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protein

Rho GTPase-activating protein 17

ARHGAP17
protein:Q68EM7disease:adad:direction:up

Gene

ARHGAP17

Organism

Homo sapiens(9606)

Length

881 aa

Mass

95,437 Da

AI summarysource-grounded · cited inline
claude-haiku-4-5-20251001

ARHGAP17 (Rho GTPase-activating protein 17) is a Rho family GTPase regulator that functions as a GTPase-activating protein for CDC42 and RAC1, converting them to inactive GDP-bound states (UniProt: Q68EM7). It plays a central role in maintaining epithelial tight junctions and apical polarity by regulating the uptake and trafficking of polarity proteins, and participates in calcium-dependent exocytosis through reorganization of cortical actin filaments.

ARHGAP17 is expressed in human tissues and operates within signaling pathways governing cell polarity and junction integrity. No disease associations are documented in the UniProt record, though the protein's role in cellular organization and membrane trafficking suggests broader biological significance in epithelial homeostasis.

In Alzheimer's Disease, ARHGAP17 shows elevated abundance in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics), with a mean log2 fold-change of 0.29 across measured fractions. This upregulation may reflect compensatory mechanisms or disease-associated remodeling of cellular polarity and membrane dynamics in AD pathology.

Generated from the curated entity record below. May contain errors — verify against source links.

Proteomics Evidence · AD

↑ Up in AD

P3

+0.286

P2

not detected

S2

not detected

S3

not detected

Mean log₂FC across detected fractions: +0.2857 (1 of 4 fractions detected)

Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.

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Function

Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1

Sources

Last updated 5/8/2026, 6:30:42 AM