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Protein

Protein ECT2

Gene

Ect2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
Biological processCell 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:95281 Ect2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000809392 – 913Protein ECT2Add BLAST912

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei359Phosphothreonine; by PKC/PRKCIBy similarity1
Modified residuei367PhosphoserineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei373PhosphothreonineCombined sources1
Modified residuei376PhosphoserineCombined sources1
Modified residuei444Phosphothreonine; by CDK1By similarity1
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei716PhosphoserineBy similarity1
Modified residuei842PhosphoserineBy similarity1
Modified residuei846Phosphothreonine; by CDK1By similarity1
Modified residuei861PhosphoserineBy similarity1
Modified residuei865PhosphoserineBy similarity1

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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ07139
PaxDbiQ07139
PeptideAtlasiQ07139
PRIDEiQ07139

PTM databases

iPTMnetiQ07139
PhosphoSitePlusiQ07139

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

BgeeiENSMUSG00000027699
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-protein interaction databases

BioGridi199370, 14 interactors
IntActiQ07139, 14 interactors
STRINGi10090.ENSMUSP00000103935

Structurei

Secondary structure

1913
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni270 – 273Combined sources4
Beta strandi275 – 281Combined sources7
Helixi283 – 296Combined sources14
Beta strandi309 – 313Combined sources5
Turni315 – 317Combined sources3
Beta strandi329 – 332Combined sources4
Helixi334 – 342Combined sources9
Helixi349 – 351Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2COUNMR-A266-361[»]
ProteinModelPortaliQ07139
SMRiQ07139
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07139

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini176 – 260BRCT 1PROSITE-ProRule annotationAdd BLAST85
Domaini266 – 354BRCT 2PROSITE-ProRule annotationAdd BLAST89
Domaini452 – 641DHPROSITE-ProRule annotationAdd BLAST190
Domaini675 – 794PHAdd BLAST120

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi378 – 382Nuclear localization signalBy similarity5
Motifi401 – 405Nuclear localization signalBy similarity5

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3524 Eukaryota
ENOG410XRV9 LUCA
GeneTreeiENSGT00840000129846
HOGENOMiHOG000012876
HOVERGENiHBG005563
InParanoidiQ07139
KOiK20704
OMAiFKSPHGH
OrthoDBiEOG091G02MY
TreeFamiTF101161

Family and domain databases

CDDicd00027 BRCT, 2 hits
cd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 1 hit
3.40.50.10190, 3 hits
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR026817 Ect2
IPR001331 GDS_CDC24_CS
IPR011993 PH-like_dom_sf
PANTHERiPTHR16777 PTHR16777, 1 hit
PfamiView protein in Pfam
PF00533 BRCT, 1 hit
PF12738 PTCB-BRCT, 1 hit
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
SSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits
PS00741 DH_1, 1 hit
PS50010 DH_2, 1 hit

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 differs from that shown. Erroneous CDS prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11S → T in AAH32155 (PubMed:15489334).Curated1
Sequence conflicti28E → G in AAH32155 (PubMed:15489334).Curated1
Sequence conflicti147R → S in AAH23881 (PubMed:15489334).Curated1
Sequence conflicti555E → K in AAH45614 (PubMed:15489334).Curated1
Sequence conflicti872L → V in AAH32155 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04197949 – 52VEAR → LKQE in isoform 3. 1 Publication4
Alternative sequenceiVSP_04198053 – 913Missing in isoform 3. 1 PublicationAdd BLAST861
Alternative sequenceiVSP_04198171 – 101Missing in isoform 2. 3 PublicationsAdd BLAST31

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_006535385.3 [Q07139-1]
XP_006535449.1, XM_006535386.3 [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

Similar proteinsi

Entry informationi

Entry nameiECT2_MOUSE
AccessioniPrimary (citable) accession number: Q07139
Secondary accession number(s): Q3TZP2
, Q5DTR8, Q80VE4, Q8CIH2, Q8K2A0, Q8R3E2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 16, 2011
Last modified: March 28, 2018
This is version 146 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health