Q9H8V3 (ECT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein ECT2

Alternative name(s):
Epithelial cell-transforming sequence 2 oncogene

Gene names

Name:

ECT2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27
Subunit structure	Interacts with NR1I3 By similarity. Homomdimer. Homooligomer. Found in the centralspindlin complex. Interacts (Thr-359 phosphorylated form) with PARD6A; the interaction is observed in cancer cells. Interacts (Thr-359 phosphorylated form) with PRKCI; the interaction is observed in cancer cells. Interacts with PKP4; the interaction is observed at the midbody. Interacts with RACGAP1; the interaction is direct, occurs in a microtubule-dependent manner, is inhibited in metaphase by phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity. Interacts with PLK1; the interaction is stimulated upon its phosphorylation on Thr-444. Associates with RACGAP1 at anaphase and during cytokinesis. Interacts with KIF23, PARD3, PARD6A, PARD6B and PRKCQ. Ref.3 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25
Subcellular location	Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › spindle. Cleavage furrow. Midbody. Cell junction. Cell junction › tight junction. Note: Sequestered within the nucleus during interphase. Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis. Colocalizes with the centralspindlin complex to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis. Colocalized with RhoA at the midbody. Its subcellular localization to tight junction is increased by calcium. Localized predominantly in the cytoplasm of numerous carcinoma cells. Ref.1 Ref.3 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.23 Ref.24
Tissue specificity	Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma. Ref.23
Induction	Up-regulated by calcium in cells forming cell-cell contact sites. Up-regulated by DNA damaging agents like H2O2 or ionizing radiation (IR). Ref.9 Ref.27
Domain	The BRCT domain 1 and 2 are required for the intramolecular interaction, but not for the intermolecular oligomerization. The BRCT domains negatively inhibit its GEF activity in interphase cells. The same BRCT domains may act as a positive regulatory motif for the completion of cytokinesis after the breakdown of nuclear membrane during mitosis.
Post-translational modification	Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2 phase of the cell cycle. Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity. Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation. Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359 is required for its transformation activity in cancer cells. Ref.1 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.26
Sequence similarities	Contains 2 BRCT domains. Contains 1 DH (DBL-homology) domain. Contains 1 PH domain.
Sequence caution	The sequence BAA91624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Neurogenesis Protein transport Transport
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus Tight junction
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Oncogene
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of Rac GTPase activity Inferred from mutant phenotype Ref.23. Source: UniProtKB activation of protein kinase activity Inferred from direct assay Ref.9. Source: UniProtKB apoptotic process Traceable author statement. Source: Reactome cell cycle cytokinesis Inferred from mutant phenotype Ref.15. Source: UniProtKB cellular response to calcium ion Inferred from direct assay Ref.9. Source: UniProtKB cellular response to hydrogen peroxide Inferred from direct assay Ref.27. Source: UniProtKB cellular response to ionizing radiation Inferred from direct assay Ref.27. Source: UniProtKB induction of apoptosis by extracellular signals Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of Cdc42 GTPase activity Inferred from direct assay Ref.23. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from direct assay Ref.10. Source: UniProtKB positive regulation of neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from direct assay Ref.10. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of attachment of spindle microtubules to kinetochore Inferred from mutant phenotype Ref.11. Source: UniProtKB small GTPase mediated signal transduction Traceable author statement. Source: Reactome tight junction assembly Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular component	centralspindlin complex Inferred from direct assay Ref.15. Source: UniProtKB cleavage furrow Inferred from direct assay Ref.12. Source: UniProtKB cytosol Traceable author statement. Source: Reactome midbody Inferred from direct assay Ref.10Ref.12Ref.24. Source: UniProtKB nucleus Inferred from direct assay Ref.9Ref.12Ref.23. Source: UniProtKB tight junction Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	GTPase activator activity Inferred from mutant phenotype Ref.11. Source: UniProtKB Rho guanyl-nucleotide exchange factor activity Inferred from direct assay Ref.9Ref.10. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.10. Source: UniProtKB signal transducer activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	3	EBI-1054039,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H8V3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9H8V3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: Missing.
     71-101: Missing.

Isoform 3 (identifier: Q9H8V3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     886-914: GIPSPSLVSLPSFFERRSHTLSRSTTHLI → ITHSVSTSNV...SKSSLTFVKN

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 914

914

Protein ECT2

PRO_0000080938

Regions

Domain

171 – 260

90

BRCT 1

Domain

266 – 354

89

BRCT 2

Domain

452 – 641

190

DH

Domain

675 – 794

120

PH

Motif

378 – 382

5

Nuclear localization signal

Motif

401 – 405

5

Nuclear localization signal

Amino acid modifications

Modified residue

40

1

Phosphoserine Ref.19

Modified residue

359

1

Phosphothreonine; by PKC/PRKCI Ref.16 Ref.26

Modified residue

367

1

Phosphoserine Ref.21

Modified residue

370

1

Phosphoserine Ref.21

Modified residue

373

1

Phosphothreonine; by CDK1 Ref.17 Ref.21

Modified residue

376

1

Phosphoserine Ref.21

Modified residue

444

1

Phosphothreonine; by CDK1

Modified residue

842

1

Phosphoserine Ref.21

Modified residue

846

1

Phosphothreonine; by CDK1 Ref.21

Modified residue

889

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

44

1

Missing in isoform 2.

VSP_041976

Alternative sequence

71 – 101

31

Missing in isoform 2.

VSP_041977

Alternative sequence

886 – 914

29

GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3.

VSP_041978

Natural variant

15

1

S → T.
Corresponds to variant rs34703432 [ dbSNP | Ensembl ].

VAR_047064

Natural variant

833

1

T → P in a breast cancer sample; somatic mutation. Ref.29

VAR_035975

Experimental info

Mutagenesis

184

1

T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. Ref.24

Mutagenesis

226

1

K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. Ref.24

Mutagenesis

336

1

W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. Ref.10

Mutagenesis

359

1

T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. Ref.26

Mutagenesis

373

1

T → A: Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells. Ref.12 Ref.17

Mutagenesis

373

1

T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. Ref.12 Ref.17

Mutagenesis

379 – 381

3

KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity.

Mutagenesis

402 – 404

3

RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. Ref.8

Mutagenesis

444

1

T → A: Diminishes its phosphorylation status. Reduces its interaction with PLK1 and Rho exchange activity. Does not change its subcellular localization. Does not inhibit anchorage-independent growth and invasion in cancer cells. Ref.18

Mutagenesis

444

1

T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. Ref.18

Mutagenesis

596 – 599

4

PVQR → AAAA: Inhibits activation of the transforming activity. Ref.8

Mutagenesis

846

1

T → A: Diminishes its phosphorylation status. Ref.18

Sequence conflict

66

1

I → T in BAB14498. Ref.5

Sequence conflict

276

1

L → F in BAB14498. Ref.5

Sequence conflict

393

1

E → D in BAB14498. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

914

Helix Strand Turn

Details...

Turn

270 – 273

4

Helix

283 – 295

13

Beta strand

309 – 313

5

Turn

315 – 317

3

Beta strand

318 – 320

3

Beta strand

330 – 333

4

Helix

334 – 337

4

Turn

341 – 344

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 16, 2011. Version 4. Checksum: F40FC4F982FB8C78	FASTA	914	103,505
	10 20 30 40 50 60 MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE TRVILVQEAG 70 80 90 100 110 120 KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN MDIKVGFVKM ESVEEFEGLD 130 140 150 160 170 180 SPEFENVFVV TDFQDSVFND LYKADCRVIG PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV 190 200 210 220 230 240 LCFTGFRKKE ELVRLVTLVH HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP 250 260 270 280 290 300 EWIYKAWERR NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 310 320 330 340 350 360 LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET MYLYEKANTP 370 380 390 400 410 420 ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP PRKRPSAEHS LSIGSLLDIS 430 440 450 460 470 480 NTPESSINYG DTPKSCTKSS KSSTPVPSKQ SARWQVAKEL YQTESNYVNI LATIIQLFQV 490 500 510 520 530 540 PLEEEGQRGG PILAPEEIKT IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS 550 560 570 580 590 600 KDLVKTYPPF VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 610 620 630 640 650 660 PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ IFDVVYEVDG 670 680 690 700 710 720 CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC LEIARKRHKV IGTFRSPHGQ 730 740 750 760 770 780 TRPPASLKHI HLMPLSQIKK VLDIRETEDC HNAFALLVRP PTEQANVLLS FQMTSDELPK 790 800 810 820 830 840 ENWLKMLCRH VANTICKADA ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA 850 860 870 880 890 900 FSFSKTPKRA LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAGIPSP SLVSLPSFFE 910 RRSHTLSRST THLI
	Isoform 2 [UniParc]. Checksum: AAD4483A503D086C	FASTA	882	99,921
	10 20 30 40 50 60 MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEMPQIET RVILVQEAGK 70 80 90 100 110 120 QEELIKALKD IKVGFVKMES VEEFEGLDSP EFENVFVVTD FQDSVFNDLY KADCRVIGPP 130 140 150 160 170 180 VVLNCSQKGE PLPFSCRPLY CTSMMNLVLC FTGFRKKEEL VRLVTLVHHM GGVIRKDFNS 190 200 210 220 230 240 KVTHLVANCT QGEKFRVAVS LGTPIMKPEW IYKAWERRNE QDFYAAVDDF RNEFKVPPFQ 250 260 270 280 290 300 DCILSFLGFS DEEKTNMEEM TEMQGGKYLP LGDERCTHLV VEENIVKDLP FEPSKKLYVV 310 320 330 340 350 360 KQEWFWGSIQ MDARAGETMY LYEKANTPEL KKSVSMLSLN TPNSNRKRRR LKETLAQLSR 370 380 390 400 410 420 ETDVSPFPPR KRPSAEHSLS IGSLLDISNT PESSINYGDT PKSCTKSSKS STPVPSKQSA 430 440 450 460 470 480 RWQVAKELYQ TESNYVNILA TIIQLFQVPL EEEGQRGGPI LAPEEIKTIF GSIPDIFDVH 490 500 510 520 530 540 TKIKDDLEDL IVNWDESKSI GDIFLKYSKD LVKTYPPFVN FFEMSKETII KCEKQKPRFH 550 560 570 580 590 600 AFLKINQAKP ECGRQSLVEL LIRPVQRLPS VALLLNDLKK HTADENPDKS TLEKAIGSLK 610 620 630 640 650 660 EVMTHINEDK RKTEAQKQIF DVVYEVDGCP ANLLSSHRSL VQRVETISLG EHPCDRGEQV 670 680 690 700 710 720 TLFLFNDCLE IARKRHKVIG TFRSPHGQTR PPASLKHIHL MPLSQIKKVL DIRETEDCHN 730 740 750 760 770 780 AFALLVRPPT EQANVLLSFQ MTSDELPKEN WLKMLCRHVA NTICKADAEN LIYTADPESF 790 800 810 820 830 840 EVNTKDMDST LSRASRAIKK TSKKVTRAFS FSKTPKRALR RALMTSHGSV EGRSPSSNDK 850 860 870 880 HVMSRLSSTS SLAGIPSPSL VSLPSFFERR SHTLSRSTTH LI
	Isoform 3 [UniParc]. Checksum: F505EBBF2E1BBE23	FASTA	958	108,529
	10 20 30 40 50 60 MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE TRVILVQEAG 70 80 90 100 110 120 KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN MDIKVGFVKM ESVEEFEGLD 130 140 150 160 170 180 SPEFENVFVV TDFQDSVFND LYKADCRVIG PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV 190 200 210 220 230 240 LCFTGFRKKE ELVRLVTLVH HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP 250 260 270 280 290 300 EWIYKAWERR NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 310 320 330 340 350 360 LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET MYLYEKANTP 370 380 390 400 410 420 ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP PRKRPSAEHS LSIGSLLDIS 430 440 450 460 470 480 NTPESSINYG DTPKSCTKSS KSSTPVPSKQ SARWQVAKEL YQTESNYVNI LATIIQLFQV 490 500 510 520 530 540 PLEEEGQRGG PILAPEEIKT IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS 550 560 570 580 590 600 KDLVKTYPPF VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 610 620 630 640 650 660 PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ IFDVVYEVDG 670 680 690 700 710 720 CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC LEIARKRHKV IGTFRSPHGQ 730 740 750 760 770 780 TRPPASLKHI HLMPLSQIKK VLDIRETEDC HNAFALLVRP PTEQANVLLS FQMTSDELPK 790 800 810 820 830 840 ENWLKMLCRH VANTICKADA ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA 850 860 870 880 890 900 FSFSKTPKRA LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAITHSV STSNVIGFTK 910 920 930 940 950 HVYVQRLNST GGRSQYSWFQ SVRHSAFRAS FSEILEGNTD FSNFKKVLSK SSLTFVKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis." Tatsumoto T., Xie X., Blumenthal R., Okamoto I., Miki T. J. Cell Biol. 147:921-928(1999) [PubMed: 10579713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[2]	"Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains." Saito S., Tatsumoto T., Lorenzi M.V., Chedid M., Kapoor V., Sakata H., Rubin J.S., Miki T. J. Cell. Biochem. 90:819-836(2003) [PubMed: 14587037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"The armadillo protein p0071 regulates Rho signalling during cytokinesis." Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M. Nat. Cell Biol. 8:1432-1440(2006) [PubMed: 17115030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PKP4, SUBCELLULAR LOCATION.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Teratocarcinoma and Testis.
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 662-914 (ISOFORM 3). Tissue: Testis.
[8]	"Deregulation and mislocalization of the cytokinesis regulator ECT2 activate the Rho signaling pathways leading to malignant transformation." Saito S., Liu X.F., Kamijo K., Raziuddin R., Tatsumoto T., Okamoto I., Chen X., Lee C.C., Lorenzi M.V., Ohara N., Miki T. J. Biol. Chem. 279:7169-7179(2004) [PubMed: 14645260] [Abstract] Cited for: FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 379-ARG--ARG-381; 402-ARG--ARG-404 AND 596-PRO--ARG-599.
[9]	"Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity." Liu X.F., Ishida H., Raziuddin R., Miki T. Mol. Cell. Biol. 24:6665-6675(2004) [PubMed: 15254234] [Abstract] Cited for: FUNCTION, INTERACTION WITH PARD3; PARD6A; PARD6B AND PRKCQ, INDUCTION, SUBCELLULAR LOCATION.
[10]	"The tandem BRCT domains of Ect2 are required for both negative and positive regulation of Ect2 in cytokinesis." Kim J.E., Billadeau D.D., Chen J. J. Biol. Chem. 280:5733-5739(2005) [PubMed: 15545273] [Abstract] Cited for: FUNCTION, HOMODIMERIZATION, HOMOOLIGOMERIZATION, MUTAGENESIS OF TRP-336.
[11]	"Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis." Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S. J. Cell Biol. 168:221-232(2005) [PubMed: 15642749] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"An ECT2-centralspindlin complex regulates the localization and function of RhoA." Yuce O., Piekny A., Glotzer M. J. Cell Biol. 170:571-582(2005) [PubMed: 16103226] [Abstract] Cited for: FUNCTION, INTERACTION WITH RACGAP1, MUTAGENESIS OF THR-373, SUBCELLULAR LOCATION.
[13]	"MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis." Zhao W.-M., Fang G. Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005) [PubMed: 16129829] [Abstract] Cited for: INTERACTION WITH RACGAP1.
[14]	"Nucleotide exchange factor ECT2 regulates epithelial cell polarity." Liu X.F., Ohno S., Miki T. Cell. Signal. 18:1604-1615(2006) [PubMed: 16495035] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Dissecting the role of Rho-mediated signaling in contractile ring formation." Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T. Mol. Biol. Cell 17:43-55(2006) [PubMed: 16236794] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION.
[16]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Cytokinesis regulator ECT2 changes its conformation through phosphorylation at Thr-341 in G2/M phase." Hara T., Abe M., Inoue H., Yu L.R., Veenstra T.D., Kang Y.H., Lee K.S., Miki T. Oncogene 25:566-578(2006) [PubMed: 16170345] [Abstract] Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-373, MUTAGENESIS OF THR-373.
[18]	"Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA." Niiya F., Tatsumoto T., Lee K.S., Miki T. Oncogene 25:827-837(2006) [PubMed: 16247472] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH PLK1, MUTAGENESIS OF THR-444 AND THR-846.
[19]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-889, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis." Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R. EMBO J. 27:1791-1803(2008) [PubMed: 18511905] [Abstract] Cited for: INTERACTION WITH RAB11FIP3.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-370; THR-373; SER-376; SER-842 AND THR-846, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Centrosome/spindle pole-associated protein regulates cytokinesis via promoting the recruitment of MyoGEF to the central spindle." Asiedu M., Wu D., Matsumura F., Wei Q. Mol. Biol. Cell 20:1428-1440(2009) [PubMed: 19129481] [Abstract] Cited for: FUNCTION.
[23]	"Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular transformation." Justilien V., Fields A.P. Oncogene 28:3597-3607(2009) [PubMed: 19617897] [Abstract] Cited for: FUNCTION, INTERACTION WITH PARD6A AND PRKCI, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[24]	"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation." Wolfe B.A., Takaki T., Petronczki M., Glotzer M. PLoS Biol. 7:E1000110-E1000110(2009) [PubMed: 19468300] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-184 AND LYS-226.
[25]	"Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells." Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V. PLoS Biol. 7:E1000111-E1000111(2009) [PubMed: 19468302] [Abstract] Cited for: INTERACTION WITH RACGAP1.
[26]	"Oncogenic activity of Ect2 is regulated through protein kinase C iota-mediated phosphorylation." Justilien V., Jameison L., Der C.J., Rossman K.L., Fields A.P. J. Biol. Chem. 286:8149-8157(2011) [PubMed: 21189248] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-359, MUTAGENESIS OF THR-359, IDENTIFICATION BY MASS SPECTROMETRY.
[27]	"The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate RhoB-mediated cell death after DNA damage." Srougi M.C., Burridge K. PLoS ONE 6:E17108-E17108(2011) [PubMed: 21373644] [Abstract] Cited for: FUNCTION, INDUCTION.
[28]	"Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)." Structural genomics consortium (SGC) Submitted (JAN-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 268-361.
[29]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-833.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY376439 mRNA. Translation: AAQ83675.1.
DQ847274 mRNA. Translation: ABH10140.1.
AK001323 mRNA. Translation: BAA91624.1. Different initiation.
AK023267 mRNA. Translation: BAB14498.1.
AK314581 mRNA. Translation: BAG37157.1.
AC108667 Genomic DNA. No translation available.
BC112086 mRNA. Translation: AAI12087.1.
AL137710 mRNA. Translation: CAB70886.1.

IPI

IPI00748143.
IPI00794284.

RefSeq

NP_060568.3. NM_018098.4.

UniGene

Hs.518299.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L46	X-ray	1.48	A/B	268-361	[»]

ProteinModelPortal

Q9H8V3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47496N.

IntAct

Q9H8V3. 4 interactions.

MINT

MINT-6166617.

STRING

Q9H8V3.

PTM databases

PhosphoSite

Q9H8V3.

Polymorphism databases

DMDM

212276511.

Proteomic databases

PRIDE

Q9H8V3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000232458; ENSP00000232458; ENSG00000114346.
ENST00000392692; ENSP00000376457; ENSG00000114346.
ENST00000417960; ENSP00000415876; ENSG00000114346.
ENST00000441497; ENSP00000412259; ENSG00000114346.
ENST00000540509; ENSP00000443160; ENSG00000114346.

GeneID

1894.

KEGG

hsa:1894.

Organism-specific databases

CTD

1894.

GeneCards

GC03P172468.

H-InvDB

HIX0003865.

HGNC

HGNC:3155. ECT2.

MIM

600586. gene.

neXtProt

NX_Q9H8V3.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084097.

HOVERGEN

HBG005563.

OMA

ICKADAE.

OrthoDB

EOG4GHZNG.

PhylomeDB

Q9H8V3.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9H8V3.

Bgee

Q9H8V3.

CleanEx

HS_ECT2.

Genevestigator

Q9H8V3.

Family and domain databases

InterPro

IPR001357. BRCT.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:1.20.900.10. RhoGEF. 1 hit.

Pfam

PF00533. BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 2 hits.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 2 hits.
SSF48065. DH-domain. 1 hit.

PROSITE

PS50172. BRCT. 2 hits.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

ECT2_HUMAN

Accession

Primary (citable) accession number: Q9H8V3
Secondary accession number(s): Q0MT80 , Q2M269, Q6U836, Q9NSV8, Q9NVW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 16, 2011
Last modified:	January 25, 2012
This is version 89 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.