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{{Infobox_gene}}
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'''Molybdenum cofactor synthesis protein 2A''' and '''molybdenum cofactor synthesis protein 2B''' are a pair of [[protein]]s that in humans are encoded from the same ''MOCS2'' [[gene]].<ref name="pmid10053004">{{cite journal |vauthors=Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT |title=Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B |journal=American Journal of Human Genetics |volume=64 |issue=3 |pages=706–11 |date=March 1999 |pmid=10053004 |pmc=1377787 |doi=10.1086/302296}}</ref><ref name="pmid9889283">{{cite journal |vauthors=Sloan J, Kinghorn JR, Unkles SE |title=The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames |journal=Nucleic Acids Research |volume=27 |issue=3 |pages=854–8 |date=February 1999 |pmid=9889283 |pmc=148257 |doi=10.1093/nar/27.3.854}}</ref><ref name="entrez">{{EntrezGene|4338}}: MOCS2 molybdenum cofactor synthesis 2</ref>  These two proteins dimerize to form [[molybdopterin synthase]].
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== Function ==
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Eukaryotic [[molybdoenzyme]]s use a unique [[molybdenum cofactor]] (MoCo) consisting of a [[pterin]], termed [[molybdopterin]], and the catalytically active metal [[molybdenum]]. MoCo is synthesized from [[cyclic pyranopterin monophosphate]] (precursor Z) by the [[heterodimeric]] enzyme [[molybdopterin synthase]].<ref name="entrez"/>
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== Gene ==
}}
The large and small subunits of molybdopterin synthase are both encoded from the MOCS2 gene by overlapping open reading frames. The proteins were initially thought to be encoded from a [[multicistronic message|bicistronic]] [[Transcription (genetics)|transcript]]. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.<ref name="entrez"/>
 
The MOCS2 gene contains 7 exons. Exons 1 to 3 encode MOCS2A (the small subunit), and exons 3 to 7 encode MOCS2B (large subunit).<ref name="pmid10053004"/>
 
===Genetic disease===
Defects in both copies of MOCS2 cause the [[molybdenum cofactor deficiency]] disease in babies.<ref>{{cite journal  |vauthors=Ichida K, Aydin HI, Hosoyamada M, etal |title=A Turkish case with molybdenum cofactor deficiency |journal=Nucleosides, Nucleotides & Nucleic Acids |volume=25 |issue=9–11 |pages=1087–91 |year=2006 |pmid=17065069 |doi=10.1080/15257770600894022}}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Protein Structure ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Molybdenum cofactor synthesis 2
| HGNCid = 7193
| Symbol = MOCS2
| AltSymbols =; MCBPE; MOCO1; MOCS2A; MOCS2B; MPTS
| OMIM = 603708
| ECnumber = 
| Homologene = 32193
| MGIid = 1336894
| GeneAtlas_image1 = PBB_GE_MOCS2_218212_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0019008 |text = molybdopterin synthase complex}}
| Process = {{GNF_GO|id=GO:0006777 |text = Mo-molybdopterin cofactor biosynthetic process}} {{GNF_GO|id=GO:0006790 |text = sulfur metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4338
    | Hs_Ensembl = ENSG00000164172
    | Hs_RefseqProtein = NP_004522
    | Hs_RefseqmRNA = NM_004531
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 52427266
    | Hs_GenLoc_end = 52441359
    | Hs_Uniprot = O96007
    | Mm_EntrezGene = 17434
    | Mm_Ensembl = ENSMUSG00000015536
    | Mm_RefseqmRNA = NM_013826
    | Mm_RefseqProtein = NP_038854
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 115939136
    | Mm_GenLoc_end = 115949884
    | Mm_Uniprot = Q8C5E5
  }}
}}
'''Molybdenum cofactor synthesis 2''', also known as '''MOCS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MOCS2 molybdenum cofactor synthesis 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4338| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.<ref name="pmid12732628">{{cite journal |vauthors=Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR |title=Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency |journal=The Journal of Biological Chemistry |volume=278 |issue=28 |pages=26127–34 |date=July 2003 |pmid=12732628 |doi=10.1074/jbc.M303092200}}</ref>
{{PBB_Summary
| section_title =
| summary_text = Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin, termed molybdopterin, and the catalytically active metal molybdenum. MoCo is synthesized from precursor Z by the heterodimeric enzyme molybdopterin synthase. The large and small subunits of molybdopterin synthase are both encoded from this gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.<ref name="entrez">{{cite web | title = Entrez Gene: MOCS2 molybdenum cofactor synthesis 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4338| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Reiss J, Johnson JL |title=Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH. |journal=Hum. Mutat. |volume=21 |issue= 6 |pages= 569-76 |year= 2003 |pmid= 12754701 |doi= 10.1002/humu.10223 }}
*{{cite journal |vauthors=Reiss J, Johnson JL |title=Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH |journal=Human Mutation |volume=21 |issue=6 |pages=569–76 |date=June 2003 |pmid=12754701 |doi=10.1002/humu.10223}}
*{{cite journal | author=Krawczak M, Reiss J, Cooper DN |title=The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences. |journal=Hum. Genet. |volume=90 |issue= 1-2 |pages= 41-54 |year= 1992 |pmid= 1427786 |doi= }}
*{{cite journal |vauthors=Krawczak M, Reiss J, Cooper DN |title=The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences |journal=Human Genetics |volume=90 |issue=1–2 |pages=41–54 |year=1992 |pmid=1427786 |doi=10.1007/bf00210743}}
*{{cite journal  | author=Reiss J, Cohen N, Dorche C, ''et al.'' |title=Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 51-3 |year= 1998 |pmid= 9731530 |doi= 10.1038/1706 }}
*{{cite journal  |vauthors=Reiss J, Cohen N, Dorche C, etal |title=Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency |journal=Nature Genetics |volume=20 |issue=1 |pages=51–3 |date=September 1998 |pmid=9731530 |doi=10.1038/1706}}
*{{cite journal  | author=Feng G, Tintrup H, Kirsch J, ''et al.'' |title=Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity. |journal=Science |volume=282 |issue= 5392 |pages= 1321-4 |year= 1998 |pmid= 9812897 |doi= }}
*{{cite journal  |vauthors=Feng G, Tintrup H, Kirsch J, etal |title=Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity |journal=Science |volume=282 |issue=5392 |pages=1321–4 |date=November 1998 |pmid=9812897 |doi=10.1126/science.282.5392.1321}}
*{{cite journal  | author=Sloan J, Kinghorn JR, Unkles SE |title=The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames. |journal=Nucleic Acids Res. |volume=27 |issue= 3 |pages= 854-8 |year= 1999 |pmid= 9889283 |doi=  }}
*{{cite journal |vauthors=Stallmeyer B, Drugeon G, Reiss J, Haenni AL, Mendel RR |title=Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames |journal=American Journal of Human Genetics |volume=64 |issue=3 |pages=698–705 |date=March 1999 |pmid=10053003 |pmc=1377786 |doi=10.1086/302295}}
*{{cite journal | author=Stallmeyer B, Drugeon G, Reiss J, ''et al.'' |title=Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames. |journal=Am. J. Hum. Genet. |volume=64 |issue= 3 |pages= 698-705 |year= 1999 |pmid= 10053003 |doi= }}
*{{cite journal  |vauthors=Johnson JL, Coyne KE, Rajagopalan KV, etal |title=Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency |journal=American Journal of Medical Genetics |volume=104 |issue=2 |pages=169–73 |date=November 2001 |pmid=11746050 |doi=10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8}}
*{{cite journal  | author=Reiss J, Dorche C, Stallmeyer B, ''et al.'' |title=Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B. |journal=Am. J. Hum. Genet. |volume=64 |issue= 3 |pages= 706-11 |year= 1999 |pmid= 10053004 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=99 |issue=26 |pages=16899–903 |date=December 2002 |pmid=12477932 |pmc=139241 |doi=10.1073/pnas.242603899}}
*{{cite journal  | author=Johnson JL, Coyne KE, Rajagopalan KV, ''et al.'' |title=Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency. |journal=Am. J. Med. Genet. |volume=104 |issue= 2 |pages= 169-73 |year= 2002 |pmid= 11746050 |doi= }}
*{{cite journal |vauthors=Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S |title=Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=101 |issue=16 |pages=5946–51 |date=April 2004 |pmid=15073332 |pmc=395903 |doi=10.1073/pnas.0308191101}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Research |volume=14 |issue=10B |pages=2121–7 |date=October 2004 |pmid=15489334 |pmc=528928 |doi=10.1101/gr.2596504}}
*{{cite journal | author=Leimkuhler S, Freuer A, Araujo JA, ''et al.'' |title=Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 26127-34 |year= 2003 |pmid= 12732628 |doi= 10.1074/jbc.M303092200 }}
*{{cite journal  |vauthors=Leimkühler S, Charcosset M, Latour P, etal |title=Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase |journal=Human Genetics |volume=117 |issue=6 |pages=565–70 |date=October 2005 |pmid=16021469 |doi=10.1007/s00439-005-1341-9}}
*{{cite journal  | author=Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S |title=Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 16 |pages= 5946-51 |year= 2004 |pmid= 15073332 |doi= 10.1073/pnas.0308191101 }}
*{{cite journal |vauthors=Hahnewald R, Leimkühler S, Vilaseca A, Acquaviva-Bourdain C, Lenz U, Reiss J |title=A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase |journal=Molecular Genetics and Metabolism |volume=89 |issue=3 |pages=210–3 |date=November 2006 |pmid=16737835 |doi=10.1016/j.ymgme.2006.04.008}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal |vauthors=Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nature Biotechnology |volume=24 |issue=10 |pages=1285–92 |date=October 2006 |pmid=16964243 |doi=10.1038/nbt1240}}
*{{cite journal  | author=Leimkühler S, Charcosset M, Latour P, ''et al.'' |title=Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase. |journal=Hum. Genet. |volume=117 |issue= 6 |pages= 565-70 |year= 2005 |pmid= 16021469 |doi= 10.1007/s00439-005-1341-9 }}
*{{cite journal |vauthors=Per H, Gümüş H, Ichida K, Cağlayan O, Kumandaş S |title=Molybdenum cofactor deficiency: clinical features in a Turkish patient |journal=Brain & Development |volume=29 |issue=6 |pages=365–8 |date=July 2007 |pmid=17158010 |doi=10.1016/j.braindev.2006.10.007}}
*{{cite journal | author=Hahnewald R, Leimkühler S, Vilaseca A, ''et al.'' |title=A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase. |journal=Mol. Genet. Metab. |volume=89 |issue= 3 |pages= 210-3 |year= 2006 |pmid= 16737835 |doi= 10.1016/j.ymgme.2006.04.008 }}
*{{cite journal | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
*{{cite journal | author=Per H, Gümüş H, Ichida K, ''et al.'' |title=Molybdenum cofactor deficiency: clinical features in a Turkish patient. |journal=Brain Dev. |volume=29 |issue= 6 |pages= 365-8 |year= 2007 |pmid= 17158010 |doi= 10.1016/j.braindev.2006.10.007 }}
}}
}}
{{refend}}
{{refend}}


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{{Metabolism of vitamins, coenzymes, and cofactors}}
 
 
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Latest revision as of 23:42, 2 June 2016

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of proteins that in humans are encoded from the same MOCS2 gene.[1][2][3] These two proteins dimerize to form molybdopterin synthase.

Function

Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin, termed molybdopterin, and the catalytically active metal molybdenum. MoCo is synthesized from cyclic pyranopterin monophosphate (precursor Z) by the heterodimeric enzyme molybdopterin synthase.[3]

Gene

The large and small subunits of molybdopterin synthase are both encoded from the MOCS2 gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits.[3]

The MOCS2 gene contains 7 exons. Exons 1 to 3 encode MOCS2A (the small subunit), and exons 3 to 7 encode MOCS2B (large subunit).[1]

Genetic disease

Defects in both copies of MOCS2 cause the molybdenum cofactor deficiency disease in babies.[4]

Protein Structure

MOCS2A and MOCS2B subunits form dimers in solution. These dimers in turn dimerize to form the tetrameric molybdopterin synthase complex.[5]

References

  1. ↑ 1.0 1.1 Reiss J, Dorche C, Stallmeyer B, Mendel RR, Cohen N, Zabot MT (March 1999). "Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B". American Journal of Human Genetics. 64 (3): 706–11. doi:10.1086/302296. PMC 1377787. PMID 10053004.
  2. ↑ Sloan J, Kinghorn JR, Unkles SE (February 1999). "The two subunits of human molybdopterin synthase: evidence for a bicistronic messenger RNA with overlapping reading frames". Nucleic Acids Research. 27 (3): 854–8. doi:10.1093/nar/27.3.854. PMC 148257. PMID 9889283.
  3. ↑ 3.0 3.1 3.2 EntrezGene 4338: MOCS2 molybdenum cofactor synthesis 2
  4. ↑ Ichida K, Aydin HI, Hosoyamada M, et al. (2006). "A Turkish case with molybdenum cofactor deficiency". Nucleosides, Nucleotides & Nucleic Acids. 25 (9–11): 1087–91. doi:10.1080/15257770600894022. PMID 17065069.
  5. ↑ Leimkuhler S, Freuer A, Araujo JA, Rajagopalan KV, Mendel RR (July 2003). "Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency". The Journal of Biological Chemistry. 278 (28): 26127–34. doi:10.1074/jbc.M303092200. PMID 12732628.

Further reading



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