MOGS

Protein identityUniProt · HPA

UniProt accession

Q13724

Gene

MOGS

Ensembl

ENSG00000115275

Chromosome

2

Canonical length

837 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Endoplasmic reticulum

OverviewNCBI Gene

This gene encodes the first enzyme in the N-linked oligosaccharide processing pathway. The enzyme cleaves the distal alpha-1,2-linked glucose residue from the Glc(3)-Man(9)-GlcNAc(2) oligosaccharide precursor. This protein is located in the lumen of the endoplasmic reticulum. Defects in this gene are a cause of type IIb congenital disorder of glycosylation (CDGIIb). Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2009]

Canonical amino-acid sequenceUniProt

837 residues, UniProt reviewed canonical sequence.

>Q13724|MOGS
     1  MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV LSLALGMSGR
    61  WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR PHVYFGMKTR SPKPLLTGLM
   121  WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF HDGLSFGRQH IQDGALRLTT EFVKRPGGQH
   181  GGDWSWRVTV EPQDSGTSAL PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF
   241  RFTLLPPTSP GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL
   301  PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP RLAGSLLTQA
   361  LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG GIGYFYGQGL VLPDIGVEGS
   421  EQKVDPALFP PVPLFTAVPS RSFFPRGFLW DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA
   481  DGWIGREQIL GDEARARVPP EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR
   541  LHAWFSWLHQ SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL
   601  RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG VFADFGNHTK
   661  AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR LLDPTSSRLG PLLDILADSR
   721  HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW RGAVWLNVNY LALGALHHYG HLEGPHQARA
   781  AKLHGELRAN VVGNVWRQYQ ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MOGS can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Other membrane

Secreted

No

Transmembrane segments

1

Mean surface accessibility (rSASA)

0.24

Highest tissue expression

40 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MOGS.

Disease | AllUniProt

Conditions MOGS is implicated in, by any mechanism.

• Type IIb congenital disorder of glycosylation (CDGIIb) MIM:606056

Disease | GeneticClinVar

38 pathogenic / likely-pathogenic of 628 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• MOGS-congenital disorder of glycosylation
• MOGS-related disorder

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.96

gnomAD pLI

0

gnomAD missense Z

0.66

DepMap mean gene effect

-0.2

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• oligosaccharide metabolic process
• protein folding
• protein N-linked glycosylation
• viral protein processing

Molecular functions

• Glc3Man9GlcNAc2 oligosaccharide glucosidase activity
• glucosidase activity

Cellular components

• endoplasmic reticulum
• endoplasmic reticulum membrane
• extracellular exosome
• membrane

Protein domainsUniProt · Pfam · InterPro

• Six-hairpin glycosidase superfamily
• Six-hairpin glycosidase-like superfamily
• Glycoside hydrolase family 63
• Glycosyl hydrolase family 63, C-terminal
• Glycosyl hydrolase family 63, N-terminal
• Glycosyl hydrolase family 63, N-terminal domain superfamily
• Glycosyl hydrolase family 63 C-terminal domain
• Glycosyl hydrolase family 63 N-terminal domain

KeywordsUniProt

• Endoplasmic reticulum
• Glycoprotein
• Glycosidase
• Hydrolase
• Membrane
• Signal-anchor
• Transmembrane
• Transmembrane helix

InteractionsUniProt · HPA

Protein binding partners of MOGS in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CANX