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Q9H8V3 (ECT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ECT2
Alternative name(s):
Epithelial cell-transforming sequence 2 oncogene
Gene names
Name:ECT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.16 Ref.21 Ref.22 Ref.23 Ref.27 Ref.28

Subunit structure

Interacts with NR1I3 By similarity. Homodimer. 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.16 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle. Cleavage furrow. Midbody. Cell junction. Cell junctiontight 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.22 Ref.23

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.22

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.28

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.27

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 processCell cycle
Cell division
Differentiation
Neurogenesis
Protein transport
Transport
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
Tight junction
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseOncogene
   DomainRepeat
   Molecular functionGuanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rac GTPase activity

Inferred from mutant phenotype Ref.22. Source: UniProtKB

activation of Rho GTPase activity

Inferred from direct assay Ref.22. Source: UniProtKB

activation of protein kinase activity

Inferred from direct assay Ref.9. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from direct assay Ref.9. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from direct assay Ref.28. Source: UniProtKB

cellular response to ionizing radiation

Inferred from direct assay Ref.28. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of Cdc42 GTPase activity

Inferred from direct assay Ref.22. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of Rho GTPase activity

Inferred from direct assay Ref.3PubMed 20047078. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of 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

regulation of protein kinase activity

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

tight junction assembly

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.9. Source: UniProtKB

centralspindlin complex

Inferred from direct assay Ref.15. Source: UniProtKB

cleavage furrow

Inferred from direct assay Ref.12PubMed 20047078. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.22PubMed 20047078. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

midbody

Inferred from direct assay Ref.10Ref.12Ref.23PubMed 20047078. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.9Ref.12Ref.15PubMed 20047078. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9Ref.12Ref.22PubMed 20047078. Source: UniProtKB

tight junction

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionGTPase activator activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

Rho guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 12761501Ref.9Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.12Ref.13Ref.15Ref.3Ref.18Ref.21Ref.23Ref.24Ref.22. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.10. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163333EBI-1054039,EBI-389883

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: Q9H8V3-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.30
Chain2 – 914913Protein ECT2
PRO_0000080938

Regions

Domain171 – 26090BRCT 1
Domain266 – 35489BRCT 2
Domain452 – 641190DH
Domain675 – 794120PH
Motif378 – 3825Nuclear localization signal
Motif401 – 4055Nuclear localization signal

Amino acid modifications

Modified residue21N-acetylalanine Ref.30
Modified residue3591Phosphothreonine; by PKC/PRKCI Ref.26 Ref.27 Ref.29
Modified residue3671Phosphoserine Ref.20
Modified residue3701Phosphoserine Ref.20
Modified residue3731Phosphothreonine; by CDK1 Ref.16 Ref.20
Modified residue3761Phosphoserine Ref.20
Modified residue4441Phosphothreonine; by CDK1 Ref.17
Modified residue8421Phosphoserine Ref.20
Modified residue8461Phosphothreonine; by CDK1 Ref.20

Natural variations

Alternative sequence441Missing in isoform 2.
VSP_041976
Alternative sequence71 – 10131Missing in isoform 2 and isoform 4.
VSP_041977
Alternative sequence886 – 91429GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3.
VSP_041978
Natural variant151S → T.
Corresponds to variant rs34703432 [ dbSNP | Ensembl ].
VAR_047064
Natural variant8331T → P in a breast cancer sample; somatic mutation. Ref.32
VAR_035975

Experimental info

Mutagenesis1841T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. Ref.23
Mutagenesis2261K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. Ref.23
Mutagenesis3361W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. Ref.10
Mutagenesis3591T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. Ref.27
Mutagenesis3731T → 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.16
Mutagenesis3731T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. Ref.12 Ref.16
Mutagenesis379 – 3813KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity.
Mutagenesis402 – 4043RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. Ref.8
Mutagenesis4441T → 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.17
Mutagenesis4441T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. Ref.17
Mutagenesis596 – 5994PVQR → AAAA: Inhibits activation of the transforming activity. Ref.8
Mutagenesis8461T → A: Diminishes its phosphorylation status. Ref.17
Sequence conflict661I → T in BAB14498. Ref.5
Sequence conflict2761L → F in BAB14498. Ref.5
Sequence conflict3931E → D in BAB14498. Ref.5

Secondary structure

................. 914
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 16, 2011. Version 4.
Checksum: F40FC4F982FB8C78

FASTA914103,505
        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 

« Hide

Isoform 2 [UniParc].

Checksum: AAD4483A503D086C
Show »

FASTA88299,921
Isoform 3 [UniParc].

Checksum: F505EBBF2E1BBE23
Show »

FASTA958108,529
Isoform 4 [UniParc].

Checksum: BAEFC693495C50E1
Show »

FASTA883100,051

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION.
[16]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-373, MUTAGENESIS OF THR-373.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-444, INTERACTION WITH PLK1, MUTAGENESIS OF THR-444 AND THR-846.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP3.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-370; THR-373; SER-376; SER-842 AND THR-846, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular transformation."
Justilien V., Fields A.P.
Oncogene 28:3597-3607(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARD6A AND PRKCI, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[23]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KIF23 AND RACGAP1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-184 AND LYS-226.
[24]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RACGAP1.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-359, MUTAGENESIS OF THR-359, IDENTIFICATION BY MASS SPECTROMETRY.
[28]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[31]"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.
[32]"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. expand/collapse author list , 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] [Europe PMC] [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.
CCDSCCDS3220.1. [Q9H8V3-4]
CCDS58860.1. [Q9H8V3-1]
RefSeqNP_001245244.1. NM_001258315.1. [Q9H8V3-1]
NP_001245245.1. NM_001258316.1. [Q9H8V3-4]
NP_060568.3. NM_018098.5. [Q9H8V3-4]
XP_006713586.1. XM_006713523.1. [Q9H8V3-3]
UniGeneHs.518299.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L46X-ray1.48A/B268-361[»]
ProteinModelPortalQ9H8V3.
SMRQ9H8V3. Positions 176-361, 443-730.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108223. 139 interactions.
DIPDIP-47496N.
IntActQ9H8V3. 7 interactions.
MINTMINT-6166617.
STRING9606.ENSP00000232458.

PTM databases

PhosphoSiteQ9H8V3.

Polymorphism databases

DMDM357529579.

Proteomic databases

MaxQBQ9H8V3.
PaxDbQ9H8V3.
PRIDEQ9H8V3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000232458; ENSP00000232458; ENSG00000114346. [Q9H8V3-4]
ENST00000392692; ENSP00000376457; ENSG00000114346. [Q9H8V3-1]
ENST00000417960; ENSP00000415876; ENSG00000114346. [Q9H8V3-2]
ENST00000441497; ENSP00000412259; ENSG00000114346. [Q9H8V3-4]
ENST00000540509; ENSP00000443160; ENSG00000114346. [Q9H8V3-1]
GeneID1894.
KEGGhsa:1894.
UCSCuc003fih.3. human. [Q9H8V3-2]
uc003fil.2. human. [Q9H8V3-1]

Organism-specific databases

CTD1894.
GeneCardsGC03P172468.
HGNCHGNC:3155. ECT2.
HPAHPA053261.
MIM600586. gene.
neXtProtNX_Q9H8V3.
PharmGKBPA27600.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOGENOMHOG000012876.
HOVERGENHBG005563.
TreeFamTF101161.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9H8V3.

Gene expression databases

ArrayExpressQ9H8V3.
BgeeQ9H8V3.
CleanExHS_ECT2.
GenevestigatorQ9H8V3.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR001357. BRCT_dom.
IPR000219. DH-domain.
IPR026817. Ect2.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR16777. PTHR16777. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 2 hits.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSECT2. human.
EvolutionaryTraceQ9H8V3.
GeneWikiECT2.
GenomeRNAi1894.
NextBio7725.
PROQ9H8V3.
SOURCESearch...

Entry information

Entry nameECT2_HUMAN
AccessionPrimary (citable) accession number: Q9H8V3
Secondary accession number(s): Q0MT80 expand/collapse secondary AC list , Q2M269, Q6U836, Q9NSV8, Q9NVW9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 16, 2011
Last modified: July 9, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM