CDC42EP2

Cdc42 effector protein 2 is a protein that in humans is encoded by the CDC42EP2 gene.[4][5][6]

CDC42EP2
Identifiers
Aliases	CDC42EP2, BORG1, CEP2, CDC42 effector protein 2
External IDs	OMIM: 606132 MGI: 1929744 HomoloGene: 4933 GeneCards: CDC42EP2
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.1 Start 65,314,866 bp[1] End 65,322,417 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GTP-Rho binding • GO:0001948 protein binding • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • opioid peptide activity Cellular component • cytoplasm • microtubule cytoskeleton • cell membrane • membrane • endomembrane system • cytoskeleton • cytosol • phagocytic vesicle Biological process • positive regulation of pseudopodium assembly • positive regulation of actin filament polymerization • positive regulation of protein complex assembly • actin cytoskeleton organization • Rho protein signal transduction • actin filament organization • regulation of cell shape • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • regulation of receptor activity • cellular response to interferon-gamma Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10435	104252
Ensembl	ENSG00000149798	n/a
UniProt	O14613	Q8JZX9
RefSeq (mRNA)	NM_006779	NM_026772
RefSeq (protein)	NP_006770	NP_081048
Location (UCSC)	Chr 11: 65.31 – 65.32 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Function

CDC42, a small Rho GTPase, regulates the formation of F-actin-containing structures through its interaction with the downstream effector proteins. The protein encoded by this gene is a member of the Borg family of CDC42 effector proteins. Borg family proteins contain a CRIB (Cdc42/Rac interactive-binding) domain. They bind to, and negatively regulate the function of, CDC42. Coexpression of this protein with dominant negative mutant CDC42 protein in fibroblast was found to induce pseudopodia formation, which suggested a role of this protein in actin filament assembly and cell shape control.[6]

Interactions

CDC42EP2 has been shown to interact with CDC42[4][5] and RHOQ.[4]

References

1. GRCh38: Ensembl release 89: ENSG00000149798 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Joberty G, Perlungher RR, Macara IG (Oct 1999). "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins". Molecular and Cellular Biology. 19 (10): 6585–97. doi:10.1128/MCB.19.10.6585. PMC 84628. PMID 10490598.
5. Hirsch DS, Pirone DM, Burbelo PD (Jan 2001). "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes". The Journal of Biological Chemistry. 276 (2): 875–83. doi:10.1074/jbc.M007039200. PMID 11035016.
6. "Entrez Gene: CDC42EP2 CDC42 effector protein (Rho GTPase binding) 2".

External links

• Human CDC42EP2 genome location and CDC42EP2 gene details page in the UCSC Genome Browser.

Further reading

• Guru SC, Agarwal SK, Manickam P, Olufemi SE, Crabtree JS, Weisemann JM, Kester MB, Kim YS, Wang Y, Emmert-Buck MR, Liotta LA, Spiegel AM, Boguski MS, Roe BA, Collins FS, Marx SJ, Burns L, Chandrasekharappa SC (Jul 1997). "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus". Genome Research. 7 (7): 725–35. doi:10.1101/gr.7.7.725. PMC 310681. PMID 9253601.
• Burbelo PD, Snow DM, Bahou W, Spiegel S (Aug 1999). "MSE55, a Cdc42 effector protein, induces long cellular extensions in fibroblasts". Proceedings of the National Academy of Sciences of the United States of America. 96 (16): 9083–8. doi:10.1073/pnas.96.16.9083. PMC 17736. PMID 10430899.
• Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, Macara IG (Oct 2001). "Borg proteins control septin organization and are negatively regulated by Cdc42". Nature Cell Biology. 3 (10): 861–6. doi:10.1038/ncb1001-861. PMID 11584266.
• Xue Y, Bi F, Zhang X, Zhang S, Pan Y, Liu N, Shi Y, Yao X, Zheng Y, Fan D (Jun 2006). "Role of Rac1 and Cdc42 in hypoxia induced p53 and von Hippel-Lindau suppression and HIF1alpha activation". International Journal of Cancer. 118 (12): 2965–72. doi:10.1002/ijc.21763. PMID 16395716.