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Q9NZB8

- MOCS1_HUMAN

UniProt

Q9NZB8 - MOCS1_HUMAN

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Protein

Molybdenum cofactor biosynthesis protein 1

Gene

MOCS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

GTP = cyclic pyranopterin phosphate + diphosphate.1 Publication

Cofactori

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.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731GTPBy similarity
Metal bindingi80 – 801Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated
Metal bindingi84 – 841Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated
Binding sitei86 – 861S-adenosyl-L-methionineBy similarity
Metal bindingi87 – 871Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated
Binding sitei123 – 1231GTPBy similarity
Binding sitei127 – 1271S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei154 – 1541GTPBy similarity
Binding sitei178 – 1781S-adenosyl-L-methionineBy similarity
Binding sitei215 – 2151GTPBy similarity
Binding sitei249 – 2491S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi312 – 3121Iron-sulfur 2 (4Fe-4S-substrate)Curated
Metal bindingi315 – 3151Iron-sulfur 2 (4Fe-4S-substrate)Curated
Metal bindingi329 – 3291Iron-sulfur 2 (4Fe-4S-substrate)Curated
Active sitei606 – 6061For molybdenum cofactor biosynthesis protein C activitySequence Analysis

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  2. cyclic pyranopterin monophosphate synthase activity Source: UniProtKB-EC
  3. GTP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. molybdopterin cofactor biosynthetic process Source: Reactome
  2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
  4. vitamin metabolic process Source: Reactome
  5. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

4Fe-4S, GTP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended 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:
Cyclic pyranopterin monophosphate synthase (EC:4.1.99.18)
Alternative name(s):
Molybdenum cofactor biosynthesis protein A
Cyclic pyranopterin monophosphate synthase accessory protein
Alternative name(s):
Molybdenum cofactor biosynthesis protein C
Gene namesi
Name:MOCS1
ORF Names:MIG11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7190. MOCS1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. molybdopterin synthase complex Source: InterPro
  3. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671R → W in MOCODA. 1 Publication
VAR_054823
Natural varianti73 – 731R → W in MOCODA. 1 Publication
VAR_015658
Natural varianti80 – 801C → G in MOCODA. 1 Publication
VAR_054824
Natural varianti84 – 841C → F in MOCODA. 1 Publication
VAR_054825
Natural varianti123 – 1231R → W in MOCODA. 1 Publication
VAR_054826
Natural varianti126 – 1261G → D in MOCODA. 1 Publication
VAR_015659
Natural varianti127 – 1271G → D in MOCODA. 1 Publication
VAR_015660
Natural varianti319 – 3191R → Q in MOCODA. 1 Publication
VAR_015661
Natural varianti324 – 3241G → E in MOCODA. 1 Publication
VAR_015662
Natural varianti324 – 3241G → R in MOCODA. 1 Publication
VAR_054827

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801C → S: Impairs precursor Z synthesis. 1 Publication
Mutagenesisi84 – 841C → S: Impairs precursor Z synthesis. 1 Publication
Mutagenesisi87 – 871C → S: Impairs precursor Z synthesis. 1 Publication
Mutagenesisi312 – 3121C → S: Impairs precursor Z synthesis. 1 Publication
Mutagenesisi315 – 3151C → S: Impairs precursor Z synthesis. 1 Publication
Mutagenesisi329 – 3291C → S: Impairs precursor Z synthesis. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi252150. phenotype.
Orphaneti308386. Sulfite oxidase deficiency due to molybdenum cofactor deficiency type A.
PharmGKBiPA30900.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Molybdenum cofactor biosynthesis protein 1PRO_0000097870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei528 – 5281N6-acetyllysineBy similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NZB8.
PaxDbiQ9NZB8.
PRIDEiQ9NZB8.

PTM databases

PhosphoSiteiQ9NZB8.

Expressioni

Tissue specificityi

Isoform MOCS1A and isoform 2 are widely expressed.2 Publications

Gene expression databases

BgeeiQ9NZB8.
CleanExiHS_MOCS1.
ExpressionAtlasiQ9NZB8. baseline and differential.
GenevestigatoriQ9NZB8.

Organism-specific databases

HPAiHPA045783.

Interactioni

Subunit structurei

Isoform MOCS1A and isoform MOCS1B probably form a heterooligomer.Curated

Protein-protein interaction databases

BioGridi110480. 5 interactions.
IntActiQ9NZB8. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9NZB8.
SMRiQ9NZB8. Positions 61-351, 488-635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383Molybdenum cofactor biosynthesis protein AAdd
BLAST
Regioni317 – 3193GTP bindingBy similarity
Regioni414 – 636223Molybdenum cofactor biosynthesis protein CAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2896.
GeneTreeiENSGT00390000016567.
InParanoidiQ9NZB8.
KOiK03639.
OMAiREYPGDI.
OrthoDBiEOG72JWHH.
PhylomeDBiQ9NZB8.
TreeFamiTF300424.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.70.640. 1 hit.
HAMAPiMF_01224_B. MoaC_B.
MF_01225_B. MoaA_B.
InterProiIPR013785. 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]
PfamiPF01967. MoaC. 1 hit.
PF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55040. SSF55040. 1 hit.
TIGRFAMsiTIGR02666. moaA. 1 hit.
TIGR00581. moaC. 1 hit.
PROSITEiPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL
60 70 80 90 100
REHAAPFSAF LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN
110 120 130 140 150
LLTTEEILTL ARLFVKEGID KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT
160 170 180 190 200
IGVTTNGINL ARLLPQLQKA GLSAINISLD TLVPAKFEFI VRRKGFHKVM
210 220 230 240 250
EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP LDVRFIEYMP
260 270 280 290 300
FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ
310 320 330 340 350
ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE
360 370 380 390 400
LLRIIGAAVG RKKRQHAGMF SISQMKNRPM ILIELFLMFP NSPPANPSIF
410 420 430 440 450
SWDPLHVQGL RPRMSFSSQV ATLWKGCRVP QTPPLAQQRL GSGSFQRHYT
460 470 480 490 500
SRADSDANSK CLSPGSWASA APSGPQLTSE QLTHVDSEGR AAMVDVGRKP
510 520 530 540 550
DTERVAVASA VVLLGPVAFK LVQQNQLKKG DALVVAQLAG VQAAKVTSQL
560 570 580 590 600
IPLCHHVALS HIQVQLELDS TRHAVKIQAS CRARGPTGVE MEALTSAAVA
610 620 630
ALTLYDMCKA VSRDIVLEEI KLISKTGGQR GDFHRA

Note: Multidomain protein with inactive MOCS1A and active MOCS1B.

Length:636
Mass (Da):70,105
Last modified:May 16, 2003 - v3
Checksum:i6774A563BAC42120
GO
Isoform MOCS1A (identifier: Q9NZB8-5) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:385
Mass (Da):43,088
Checksum:i77AB231D6DBB267E
GO
Isoform 2 (identifier: Q9NZB8-6) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:385
Mass (Da):43,150
Checksum:i8E43CD0F611F8804
GO
Isoform 3 (identifier: Q9NZB8-3) [UniParc]FASTAAdd to Basket

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.Curated

Show »
Length:356
Mass (Da):40,378
Checksum:i99F4B6D6B6A7B885
GO
Isoform 4 (identifier: Q9NZB8-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:281
Mass (Da):31,453
Checksum:i0397D4D12A8C191B
GO
Isoform 6 (identifier: Q9NZB8-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:620
Mass (Da):68,257
Checksum:i23CB32E0E6F8535D
GO
Isoform 7 (identifier: Q9NZB8-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     368-383: Missing.

Show »
Length:533
Mass (Da):58,455
Checksum:iFBE48E29A35248D4
GO
Isoform 8 (identifier: Q9NZB8-8) [UniParc]FASTAAdd to Basket

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

Show »
Length:636
Mass (Da):70,167
Checksum:iD78D063A89E6131D
GO

Sequence cautioni

The sequence AAB87524.1 differs from that shown. Reason: Alternative splicing in the MOCS1A-MOCS1B joining region.
The sequence CAC44526.1 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 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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331A → V in BAG51799. (PubMed:14702039)Curated
Sequence conflicti233 – 2331A → V in BAG62053. (PubMed:14702039)Curated
Sequence conflicti239 – 2391L → H in AAB87523. 1 PublicationCurated
Sequence conflicti421 – 4211A → G in BAG51799. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671R → W in MOCODA. 1 Publication
VAR_054823
Natural varianti73 – 731R → W in MOCODA. 1 Publication
VAR_015658
Natural varianti80 – 801C → G in MOCODA. 1 Publication
VAR_054824
Natural varianti84 – 841C → F in MOCODA. 1 Publication
VAR_054825
Natural varianti123 – 1231R → W in MOCODA. 1 Publication
VAR_054826
Natural varianti126 – 1261G → D in MOCODA. 1 Publication
VAR_015659
Natural varianti127 – 1271G → D in MOCODA. 1 Publication
VAR_015660
Natural varianti319 – 3191R → Q in MOCODA. 1 Publication
VAR_015661
Natural varianti324 – 3241G → E in MOCODA. 1 Publication
VAR_015662
Natural varianti324 – 3241G → R in MOCODA. 1 Publication
VAR_054827
Natural varianti390 – 3901P → H.
Corresponds to variant rs11969769 [ dbSNP | Ensembl ].
VAR_056131
Natural varianti452 – 4521R → L.
Corresponds to variant rs11969206 [ dbSNP | Ensembl ].
VAR_061346

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787Missing in isoform 4 and isoform 7. 2 PublicationsVSP_036821Add
BLAST
Alternative sequencei1 – 4141MAARP…RAASE → MWKSWKLRTDVRVREGAGGS PCASSQPGSRGPCFLPGLSS Q in isoform 2 and isoform 8. 1 PublicationVSP_036822Add
BLAST
Alternative sequencei1 – 4141MAARP…RAASE → MWKSWKLRTDVR in isoform 3. CuratedVSP_036823Add
BLAST
Alternative sequencei368 – 38316Missing in isoform 6 and isoform 7. 2 PublicationsVSP_007439Add
BLAST
Alternative sequencei368 – 3681G → E in isoform 4. 1 PublicationVSP_036824
Alternative sequencei369 – 636268Missing in isoform 4. 1 PublicationVSP_036825Add
BLAST
Alternative sequencei384 – 3852EL → GG in isoform MOCS1A, isoform 2 and isoform 3. 3 PublicationsVSP_036826
Alternative sequencei386 – 636251Missing in isoform MOCS1A, isoform 2 and isoform 3. 3 PublicationsVSP_036827Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43460.1. [Q9NZB8-5]
CCDS4846.1. [Q9NZB8-6]
RefSeqiNP_001068566.1. NM_001075098.3. [Q9NZB8-5]
NP_005934.2. NM_005943.5. [Q9NZB8-6]
UniGeneiHs.357128.
Hs.718492.

Genome annotation databases

EnsembliENST00000340692; ENSP00000344794; ENSG00000124615. [Q9NZB8-1]
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]
GeneIDi4337.
KEGGihsa:4337.
UCSCiuc003opa.3. human. [Q9NZB8-6]
uc003opb.3. human. [Q9NZB8-8]
uc003opd.3. human. [Q9NZB8-5]
uc003ope.3. human. [Q9NZB8-7]

Polymorphism databases

DMDMi30913216.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS43460.1. [Q9NZB8-5 ]
CCDS4846.1. [Q9NZB8-6 ]
RefSeqi NP_001068566.1. NM_001075098.3. [Q9NZB8-5 ]
NP_005934.2. NM_005943.5. [Q9NZB8-6 ]
UniGenei Hs.357128.
Hs.718492.

3D structure databases

ProteinModelPortali Q9NZB8.
SMRi Q9NZB8. Positions 61-351, 488-635.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110480. 5 interactions.
IntActi Q9NZB8. 1 interaction.

PTM databases

PhosphoSitei Q9NZB8.

Polymorphism databases

DMDMi 30913216.

Proteomic databases

MaxQBi Q9NZB8.
PaxDbi Q9NZB8.
PRIDEi Q9NZB8.

Protocols and materials databases

DNASUi 4337.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340692 ; ENSP00000344794 ; ENSG00000124615 . [Q9NZB8-1 ]
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 ]
GeneIDi 4337.
KEGGi hsa:4337.
UCSCi uc003opa.3. human. [Q9NZB8-6 ]
uc003opb.3. human. [Q9NZB8-8 ]
uc003opd.3. human. [Q9NZB8-5 ]
uc003ope.3. human. [Q9NZB8-7 ]

Organism-specific databases

CTDi 4337.
GeneCardsi GC06M039920.
HGNCi HGNC:7190. MOCS1.
HPAi HPA045783.
MIMi 252150. phenotype.
603707. gene.
neXtProti NX_Q9NZB8.
Orphaneti 308386. Sulfite oxidase deficiency due to molybdenum cofactor deficiency type A.
PharmGKBi PA30900.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2896.
GeneTreei ENSGT00390000016567.
InParanoidi Q9NZB8.
KOi K03639.
OMAi REYPGDI.
OrthoDBi EOG72JWHH.
PhylomeDBi Q9NZB8.
TreeFami TF300424.

Enzyme and pathway databases

UniPathwayi UPA00344 .
Reactomei REACT_25073. Molybdenum cofactor biosynthesis.

Miscellaneous databases

GeneWikii MOCS1.
GenomeRNAii 4337.
NextBioi 17062.
PROi Q9NZB8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZB8.
CleanExi HS_MOCS1.
ExpressionAtlasi Q9NZB8. baseline and differential.
Genevestigatori Q9NZB8.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
3.30.70.640. 1 hit.
HAMAPi MF_01224_B. MoaC_B.
MF_01225_B. MoaA_B.
InterProi IPR013785. 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 ]
Pfami PF01967. MoaC. 1 hit.
PF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
SUPFAMi SSF55040. SSF55040. 1 hit.
TIGRFAMsi TIGR02666. moaA. 1 hit.
TIGR00581. moaC. 1 hit.
PROSITEi PS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiMOCS1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZB8
Secondary accession number(s): B3KPT7
, B4DTP1, O14940, O14941, O75710, Q5J7W0, Q5TCE1, Q5TCE2, Q5TCE6, Q5TCE9, Q5TCF0, Q5TCF1, Q8N418, Q9NZB7, Q9UEM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3