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Q9NZB8 (MOCS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Molybdenum cofactor biosynthesis protein 1
Alternative name(s):
Cell migration-inducing gene 11 protein
Molybdenum cofactor synthesis-step 1 protein A-B

Including the following 2 domains:

  1. Cyclic pyranopterin monophosphate synthase
    EC=4.1.99.18
    Alternative name(s):
    Molybdenum cofactor biosynthesis protein A
  2. Cyclic pyranopterin monophosphate synthase accessory protein
    Alternative name(s):
    Molybdenum cofactor biosynthesis protein C
Gene names
Name:MOCS1
ORF Names:MIG11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform MOCS1A and isoform MOCS1B probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). Ref.8

Catalytic activity

GTP = cyclic pyranopterin phosphate + diphosphate. Ref.8

Cofactor

Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate. Ref.10

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP-Rule MF_01224_B

Subunit structure

Isoform MOCS1A and isoform MOCS1B probably form a heterooligomer Probable.

Tissue specificity

Isoform MOCS1A and isoform 2 are widely expressed. Ref.1 Ref.9

Post-translational modification

Isoform MOCS1A, isoform 2 and isoform 3 are probably thiocarboxylated at their C-terminus. Thiocarboxylation probably plays a central role in molybdenum cofactor biosynthesis, since mutagenesis of the last 2 Gly residues of isoform MOCS1A abolishes the catalytic activity of the enzyme. Thiocarboxylation is absent in isoform MOCS1B, which lacks the C-terminal Gly residue. HAMAP-Rule MF_01224_B

Involvement in disease

Molybdenum cofactor deficiency, complementation group A (MOCODA) [MIM:252150]: An autosomal recessive metabolic disorder leading to the pleiotropic loss of molybdoenzyme activities. It is clinically characterized by onset in infancy of poor feeding, intractable seizures, severe psychomotor retardation, and death in early childhood in most patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.13 Ref.14

Miscellaneous

The MOCS1 locus has initially been reported to produce MOCS1A and MOCS1B from non-overlapping reading frames within a bicistronic transcript. However, only isoform MOCS1A seems to be translated from the bicistronic transcript. Isoform MOCS1B seems to be translated from a monocistronic mRNA that is derived by alternative splicing.

Sequence similarities

In the C-terminal section; belongs to the MoaC family.

In the N-terminal section; belongs to the MoaA/NifB/PqqE family.

Sequence caution

The sequence AAB87524.1 differs from that shown. Reason: Alternative splicing in the MOCS1A-MOCS1B joining region.

The sequence AAS00489.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC44526.1 differs from that shown. Reason: Alternative splicing in the MOCS1A-MOCS1B joining region.

The sequence CAI20007.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20012.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20013.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: So far, the different types of MOCS1A and MOCS1B isoforms have been investigated independently and several combinations might be possible.
Isoform MOCS1B (identifier: Q9NZB8-1)

Also known as: MOCS1B Type-II;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Multidomain protein with inactive MOCS1A and active MOCS1B.
Isoform MOCS1A (identifier: Q9NZB8-5)

Also known as: MOCS1A Type/Iad;

The sequence of this isoform differs from the canonical sequence as follows:
     384-385: EL → GG
     386-636: Missing.
Note: Contains a 1-thioglycine at position 385 (Probable).
Isoform 2 (identifier: Q9NZB8-6)

Also known as: MOCS1A Type-Ibcd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRML...PGESARAASE → MWKSWKLRTD...PCFLPGLSSQ
     384-385: EL → GG
     386-636: Missing.
Note: Contains a 1-thioglycine at position 385 (Probable).
Isoform 3 (identifier: Q9NZB8-3)

Also known as: MOCS1A Type-Ibd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASE → MWKSWKLRTDVR
     384-385: EL → GG
     386-636: Missing.
Note: Contains a 1-thioglycine at position 356 (Probable).
Isoform 4 (identifier: Q9NZB8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     368-368: G → E
     369-636: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: Q9NZB8-2)

Also known as: MOCS1B Type-III;

The sequence of this isoform differs from the canonical sequence as follows:
     368-383: Missing.
Note: Multidomain protein with inactive MOCS1A and active MOCS1B.
Isoform 7 (identifier: Q9NZB8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     368-383: Missing.
Isoform 8 (identifier: Q9NZB8-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MAARPLSRML...PGESARAASE → MWKSWKLRTD...PCFLPGLSSQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Molybdenum cofactor biosynthesis protein 1 HAMAP-Rule MF_01224_B
PRO_0000097870

Regions

Region1 – 383383Molybdenum cofactor biosynthesis protein A HAMAP-Rule MF_01224_B
Region317 – 3193GTP binding By similarity
Region414 – 636223Molybdenum cofactor biosynthesis protein C HAMAP-Rule MF_01224_B

Sites

Active site6061For molybdenum cofactor biosynthesis protein C activity Potential
Metal binding801Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
Metal binding841Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
Metal binding871Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable
Metal binding3121Iron-sulfur 2 (4Fe-4S-substrate) Probable
Metal binding3151Iron-sulfur 2 (4Fe-4S-substrate) Probable
Metal binding3291Iron-sulfur 2 (4Fe-4S-substrate) Probable
Binding site731GTP By similarity
Binding site861S-adenosyl-L-methionine By similarity
Binding site1231GTP By similarity
Binding site1271S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1541GTP By similarity
Binding site1781S-adenosyl-L-methionine By similarity
Binding site2151GTP By similarity
Binding site2491S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1981N6-acetyllysine Ref.11
Modified residue5281N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 8787Missing in isoform 4 and isoform 7.
VSP_036821
Alternative sequence1 – 4141MAARP…RAASE → MWKSWKLRTDVRVREGAGGS PCASSQPGSRGPCFLPGLSS Q in isoform 2 and isoform 8.
VSP_036822
Alternative sequence1 – 4141MAARP…RAASE → MWKSWKLRTDVR in isoform 3.
VSP_036823
Alternative sequence368 – 38316Missing in isoform 6 and isoform 7.
VSP_007439
Alternative sequence3681G → E in isoform 4.
VSP_036824
Alternative sequence369 – 636268Missing in isoform 4.
VSP_036825
Alternative sequence384 – 3852EL → GG in isoform MOCS1A, isoform 2 and isoform 3.
VSP_036826
Alternative sequence386 – 636251Missing in isoform MOCS1A, isoform 2 and isoform 3.
VSP_036827
Natural variant671R → W in MOCODA. Ref.14
VAR_054823
Natural variant731R → W in MOCODA. Ref.12
VAR_015658
Natural variant801C → G in MOCODA. Ref.14
VAR_054824
Natural variant841C → F in MOCODA. Ref.14
VAR_054825
Natural variant1231R → W in MOCODA. Ref.13
VAR_054826
Natural variant1261G → D in MOCODA. Ref.12
VAR_015659
Natural variant1271G → D in MOCODA. Ref.12
VAR_015660
Natural variant3191R → Q in MOCODA. Ref.12
VAR_015661
Natural variant3241G → E in MOCODA. Ref.12
VAR_015662
Natural variant3241G → R in MOCODA. Ref.13
VAR_054827
Natural variant3901P → H.
Corresponds to variant rs11969769 [ dbSNP | Ensembl ].
VAR_056131
Natural variant4521R → L.
Corresponds to variant rs11969206 [ dbSNP | Ensembl ].
VAR_061346

Experimental info

Mutagenesis801C → S: Impairs precursor Z synthesis. Ref.10
Mutagenesis841C → S: Impairs precursor Z synthesis. Ref.10
Mutagenesis871C → S: Impairs precursor Z synthesis. Ref.10
Mutagenesis3121C → S: Impairs precursor Z synthesis. Ref.10
Mutagenesis3151C → S: Impairs precursor Z synthesis. Ref.10
Mutagenesis3291C → S: Impairs precursor Z synthesis. Ref.10
Sequence conflict2331A → V in BAG51799. Ref.3
Sequence conflict2331A → V in BAG62053. Ref.3
Sequence conflict2391L → H in AAB87523. Ref.2
Sequence conflict4211A → G in BAG51799. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform MOCS1B (MOCS1B Type-II) [UniParc].

Last modified May 16, 2003. Version 3.
Checksum: 6774A563BAC42120

FASTA63670,105
        10         20         30         40         50         60 
MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL REHAAPFSAF 

        70         80         90        100        110        120 
LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN LLTTEEILTL ARLFVKEGID 

       130        140        150        160        170        180 
KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT IGVTTNGINL ARLLPQLQKA GLSAINISLD 

       190        200        210        220        230        240 
TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP 

       250        260        270        280        290        300 
LDVRFIEYMP FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 

       310        320        330        340        350        360 
ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE LLRIIGAAVG 

       370        380        390        400        410        420 
RKKRQHAGMF SISQMKNRPM ILIELFLMFP NSPPANPSIF SWDPLHVQGL RPRMSFSSQV 

       430        440        450        460        470        480 
ATLWKGCRVP QTPPLAQQRL GSGSFQRHYT SRADSDANSK CLSPGSWASA APSGPQLTSE 

       490        500        510        520        530        540 
QLTHVDSEGR AAMVDVGRKP DTERVAVASA VVLLGPVAFK LVQQNQLKKG DALVVAQLAG 

       550        560        570        580        590        600 
VQAAKVTSQL IPLCHHVALS HIQVQLELDS TRHAVKIQAS CRARGPTGVE MEALTSAAVA 

       610        620        630 
ALTLYDMCKA VSRDIVLEEI KLISKTGGQR GDFHRA 

« Hide

Isoform MOCS1A (MOCS1A Type/Iad) [UniParc].

Checksum: 77AB231D6DBB267E
Show »

FASTA38543,088
Isoform 2 (MOCS1A Type-Ibcd) [UniParc].

Checksum: 8E43CD0F611F8804
Show »

FASTA38543,150
Isoform 3 (MOCS1A Type-Ibd) [UniParc].

Checksum: 99F4B6D6B6A7B885
Show »

FASTA35640,378
Isoform 4 [UniParc].

Checksum: 0397D4D12A8C191B
Show »

FASTA28131,453
Isoform 6 (MOCS1B Type-III) [UniParc].

Checksum: 23CB32E0E6F8535D
Show »

FASTA62068,257
Isoform 7 [UniParc].

Checksum: FBE48E29A35248D4
Show »

FASTA53358,455
Isoform 8 [UniParc].

Checksum: D78D063A89E6131D
Show »

FASTA63670,167

References

« Hide 'large scale' references
[1]"Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency."
Reiss J.P., Cohen N., Dorche C., Mandel H., Mendel R.R., Stallmeyer B., Zabot M.-T., Dierks T.
Nat. Genet. 20:51-53(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MOCS1A; 2 AND 8), INVOLVEMENT IN MOCODA, TISSUE SPECIFICITY.
[2]Larin D., Ross B.M., Gilliam T.C.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MOCS1A AND MOCS1B).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MOCS1A AND 7).
Tissue: Placenta.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Colon and Kidney.
[6]"Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames."
Gray T.A., Nicholls R.D.
RNA 6:928-936(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 283-636 (ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF 377-636 (ISOFORM MOCS1B).
[7]"Identification of a human migration-inducing gene."
Kim J.W.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 386-636.
[8]"Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis."
Haenzelmann P., Schwarz G., Mendel R.R.
J. Biol. Chem. 277:18303-18312(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING (ISOFORMS MOCS1A AND MOCS1B).
[9]"The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons."
Gross-Hardt S., Reiss J.
Mol. Genet. Metab. 76:340-343(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS MOCS1A; 2 AND 3), TISSUE SPECIFICITY.
[10]"Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis."
Haenzelmann P., Hernandez H.L., Menzel C., Garcia-Serres R., Huynh B.H., Johnson M.K., Mendel R.R., Schindelin H.
J. Biol. Chem. 279:34721-34732(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, CHARACTERIZATION OF IRON-SULFUR CLUSTER-BINDING, MUTAGENESIS OF CYS-80; CYS-84; CYS-87; CYS-312; CYS-315 AND CYS-329.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A."
Reiss J.P., Christensen E., Kurlemann G., Zabot M.-T., Dorche C.
Hum. Genet. 103:639-644(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MOCODA TRP-73; ASP-126; ASP-127; GLN-319 AND GLU-324.
[13]"Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH."
Reiss J., Johnson J.L.
Hum. Mutat. 21:569-576(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MOCODA TRP-123 AND ARG-324.
[14]"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."
Leimkuehler S., Charcosset M., Latour P., Dorche C., Kleppe S., Scaglia F., Szymczak I., Schupp P., Hahnewald R., Reiss J.
Hum. Genet. 117:565-570(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MOCODA TRP-67; GLY-80 AND PHE-84.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224328 mRNA. Translation: CAA11897.1.
AJ224328 mRNA. Translation: CAA11898.1.
AJ404969 Genomic DNA. Translation: CAC44526.1. Sequence problems.
AJ293577, AJ293578, AJ293579 Genomic DNA. Translation: CAC44527.1.
AF034374 mRNA. Translation: AAB87523.1.
AF034374 mRNA. Translation: AAB87524.1. Sequence problems.
AK300300 mRNA. Translation: BAG62053.1.
AK056740 mRNA. Translation: BAG51799.1.
AL136089 Genomic DNA. Translation: CAI20007.1. Sequence problems.
AL136089 Genomic DNA. Translation: CAI20011.1.
AL136089 Genomic DNA. Translation: CAI20012.1. Sequence problems.
AL136089 Genomic DNA. Translation: CAI20013.1. Sequence problems.
AL136089 Genomic DNA. Translation: CAI20014.1.
AL136089 Genomic DNA. Translation: CAI20015.1.
BC036839 mRNA. Translation: AAH36839.1.
AF214022 mRNA. Translation: AAF67857.1.
AF214023 mRNA. Translation: AAF67858.1.
AY423726 mRNA. Translation: AAS00489.1. Different initiation.
CCDSCCDS43460.1. [Q9NZB8-5]
CCDS4846.1. [Q9NZB8-6]
RefSeqNP_001068566.1. NM_001075098.3. [Q9NZB8-5]
NP_005934.2. NM_005943.5. [Q9NZB8-6]
UniGeneHs.357128.
Hs.718492.

3D structure databases

ProteinModelPortalQ9NZB8.
SMRQ9NZB8. Positions 61-351, 488-635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110480. 1 interaction.
IntActQ9NZB8. 1 interaction.

PTM databases

PhosphoSiteQ9NZB8.

Polymorphism databases

DMDM30913216.

Proteomic databases

MaxQBQ9NZB8.
PaxDbQ9NZB8.
PRIDEQ9NZB8.

Protocols and materials databases

DNASU4337.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308559; ENSP00000309843; ENSG00000124615. [Q9NZB8-2]
ENST00000340692; ENSP00000344794; ENSG00000124615. [Q9NZB8-1]
ENST00000373175; ENSP00000362270; ENSG00000124615. [Q9NZB8-3]
ENST00000373181; ENSP00000362277; ENSG00000124615. [Q9NZB8-4]
ENST00000373186; ENSP00000362282; ENSG00000124615. [Q9NZB8-6]
ENST00000373188; ENSP00000362284; ENSG00000124615. [Q9NZB8-5]
ENST00000373195; ENSP00000362291; ENSG00000124615. [Q9NZB8-7]
ENST00000425303; ENSP00000416478; ENSG00000124615. [Q9NZB8-8]
ENST00000432280; ENSP00000410809; ENSG00000124615. [Q9NZB8-3]
GeneID4337.
KEGGhsa:4337.
UCSCuc003opa.3. human. [Q9NZB8-6]
uc003opb.3. human. [Q9NZB8-8]
uc003opd.3. human. [Q9NZB8-5]
uc003ope.3. human. [Q9NZB8-7]

Organism-specific databases

CTD4337.
GeneCardsGC06M039920.
HGNCHGNC:7190. MOCS1.
HPAHPA045783.
MIM252150. phenotype.
603707. gene.
neXtProtNX_Q9NZB8.
Orphanet308386. Sulfite oxidase deficiency due to molybdenum cofactor deficiency type A.
PharmGKBPA30900.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2896.
InParanoidQ9NZB8.
KOK03639.
OMAREYPGDI.
OrthoDBEOG72JWHH.
PhylomeDBQ9NZB8.
TreeFamTF300424.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00344.

Gene expression databases

ArrayExpressQ9NZB8.
BgeeQ9NZB8.
CleanExHS_MOCS1.
GenevestigatorQ9NZB8.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.30.70.640. 1 hit.
HAMAPMF_01224_B. MoaC_B.
MF_01225_B. MoaA_B.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR023045. Mo_CF_biosynth-C.
IPR023046. Mo_CF_biosynth-C_bac.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR002820. Mopterin_CF_biosynth-C_dom.
IPR007197. rSAM.
[Graphical view]
PfamPF01967. MoaC. 1 hit.
PF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF55040. SSF55040. 1 hit.
TIGRFAMsTIGR02666. moaA. 1 hit.
TIGR00581. moaC. 1 hit.
PROSITEPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMOCS1.
GenomeRNAi4337.
NextBio17062.
PROQ9NZB8.
SOURCESearch...

Entry information

Entry nameMOCS1_HUMAN
AccessionPrimary (citable) accession number: Q9NZB8
Secondary accession number(s): B3KPT7 expand/collapse secondary AC list , B4DTP1, O14940, O14941, O75710, Q5J7W0, Q5TCE1, Q5TCE2, Q5TCE6, Q5TCE9, Q5TCF0, Q5TCF1, Q8N418, Q9NZB7, Q9UEM1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM