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Protein

Protein ECT2

Gene

Ect2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Neurogenesis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ECT2
Alternative name(s):
Epithelial cell-transforming sequence 2 oncogene
Gene namesi
Name:Ect2
Synonyms:mKIAA4037
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95281. Ect2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeletonspindle By similarity
  • Cleavage furrow By similarity
  • Midbody By similarity
  • Cell junction By similarity
  • Cell junctiontight junction By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • centralspindlin complex Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • midbody Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 913912Protein ECT2PRO_0000080939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei359 – 3591Phosphothreonine; by PKC/PRKCIBy similarity
Modified residuei367 – 3671PhosphoserineBy similarity
Modified residuei370 – 3701PhosphoserineBy similarity
Modified residuei373 – 3731PhosphothreonineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei444 – 4441Phosphothreonine; by CDK1By similarity
Modified residuei842 – 8421PhosphoserineBy similarity
Modified residuei846 – 8461Phosphothreonine; by CDK1By similarity

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ07139.
MaxQBiQ07139.
PaxDbiQ07139.
PRIDEiQ07139.

PTM databases

PhosphoSiteiQ07139.

Expressioni

Tissue specificityi

Highest expression in testis. Also detectable in brain, kidney, liver and spleen.1 Publication

Developmental stagei

Expressed in the embryo at 16 dpc.1 Publication

Inductioni

Up-regulated by phenobarbital in the nucleus and cytoplasm of the liver.1 Publication

Gene expression databases

BgeeiQ07139.
CleanExiMM_ECT2.
ExpressionAtlasiQ07139. baseline and differential.
GenevisibleiQ07139. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with NR1I3.By similarity1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • Rho GTPase binding Source: MGI

Protein-protein interaction databases

BioGridi199370. 14 interactions.
IntActiQ07139. 14 interactions.
STRINGi10090.ENSMUSP00000103935.

Structurei

Secondary structure

1
913
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni270 – 2734Combined sources
Beta strandi275 – 2817Combined sources
Helixi283 – 29614Combined sources
Beta strandi309 – 3135Combined sources
Turni315 – 3173Combined sources
Beta strandi329 – 3324Combined sources
Helixi334 – 3429Combined sources
Helixi349 – 3513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COUNMR-A266-361[»]
ProteinModelPortaliQ07139.
SMRiQ07139. Positions 45-361, 443-706.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07139.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 26085BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini266 – 35489BRCT 2PROSITE-ProRule annotationAdd
BLAST
Domaini452 – 641190DHPROSITE-ProRule annotationAdd
BLAST
Domaini675 – 794120PHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi378 – 3825Nuclear localization signalBy similarity
Motifi401 – 4055Nuclear localization signalBy similarity

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3524. Eukaryota.
ENOG410XRV9. LUCA.
GeneTreeiENSGT00840000129846.
HOGENOMiHOG000012876.
HOVERGENiHBG005563.
InParanoidiQ07139.
OMAiFERRSHT.
OrthoDBiEOG7QK0BW.
TreeFamiTF101161.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR001357. BRCT_dom.
IPR000219. DH-domain.
IPR026817. Ect2.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16777. PTHR16777. 2 hits.
PfamiPF00533. BRCT. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q07139-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADDSVLPSP SEITSLADSS VFDSKVAEMS KENLCLASTS NVDEEMPQVE
60 70 80 90 100
ARVIMVQDAG KQEELLKALK TIKIMEVPVI KIKESCPGKS EEKLIKSIIN
110 120 130 140 150
MEMKVPCVKM DSMEEFESLD SPEFENIFVV TDFQNSVFND LYKADCRIVG
160 170 180 190 200
PPVILNCAQR GEPLPFSCRP LYCTSMLNLV LCFTGFRKKE ELVKLVTLVH
210 220 230 240 250
HMGGVIRKEC NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR
260 270 280 290 300
NEQCFCAAVD DFRNEFKVPP FQDCILSFLG FSDEEKHSME EMTEMQGGSY
310 320 330 340 350
LPVGDERCTH LIVEENTVKD LPFEPSKKLF VVKQEWFWGS IQMDARAGET
360 370 380 390 400
MYLYEKANTP ELKKSVSLLS LSTPNSNRKR RRLKETLAQL SRETDLSPFP
410 420 430 440 450
PRKRPSAEHS LSIGSLLDIS NTPESSIHYG ETPKSCAKSS RSSTPVPPKQ
460 470 480 490 500
SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT
510 520 530 540 550
IFGSIPDIFD VHMKIKDDLE DLIANWDESR SIGDIFLKYA KDLVKTYPPF
560 570 580 590 600
VNFFEMSKEM IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL
610 620 630 640 650
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ
660 670 680 690 700
IFDVVYEVDG CPANLLSSHR SLVQRVETVS LGEHPCDRGE QVTLFLFNDC
710 720 730 740 750
LEIARKRHKV IGTFRSPHDR TRPPASLKHI HLMPLSQIKK VLDIRETEDC
760 770 780 790 800
HNAFALLVRP PTEQANVLLS FQMTSEELPK ESWLKMLCRH VANTICKADA
810 820 830 840 850
ENLMYVADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA
860 870 880 890 900
LRMALSSSHS SEGRSPPSSG KLAVSRLSST SSLAGIPSPS LVSLPSFFER
910
RSHTLSRSTT HLI
Length:913
Mass (Da):103,131
Last modified:November 16, 2011 - v2
Checksum:i2F0CC71DBF9D8280
GO
Isoform 2 (identifier: Q07139-2) [UniParc]FASTAAdd to basket

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

Show »
Length:882
Mass (Da):99,648
Checksum:iB4D4033B955AE6BC
GO
Isoform 3 (identifier: Q07139-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-52: VEAR → LKQE
     53-913: Missing.

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.
Show »
Length:52
Mass (Da):5,605
Checksum:i46E34DBE58839C23
GO

Sequence cautioni

The sequence AAA37536.1 differs from that shown.Erroneous CDS prediction.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → T in AAH32155 (PubMed:15489334).Curated
Sequence conflicti28 – 281E → G in AAH32155 (PubMed:15489334).Curated
Sequence conflicti147 – 1471R → S in AAH23881 (PubMed:15489334).Curated
Sequence conflicti555 – 5551E → K in AAH45614 (PubMed:15489334).Curated
Sequence conflicti872 – 8721L → V in AAH32155 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei49 – 524VEAR → LKQE in isoform 3. 1 PublicationVSP_041979
Alternative sequencei53 – 913861Missing in isoform 3. 1 PublicationVSP_041980Add
BLAST
Alternative sequencei71 – 10131Missing in isoform 2. 3 PublicationsVSP_041981Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11316 mRNA. Translation: AAA37536.1. Sequence problems.
AK157718 mRNA. Translation: BAE34166.1.
AK220452 mRNA. Translation: BAD90277.1.
AC121099 Genomic DNA. No translation available.
AC165280 Genomic DNA. No translation available.
CH466530 Genomic DNA. Translation: EDL34919.1.
CH466530 Genomic DNA. Translation: EDL34920.1.
BC023881 mRNA. Translation: AAH23881.1.
BC025565 mRNA. Translation: AAH25565.1.
BC032155 mRNA. Translation: AAH32155.1.
BC045614 mRNA. Translation: AAH45614.1.
CCDSiCCDS17270.2. [Q07139-1]
CCDS50875.1. [Q07139-2]
PIRiS32372.
RefSeqiNP_001171096.1. NM_001177625.1. [Q07139-2]
NP_001171097.1. NM_001177626.1. [Q07139-2]
NP_031926.2. NM_007900.3. [Q07139-1]
XP_006535448.1. XM_006535385.2. [Q07139-1]
XP_006535449.1. XM_006535386.2. [Q07139-1]
UniGeneiMm.261453.

Genome annotation databases

EnsembliENSMUST00000108298; ENSMUSP00000103933; ENSMUSG00000027699. [Q07139-2]
ENSMUST00000108300; ENSMUSP00000103935; ENSMUSG00000027699. [Q07139-1]
ENSMUST00000176242; ENSMUSP00000135740; ENSMUSG00000027699. [Q07139-2]
GeneIDi13605.
KEGGimmu:13605.
UCSCiuc008oth.2. mouse. [Q07139-1]
uc008oti.2. mouse. [Q07139-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11316 mRNA. Translation: AAA37536.1. Sequence problems.
AK157718 mRNA. Translation: BAE34166.1.
AK220452 mRNA. Translation: BAD90277.1.
AC121099 Genomic DNA. No translation available.
AC165280 Genomic DNA. No translation available.
CH466530 Genomic DNA. Translation: EDL34919.1.
CH466530 Genomic DNA. Translation: EDL34920.1.
BC023881 mRNA. Translation: AAH23881.1.
BC025565 mRNA. Translation: AAH25565.1.
BC032155 mRNA. Translation: AAH32155.1.
BC045614 mRNA. Translation: AAH45614.1.
CCDSiCCDS17270.2. [Q07139-1]
CCDS50875.1. [Q07139-2]
PIRiS32372.
RefSeqiNP_001171096.1. NM_001177625.1. [Q07139-2]
NP_001171097.1. NM_001177626.1. [Q07139-2]
NP_031926.2. NM_007900.3. [Q07139-1]
XP_006535448.1. XM_006535385.2. [Q07139-1]
XP_006535449.1. XM_006535386.2. [Q07139-1]
UniGeneiMm.261453.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COUNMR-A266-361[»]
ProteinModelPortaliQ07139.
SMRiQ07139. Positions 45-361, 443-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199370. 14 interactions.
IntActiQ07139. 14 interactions.
STRINGi10090.ENSMUSP00000103935.

PTM databases

PhosphoSiteiQ07139.

Proteomic databases

EPDiQ07139.
MaxQBiQ07139.
PaxDbiQ07139.
PRIDEiQ07139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108298; ENSMUSP00000103933; ENSMUSG00000027699. [Q07139-2]
ENSMUST00000108300; ENSMUSP00000103935; ENSMUSG00000027699. [Q07139-1]
ENSMUST00000176242; ENSMUSP00000135740; ENSMUSG00000027699. [Q07139-2]
GeneIDi13605.
KEGGimmu:13605.
UCSCiuc008oth.2. mouse. [Q07139-1]
uc008oti.2. mouse. [Q07139-2]

Organism-specific databases

CTDi1894.
MGIiMGI:95281. Ect2.

Phylogenomic databases

eggNOGiKOG3524. Eukaryota.
ENOG410XRV9. LUCA.
GeneTreeiENSGT00840000129846.
HOGENOMiHOG000012876.
HOVERGENiHBG005563.
InParanoidiQ07139.
OMAiFERRSHT.
OrthoDBiEOG7QK0BW.
TreeFamiTF101161.

Enzyme and pathway databases

ReactomeiR-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-416482. G alpha (12/13) signalling events.

Miscellaneous databases

ChiTaRSiEct2. mouse.
EvolutionaryTraceiQ07139.
NextBioi284242.
PROiQ07139.
SOURCEiSearch...

Gene expression databases

BgeeiQ07139.
CleanExiMM_ECT2.
ExpressionAtlasiQ07139. baseline and differential.
GenevisibleiQ07139. MM.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR001357. BRCT_dom.
IPR000219. DH-domain.
IPR026817. Ect2.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
[Graphical view]
PANTHERiPTHR16777. PTHR16777. 2 hits.
PfamiPF00533. BRCT. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Oncogene ect2 is related to regulators of small GTP-binding proteins."
    Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.
    Nature 362:462-465(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  2. Erratum
    Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.
    Nature 364:737-737(1993)
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2).
    Strain: Czech II, FVB/N and FVB/N-3.
    Tissue: Mammary tumor.
  8. "Overexpression of the Rho-guanine nucleotide exchange factor ECT2 inhibits nuclear translocation of nuclear receptor CAR in the mouse liver."
    Hosseinpour F., Timsit Y., Koike C., Matsui K., Yamamoto Y., Moore R., Negishi M.
    FEBS Lett. 581:4937-4942(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NR1I3, INDUCTION, SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-373 AND SER-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  10. "Ect2, an ortholog of Drosophila's pebble, negatively regulates neurite outgrowth in neuroblastoma x glioma hybrid NG108-15 cells."
    Tsuji T., Higashida C., Yoshida Y., Islam M.S., Dohmoto M., Koizumi K., Higashida H.
    Cell. Mol. Neurobiol. 31:663-668(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  11. "Solution structure of the second BRCT domain of epithelial cell transforming 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 266-361.

Entry informationi

Entry nameiECT2_MOUSE
AccessioniPrimary (citable) accession number: Q07139
Secondary accession number(s): Q3TZP2
, Q5DTR8, Q80VE4, Q8CIH2, Q8K2A0, Q8R3E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 16, 2011
Last modified: May 11, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.