ECT2

ECT2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3L46, 4N40
Identifiers
Aliases	ECT2, ARHGEF31, epithelial cell transforming 2
External IDs	OMIM: 600586 MGI: 95281 HomoloGene: 7298 GeneCards: ECT2
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)[1]
End	27,153,878 bp[1]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• protein homodimerization activity; • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity; • signal transducer activity; • GO:0001948 protein binding; • Rho GTPase binding; • Rho guanyl-nucleotide exchange factor activity; • guanyl-nucleotide exchange factor activity;
Cellular component	• cytoplasm; • centralspindlin complex; • intercellular junction; • bicellular tight junction; • spindle; • cell junction; • midbody; • cleavage furrow; • mitotic spindle; • cytoskeleton; • cell nucleus; • cytosol;
Biological process	• cellular response to calcium ion; • cell differentiation; • GO:0007243 intracellular signal transduction; • GO:0032861, GO:0032862, GO:0032856 activation of GTPase activity; • nervous system development; • cell division; • positive regulation of cytokinesis; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • positive regulation of neuron differentiation; • bicellular tight junction assembly; • cell morphogenesis; • positive regulation of apoptotic process; • cellular response to ionizing radiation; • protein transport; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • positive regulation of protein import into nucleus; • cell cycle; • regulation of protein kinase activity; • regulation of Rho protein signal transduction; • regulation of attachment of spindle microtubules to kinetochore; • regulation of small GTPase mediated signal transduction; • protein homooligomerization; • activation of protein kinase activity; • cellular response to hydrogen peroxide; • transport; • mitotic cytokinesis; • cytokinesis; • G-protein coupled receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	1894
	13605
	ENSG00000114346
	ENSMUSG00000027699
	Q9H8V3
	Q07139
	NM_001258315; NM_001258316; NM_018098
	NM_001177625; NM_001177626; NM_007900
NP_001245244; NP_001245245; NP_060568; NP_001336023; NP_001336024;
	NP_001336025; NP_001336026; NP_001336027; NP_001336028; NP_001336029; NP_001336030; NP_001336031; NP_001336032; NP_001336033
	NP_001171096; NP_001171097; NP_031926
	Wikidata
View/Edit Human	View/Edit Mouse

Protein ECT2 is a protein that in humans is encoded by the ECT2 gene.[4][5][6]

Function

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.[6]

Interactions

ECT2 has been shown to interact with PARD6A.[7]

References

GRCm38: Ensembl release 89: ENSMUSG00000027699 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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. Bibcode:1993Natur.362..462M. doi:10.1038/362462a0. PMID 8464478. S2CID 722736.
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.
"Entrez Gene: ECT2 epithelial cell transforming sequence 2 oncogene".
Liu XF, Ishida H, Raziuddin R, Miki T (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. 24 (15): 6665–75. doi:10.1128/MCB.24.15.6665-6675.2004. PMC 444862. PMID 15254234.

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, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (1996). "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, Miki T, Narumiya S (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, Karnoub AE, Burridge K, Der CJ (2002). "RhoG signals in parallel with Rac1 and Cdc42". J. Biol. Chem. 277 (49): 47810–7. doi:10.1074/jbc.M203816200. PMID 12376551.
Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S (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, Chedid M, Kapoor V, Sakata H, Rubin J, Miki T (2003). "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, Dorkhom S, Kamijo K, Miki T (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.
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.
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, Higashida C, Kitamura T, Hiraoka Y, Haraguchi T, Narumiya S (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.
Yüce O, Piekny A, Glotzer M (2005). "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.
Niiya F, Xie X, Lee KS, Inoue H, Miki T (2005). "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. Bibcode:2005PNAS..10213158Z. doi:10.1073/pnas.0504145102. PMC 1201590. PMID 16129829.
Hara T, Abe M, Inoue H, Yu LR, Veenstra TD, Kang YH, Lee KS, Miki T (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.

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[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000027699 - 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.

[pmid8464478-4] 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. Bibcode:1993Natur.362..462M. doi:10.1038/362462a0. PMID 8464478. S2CID 722736.

[pmid10579713-5] 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.

[entrez-6] "Entrez Gene: ECT2 epithelial cell transforming sequence 2 oncogene".

[pmid15254234-7] Liu XF, Ishida H, Raziuddin R, Miki T (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. 24 (15): 6665–75. doi:10.1128/MCB.24.15.6665-6675.2004. PMC 444862. PMID 15254234.

ECT2

Function

Interactions

References

Further reading