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GeneQ18034884· pop 5· linked from 2 articles

Also known as ARF-GEP100, ARFGEP100, BRAG2, GEP100, IQ motif and Sec7 domain 1, IQ motif and Sec7 domain ArfGEF 1, IDDSSBA

IQ motif and SEC7 domain-containing protein 1 also known as ARF-GEP100 (ADP-Ribosylation Factor - Guanine nucleotide-Exchange Protein - 100-kDa) is a protein that in humans is encoded by the IQSEC1 gene.

Gene data

IQSEC1
Name
IQ motif and Sec7 domain ArfGEF 1
Type
protein-coding
Aliases
ARF-GEP100, ARFGEP100, BRAG2, GEP100, IDDSSBA

Predicted to enable protein kinase binding activity. Predicted to be involved in several processes, including positive regulation of focal adhesion disassembly; positive regulation of keratinocyte migration; and regulation of postsynaptic neurotransmitter receptor internalization. Located in nucleolus. Implicated in intellectual developmental disorder with short stature and behavioral abnormalities. [provided by Alliance of Genome Resources, Apr 2022]

via MyGene.info

Wikidata facts

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HomoloGene ID
82429
genomic end
13283281
genomic start
12897043
cytogenetic location
3p25.2-p25.1
Sources (3)

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Article

4 sections
Contents
  • Function
  • References
  • Further reading
  • External links

IQ motif and SEC7 domain-containing protein 1 also known as ARF-GEP100 (ADP-Ribosylation Factor - Guanine nucleotide-Exchange Protein - 100-kDa) is a protein that in humans is encoded by the IQSEC1 gene.

==Function== The ARF-GEP100 protein is involved in signal transduction. It is a guanine nucleotide exchange factor that promotes binding of GTP to ADP ribosylation factor protein ARF6 and to a lesser extent ARF1 and ARF5. This activates the ADP-ribosylation activity of the target protein and cause it to modify its substrates. ARF-GEP100, through activation of ARF6, is therefore involved in the control of processes such as endocytosis of plasma membrane proteins, E-cadherin recycling and actin cytoskeleton remodeling. ARF-GEP100 appears particularly important in regulating cell adhesion, with reductions in the level of this protein causing enhanced spreading and attachment of cells.

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