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Protein

Molybdopterin synthase sulfur carrier subunit

Gene

MOCS2

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

Functioni

Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.UniRule annotation1 Publication

Miscellaneous

This protein is produced by a bicistronic gene which also produces the large subunit (MOCS2B) from an overlapping reading frame. Expression of these 2 proteins are related since a mutation that removes the start codon of the small subunit (MOCS2A) also impairs expression of the large subunit (MOCS2B).

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processMolybdenum cofactor biosynthesis
LigandNucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16667
ReactomeiR-HSA-947581 Molybdenum cofactor biosynthesis
UniPathwayiUPA00344

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin synthase sulfur carrier subunitUniRule annotation
Alternative name(s):
MOCO1-A
Molybdenum cofactor synthesis protein 2 small subunitUniRule annotation
Molybdenum cofactor synthesis protein 2AUniRule annotation
Short name:
MOCS2AUniRule annotation
Molybdopterin-synthase small subunit
Sulfur carrier protein MOCS2AUniRule annotation
Gene namesi
Name:MOCS2UniRule annotation
Synonyms:MOCO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000164172.18
HGNCiHGNC:7193 MOCS2
MIMi603708 gene
neXtProtiNX_O96033

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Molybdenum cofactor deficiency, complementation group B (MOCODB)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized by neonatal onset of intractable seizures, opisthotonus, and facial dysmorphism associated with hypouricemia and elevated urinary sulfite levels. Affected individuals show severe neurologic damage and often die in early childhood.
See also OMIM:252160
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0548547V → F in MOCODB; in a patient with mild form of the disease; impairs interaction with MOCS2B. 2 PublicationsCorresponds to variant dbSNP:rs121908608EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4338
MalaCardsiMOCS2
MIMi252160 phenotype
OpenTargetsiENSG00000164172
Orphaneti308393 Sulfite oxidase deficiency due to molybdenum cofactor deficiency type B
PharmGKBiPA30903

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002091341 – 88Molybdopterin synthase sulfur carrier subunitAdd BLAST88

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei881-thioglycine; alternateUniRule annotation5 Publications1
Modified residuei88Glycyl adenylate; alternateUniRule annotation1 Publication1

Post-translational modificationi

C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.UniRule annotation5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO96033
MaxQBiO96033
PeptideAtlasiO96033
PRIDEiO96033
ProteomicsDBi51223

PTM databases

iPTMnetiO96033

Expressioni

Tissue specificityi

Widely expressed. Highest levels are found in heart and skeletal muscle. Lower levels are present in brain, kidney and pancreas. Very low levels are found in lung and peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiENSG00000164172
CleanExiHS_MOCS2
ExpressionAtlasiO96033 baseline and differential
GenevisibleiO96033 HS

Interactioni

Subunit structurei

Heterotetramer; composed of 2 small (MOCS2A) and 2 large (MOCS2B) subunits.UniRule annotation

Protein-protein interaction databases

BioGridi110481, 5 interactors
CORUMiO96033
IntActiO96033, 3 interactors
MINTiO96033

Structurei

Secondary structure

188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi14 – 19Combined sources6
Beta strandi22 – 27Combined sources6
Beta strandi30 – 33Combined sources4
Helixi34 – 44Combined sources11
Helixi46 – 54Combined sources9
Beta strandi56 – 59Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi78 – 82Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MPOX-ray2.43A/B7-88[»]
ProteinModelPortaliO96033
SMRiO96033
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaD family. MOCS2A subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000047669
HOGENOMiHOG000280991

Family and domain databases

Gene3Di3.10.20.30, 1 hit
HAMAPiMF_03051 MOCS2A, 1 hit
InterProiView protein in InterPro
IPR012675 Beta-grasp_dom_sf
IPR028887 MOCS2A
IPR010034 Mopterin_su_1
IPR016155 Mopterin_synth/thiamin_S_b
IPR003749 ThiS/MoaD-like
PfamiView protein in Pfam
PF02597 ThiS, 1 hit
SUPFAMiSSF54285 SSF54285, 1 hit
TIGRFAMsiTIGR01682 moaD, 1 hit

Sequencei

Sequence statusi: Complete.

O96033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPLCQVEVL YFAKSAEITG VRSETISVPQ EIKALQLWKE IETRHPGLAD
60 70 80
VRNQIIFAVR QEYVELGDQL LVLQPGDEIA VIPPISGG
Length:88
Mass (Da):9,755
Last modified:May 1, 1999 - v1
Checksum:iBD08B374B615E7BE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0548547V → F in MOCODB; in a patient with mild form of the disease; impairs interaction with MOCS2B. 2 PublicationsCorresponds to variant dbSNP:rs121908608EnsemblClinVar.1
Natural variantiVAR_05009051V → A. Corresponds to variant dbSNP:rs2233210Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091871 mRNA Translation: AAD14598.1
AF117815 mRNA Translation: AAD13296.1
CCDSiCCDS47205.1
PIRiA59370
RefSeqiNP_789776.1, NM_176806.3
UniGeneiHs.163645
Hs.594335

Genome annotation databases

EnsembliENST00000361377; ENSP00000355160; ENSG00000164172
ENST00000450852; ENSP00000411022; ENSG00000164172
ENST00000508922; ENSP00000426274; ENSG00000164172
ENST00000510818; ENSP00000424267; ENSG00000164172
ENST00000582677; ENSP00000462870; ENSG00000164172
ENST00000584946; ENSP00000464663; ENSG00000164172
GeneIDi4338
UCSCiuc011cqf.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMOC2A_HUMAN
AccessioniPrimary (citable) accession number: O96033
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 1999
Last modified: June 20, 2018
This is version 140 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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