ECT2

Epithelial cell transforming sequence 2 oncogene

PDB rendering based on 2cou.

Available structures
PDB	2cou

Identifiers

Symbols

ECT2; ARHGEF31; FLJ10461; MGC138291

External IDs

OMIM: 600586 MGI: 95281 HomoloGene: 7298 GeneCards: ECT2 Gene

Gene Ontology
Molecular function	• signal transducer activity • guanyl-nucleotide exchange factor activity • Rho guanyl-nucleotide exchange factor activity • protein binding • Rho GTPase binding
Cellular component	• cytosol • cytosol
Biological process	• cell morphogenesis • apoptosis • signal transduction • small GTPase mediated signal transduction • induction of apoptosis by extracellular signals • regulation of Rho protein signal transduction • positive regulation of I-kappaB kinase/NF-kappaB cascade • nerve growth factor receptor signaling pathway • regulation of small GTPase mediated signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
172.47 – 172.54 Mb

Chr 3:
27 – 27.05 Mb

PubMed search

[1]

[2]

Protein ECT2 is a protein that in humans is encoded by the ECT2 gene.^[1]^[2]^[3]

The protein encoded by this gene is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis.^[3]

Interactions

ECT2 has been shown to interact with PARD6A.^[4]

References

^ Miki T, Smith CL, Long JE, Eva A, Fleming TP (Apr 1993). "Oncogene ect2 is related to regulators of small GTP-binding proteins". Nature 362 (6419): 462–5. doi:10.1038/362462a0. PMID 8464478.
^ Tatsumoto T, Xie X, Blumenthal R, Okamoto I, Miki T (Dec 1999). "Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis". J Cell Biol 147 (5): 921–8. doi:10.1083/jcb.147.5.921. PMC 2169345. PMID 10579713. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2169345.
^ ^a ^b "Entrez Gene: ECT2 epithelial cell transforming sequence 2 oncogene". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1894.
^ Liu, Xiu-Fen; Ishida Hiroshi, Raziuddin Razi, Miki Toru (Aug. 2004). "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity". Mol. Cell. Biol. (United States) 24 (15): 6665–75. doi:10.1128/MCB.24.15.6665-6675.2004. ISSN 0270-7306. PMC 444862. PMID 15254234. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=444862.

Takai S, Long JE, Yamada K, Miki T (1995). "Chromosomal localization of the human ECT2 proto-oncogene to 3q26.1→q26.2 by somatic cell analysis and fluorescence in situ hybridization.". Genomics 27 (1): 220–2. doi:10.1006/geno.1995.1033. PMID 7665179.
Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
Kimura K, Tsuji T, Takada Y, et al. (2000). "Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation.". J. Biol. Chem. 275 (23): 17233–6. doi:10.1074/jbc.C000212200. PMID 10837491.
Wennerberg K, Ellerbroek SM, Liu RY, et al. (2003). "RhoG signals in parallel with Rac1 and Cdc42.". J. Biol. Chem. 277 (49): 47810–7. doi:10.1074/jbc.M203816200. PMID 12376551.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Matsuda A, Suzuki Y, Honda G, et al. (2003). "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways.". Oncogene 22 (21): 3307–18. doi:10.1038/sj.onc.1206406. PMID 12761501.
Saito S, Tatsumoto T, Lorenzi MV, et al. (2004). "Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains.". J. Cell. Biochem. 90 (4): 819–36. doi:10.1002/jcb.10688. PMID 14587037.
Hara T, Ishida H, Raziuddin R, et al. (2004). "Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells.". Mol. Biol. Cell 15 (3): 1172–84. doi:10.1091/mbc.E03-07-0531. PMC 363103. PMID 14668487. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=363103.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Liu XF, Ishida H, Raziuddin R, Miki T (2004). "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity.". Mol. Cell. Biol. 24 (15): 6665–75. doi:10.1128/MCB.24.15.6665-6675.2004. PMC 444862. PMID 15254234. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=444862.
Kim JE, Billadeau DD, Chen J (2005). "The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis.". J. Biol. Chem. 280 (7): 5733–9. doi:10.1074/jbc.M409298200. PMID 15545273.
Oceguera-Yanez F, Kimura K, Yasuda S, et al. (2005). "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis.". J. Cell Biol. 168 (2): 221–32. doi:10.1083/jcb.200408085. PMC 2171585. PMID 15642749. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2171585.
Yüce O, Piekny A, Glotzer M (2007). "An ECT2-centralspindlin complex regulates the localization and function of RhoA.". J. Cell Biol. 170 (4): 571–82. doi:10.1083/jcb.200501097. PMC 2171506. PMID 16103226. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2171506.
Niiya F, Xie X, Lee KS, et al. (2006). "Inhibition of cyclin-dependent kinase 1 induces cytokinesis without chromosome segregation in an ECT2 and MgcRacGAP-dependent manner.". J. Biol. Chem. 280 (43): 36502–9. doi:10.1074/jbc.M508007200. PMID 16118207.
Zhao WM, Fang G (2005). "MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis.". Proc. Natl. Acad. Sci. U.S.A. 102 (37): 13158–63. doi:10.1073/pnas.0504145102. PMC 1201590. PMID 16129829. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1201590.
Hara T, Abe M, Inoue H, et al. (2006). "Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase.". Oncogene 25 (4): 566–78. doi:10.1038/sj.onc.1209078. PMID 16170345.
Niiya F, Tatsumoto T, Lee KS, Miki T (2006). "Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA.". Oncogene 25 (6): 827–37. doi:10.1038/sj.onc.1209124. PMID 16247472.
Nishimura Y, Yonemura S (2006). "Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis.". J. Cell. Sci. 119 (Pt 1): 104–14. doi:10.1242/jcs.02737. PMID 16352658.

PDB gallery

2cou: Solution structure of the second BRCT domain of epithelial cell transforming 2

ECT2

Interactions

References

Further reading