1, MOCS1A, MOCS1B

External IDs

OMIM: 603707 HomoloGene: 129502 GeneCards: MOCS1

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p21.2	Start	39,899,578 bp^[1]
Band	6p21.2	End	39,934,551 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

popliteal artery

right lung

pancreatic ductal cell

right lobe of liver

subcutaneous adipose tissue

gastrocnemius muscle

tibial nerve

left ventricle

left coronary artery

upper lobe of left lung

n/a

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	metal ion binding nucleotide binding 4 iron, 4 sulfur cluster binding catalytic activity lyase activity GTP binding iron-sulfur cluster binding GTP 3',8'-cyclase activity cyclic pyranopterin monophosphate synthase activity
Cellular component	molybdopterin synthase complex cytosol nucleus
Biological process	Mo-molybdopterin cofactor biosynthetic process molybdopterin cofactor biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


4337


n/a

Ensembl


ENSG00000124615


n/a

UniProt


Q9NZB8


n/a

RefSeq (mRNA)

NM_001075098 NM_005942 NM_005943 NM_138928 NM_001358529
NM_001358530 NM_001358531 NM_001358533 NM_001358534


n/a

RefSeq (protein)

NP_001068566 NP_005934 NP_001345458 NP_001345459 NP_001345460
NP_001345462 NP_001345463


n/a

Location (UCSC)

Chr 6: 39.9 – 39.93 Mb

n/a

PubMed search

^[2]

n/a

Wikidata

View/Edit Human

Molybdenum cofactor biosynthesis protein 1 is a protein that in humans and other animals, fungi, and cellular slime molds, is encoded by the MOCS1 gene.^[3]^[4] ^[5] ^[6]

Both copies of this gene are defective in patients with molybdenum cofactor deficiency, type A.^[6]

Molybdenum cofactor biosynthesis is a conserved pathway leading to the biological activation of molybdenum. The protein encoded by this gene is involved in molybdopterin biosynthesis. (This gene was originally thought to produce a bicistronic mRNA with the potential to produce two proteins (MOCS1A and MOCS1B) from adjacent open reading frames. However, only the first open reading frame (MOCS1A) has been found to encode a protein from the putative bicistronic mRNA.) Two of the splice variants found for this gene express proteins (MOCS1A-MOCS1B) that result from a fusion between the two open reading frames.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000124615 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "MOCS1 - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 19 July 2018.
^ Reiss J, Cohen N, Dorche C, Mandel H, Mendel RR, Stallmeyer B, Zabot MT, Dierks T (Oct 1998). "Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency". Nat Genet. 20 (1): 51–3. doi:10.1038/1706. PMID 9731530. S2CID 23833158.
^ Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT (Apr 1999). "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". Am J Hum Genet. 64 (3): 706–11. doi:10.1086/302296. PMC 1377787. PMID 10053004.
^ ^a ^b "Entrez Gene: MOCS1 molybdenum cofactor synthesis 1".

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.
Shalata A, Mandel H, Reiss J, et al. (1998). "Localization of a gene for molybdenum cofactor deficiency, on the short arm of chromosome 6, by homozygosity mapping". Am. J. Hum. Genet. 63 (1): 148–54. doi:10.1086/301916. PMC 1377237. PMID 9634514.
Feng G, Tintrup H, Kirsch J, et al. (1998). "Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity". Science. 282 (5392): 1321–4. Bibcode:1998Sci...282.1321F. doi:10.1126/science.282.5392.1321. PMID 9812897.
Reiss J, Christensen E, Kurlemann G, et al. (1999). "Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A.". Hum. Genet. 103 (6): 639–44. doi:10.1007/s004390050884. PMID 9921896. S2CID 5247017.
Reiss J, Christensen E, Dorche C (1999). "Molybdenum cofactor deficiency: first prenatal genetic analysis". Prenat. Diagn. 19 (4): 386–8. doi:10.1002/(SICI)1097-0223(199904)19:4<386::AID-PD550>3.0.CO;2-#. PMID 10327149. S2CID 196592216.
Gray TA, Nicholls RD (2000). "Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames". RNA. 6 (7): 928–36. doi:10.1017/S1355838200000182. PMC 1369970. PMID 10917590.
Hänzelmann P, Schwarz G, Mendel RR (2002). "Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis". J. Biol. Chem. 277 (21): 18303–12. doi:10.1074/jbc.M200947200. PMID 11891227.
Gross-Hardt S, Reiss J (2003). "The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons". Mol. Genet. Metab. 76 (4): 340–3. doi:10.1016/S1096-7192(02)00100-2. PMID 12208140.
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.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Hänzelmann P, Hernández HL, Menzel C, et al. (2004). "Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis". J. Biol. Chem. 279 (33): 34721–32. doi:10.1074/jbc.M313398200. PMID 15180982.
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.
Ichida K, Aydin HI, Hosoyamada M, et al. (2007). "A Turkish case with molybdenum cofactor deficiency". Nucleosides Nucleotides Nucleic Acids. 25 (9–11): 1087–91. doi:10.1080/15257770600894022. PMID 17065069. S2CID 40601679.

Metabolism of vitamins, coenzymes, and cofactors

Fat soluble vitamins

Vitamin A	Retinol binding protein
Vitamin E	Alpha-tocopherol transfer protein
Vitamin D	liver (Sterol 27-hydroxylase or CYP27A1) renal (25-Hydroxyvitamin D₃ 1-alpha-hydroxylase or CYP27B1) degradation (1,25-Dihydroxyvitamin D₃ 24-hydroxylase or CYP24A1)
Vitamin K	Vitamin K epoxide reductase