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Q9NZB8

- MOCS1_HUMAN

UniProt

Q9NZB8 - MOCS1_HUMAN

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
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (16 May 2003)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ9NZB8.
    BgeeiQ9NZB8.
    CleanExiHS_MOCS1.
    GenevestigatoriQ9NZB8.

    Organism-specific databases

    HPAiHPA045783.

    Interactioni

    Subunit structurei

    Isoform MOCS1A and isoform MOCS1B probably form a heterooligomer.Curated

    Protein-protein interaction databases

    BioGridi110480. 1 interaction.
    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.
    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

    MAARPLSRML RRLLRSSARS CSSGAPVTQP CPGESARAAS EEVSRRRQFL    50
    REHAAPFSAF LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAN 100
    LLTTEEILTL ARLFVKEGID KIRLTGGEPL IRPDVVDIVA QLQRLEGLRT 150
    IGVTTNGINL ARLLPQLQKA GLSAINISLD TLVPAKFEFI VRRKGFHKVM 200
    EGIHKAIELG YNPVKVNCVV MRGLNEDELL DFAALTEGLP LDVRFIEYMP 250
    FDGNKWNFKK MVSYKEMLDT VRQQWPELEK VPEEESSTAK AFKIPGFQGQ 300
    ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEQE 350
    LLRIIGAAVG RKKRQHAGMF SISQMKNRPM ILIELFLMFP NSPPANPSIF 400
    SWDPLHVQGL RPRMSFSSQV ATLWKGCRVP QTPPLAQQRL GSGSFQRHYT 450
    SRADSDANSK CLSPGSWASA APSGPQLTSE QLTHVDSEGR AAMVDVGRKP 500
    DTERVAVASA VVLLGPVAFK LVQQNQLKKG DALVVAQLAG VQAAKVTSQL 550
    IPLCHHVALS HIQVQLELDS TRHAVKIQAS CRARGPTGVE MEALTSAAVA 600
    ALTLYDMCKA VSRDIVLEEI KLISKTGGQR GDFHRA 636

    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. 1 interaction.
    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.
    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

    ArrayExpressi Q9NZB8.
    Bgeei Q9NZB8.
    CleanExi HS_MOCS1.
    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

    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 1, 2014
    This is version 125 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