ARHGAP31

The Rho GTPase activating protein 31 is encoded in humans by the ARHGAP31 gene. It is a Cdc42/Rac1 GTPase regulator.[5]

ARHGAP31
Identifiers
Aliases	ARHGAP31, AOS1, CDGAP, Rho GTPase activating protein 31
External IDs	OMIM: 610911 MGI: 1333857 HomoloGene: 10644 GeneCards: ARHGAP31
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q13.32-q13.33 Start 119,294,383 bp[1] End 119,420,714 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 B4 Start 38,598,340 bp[2] End 38,713,274 bp[2]
Gene ontology Molecular function • SH3 domain binding • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity Cellular component • cytosol • cell junction • cell projection • focal adhesion • lamellipodium Biological process • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • regulation of small GTPase mediated signal transduction • signal transduction • small GTPase mediated signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	57514	12549
Ensembl	ENSG00000031081	ENSMUSG00000022799
UniProt	Q2M1Z3	A6X8Z5
RefSeq (mRNA)	NM_020754	NM_020260
RefSeq (protein)	NP_065805	NP_064656
Location (UCSC)	Chr 3: 119.29 – 119.42 Mb	Chr 16: 38.6 – 38.71 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

ARHGAP31 encodes a GTPase-activating protein (GAP). A variety of cellular processes are regulated by Rho GTPases which cycle between an inactive form bound to GDP and an active form bound to GTP. This cycling between inactive and active forms is regulated by guanine nucleotide exchange factors and GAPs. The encoded protein is a GAP shown to regulate two GTPases involved in protein trafficking and cell growth.[5]

Clinical relevance

ARHGAP31 mutations result in a loss of available active Cdc42 and consequently disrupt actin cytoskeletal structures, causing syndromic cutis aplasia and limb anomalies.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000031081 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022799 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene".
6. Southgate L, Machado RD, Snape KM, Primeau M, Dafou D, Ruddy DM, Branney PA, Fisher M, Lee GJ, Simpson MA, He Y, Bradshaw TY, Blaumeiser B, Winship WS, Reardon W, Maher ER, Fitzpatrick DR, Wuyts W, Zenker M, Lamarche-Vane N, Trembath RC (May 2011). "Gain-of-Function Mutations of ARHGAP31, a Cdc42/Rac1 GTPase Regulator, Cause Syndromic Cutis Aplasia and Limb Anomalies". Am. J. Hum. Genet. 88 (5): 574–85. doi:10.1016/j.ajhg.2011.04.013. PMC 3146732. PMID 21565291.

External links

• Human ARHGAP31 genome location and ARHGAP31 gene details page in the UCSC Genome Browser.

Further reading

• Bandyopadhyay S, Chiang CY, Srivastava J, et al. (2010). "A human MAP kinase interactome". Nat. Methods. 7 (10): 801–5. doi:10.1038/nmeth.1506. PMC 2967489. PMID 20936779.
• Jenna S, Hussain NK, Danek EI, et al. (2002). "The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin". J. Biol. Chem. 277 (8): 6366–73. doi:10.1074/jbc.M105516200. PMID 11744688.
• Zhao C, Ma H, Bossy-Wetzel E, et al. (2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Danek EI, Tcherkezian J, Triki I, et al. (2007). "Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1 regulatory site". J. Biol. Chem. 282 (6): 3624–31. doi:10.1074/jbc.M610073200. PMID 17158447.
• Nagase T, Ishikawa K, Kikuno R, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (5): 337–45. doi:10.1093/dnares/6.5.337. PMID 10574462.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tcherkezian J, Triki I, Stenne R, et al. (2006). "The human orthologue of CdGAP is a phosphoprotein and a GTPase-activating protein for Cdc42 and Rac1 but not RhoA". Biol. Cell. 98 (8): 445–56. doi:10.1042/BC20050101. PMID 16519628. S2CID 25545141.
• Dubois PC, Trynka G, Franke L, et al. (2010). "Multiple common variants for celiac disease influencing immune gene expression". Nat. Genet. 42 (4): 295–302. doi:10.1038/ng.543. PMC 2847618. PMID 20190752.
• Lamarche-Vane N, Hall A (1998). "CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and Rac". J. Biol. Chem. 273 (44): 29172–7. doi:10.1074/jbc.273.44.29172. PMID 9786927.
• Horne BD, Hauser ER, Wang L, et al. (2009). "Validation study of genetic associations with coronary artery disease on chromosome 3q13-21 and potential effect modification by smoking". Ann. Hum. Genet. 73 (Pt 6): 551–8. doi:10.1111/j.1469-1809.2009.00540.x. PMC 2764812. PMID 19706030.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.