Entity Details

Primary name GPC6
Entity type gene
Source Source Link

Details

PrimaryID10082
RefseqGeneNG_011880
SymbolGPC6
Nameglypican 6
Chromosome13
Location13q31.3-q32.1
TaxID9606
Statuslive
SourceGenomegenomic
SourceOriginnatural
CreationDate1999-05-24
ModificationDate2021-06-11

Ontological Relatives

UniProt IDsGPC6_HUMAN

GO terms

Show/Hide Table
GOName
GO:0001523 retinoid metabolic process
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005796 Golgi lumen
GO:0005886 plasma membrane
GO:0006024 glycosaminoglycan biosynthetic process
GO:0006027 glycosaminoglycan catabolic process
GO:0009966 regulation of signal transduction
GO:0009986 cell surface
GO:0016477 cell migration
GO:0043202 lysosomal lumen
GO:0045202 synapse
GO:0046658 anchored component of plasma membrane
GO:0062023 collagen-containing extracellular matrix
GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
GO:0098978 glutamatergic synapse
GO:0099560 synaptic membrane adhesion
GO:1904929 coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway
GO:1905475 regulation of protein localization to membrane
GO:1905606 regulation of presynapse assembly

Diseases

Show/Hide Table
Disease IDSourceNameDescription
258315 OMIMOmodysplasia 1 (OMOD1)A rare autosomal recessive skeletal dysplasia characterized by facial dysmorphism and severe congenital micromelia with shortening and distal tapering of the humeri and femora, to give a club-like appearance. Typical facial features include a prominent forehead, frontal bossing, short nose with a depressed broad bridge, short columella, anteverted nostrils, long philtrum, and small chin. The disease is caused by variants affecting the gene represented in this entry. Point mutations leading to protein truncation, as well as larger genomic rearrangements resulting in exon deletions, have been found in family segregating omodysplasia type 1. All mutations identified in individuals affected by omodysplasia could lead to the absence of a functional protein, the mutant RNAs being suspected to be nonsense-mediated mRNA decay (NMD) targets. Even if the mRNA escapes NMD and is translated, all mutations are expected to disrupt the three-dimensional protein structure and often to abolish multiple highly conserved cysteine residues.