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Protein

Protein ECT2

Gene

ECT2

Organism
Homo sapiens (Human)
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.14 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • activation of protein kinase activity Source: UniProtKB
  • apoptotic signaling pathway Source: Reactome
  • bicellular tight junction assembly Source: UniProtKB
  • cell morphogenesis Source: Ensembl
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of neuron differentiation Source: UniProtKB
  • positive regulation of protein import into nucleus Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  • regulation of protein kinase activity Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • small GTPase mediated signal transduction Source: Reactome
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

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
SignaLinkiQ9H8V3.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ECT2
Alternative name(s):
Epithelial cell-transforming sequence 2 oncogene
Gene namesi
Name:ECT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3155. ECT2.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • centralspindlin complex Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular membrane-bounded organelle Source: HPA
  • midbody Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nuclear membrane Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi184 – 1841T → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 1 Publication
Mutagenesisi226 – 2261K → A: Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle. 1 Publication
Mutagenesisi336 – 3361W → R: Inhibits homodimerization. Increases binding with RhoA and GEF activity. 1 Publication
Mutagenesisi359 – 3591T → A: Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity. 1 Publication
Mutagenesisi373 – 3731T → A: Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells. 2 Publications
Mutagenesisi373 – 3731T → D: Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity. 2 Publications
Mutagenesisi379 – 3813KRR → AAA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication
Mutagenesisi402 – 4043RKR → AKA: Shows both nuclear and cytoplasmic localization and activates its transforming activity. 1 Publication
Mutagenesisi444 – 4441T → 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. 1 Publication
Mutagenesisi444 – 4441T → D: Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity. 1 Publication
Mutagenesisi596 – 5994PVQR → AAAA: Inhibits activation of the transforming activity. 1 Publication
Mutagenesisi846 – 8461T → A: Diminishes its phosphorylation status. 1 Publication

Keywords - Diseasei

Oncogene

Organism-specific databases

PharmGKBiPA27600.

Polymorphism and mutation databases

BioMutaiECT2.
DMDMi357529579.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 914913Protein ECT2PRO_0000080938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei359 – 3591Phosphothreonine; by PKC/PRKCI3 Publications
Modified residuei367 – 3671Phosphoserine1 Publication
Modified residuei370 – 3701Phosphoserine1 Publication
Modified residuei373 – 3731Phosphothreonine; by CDK12 Publications
Modified residuei376 – 3761Phosphoserine1 Publication
Modified residuei444 – 4441Phosphothreonine; by CDK11 Publication
Modified residuei842 – 8421Phosphoserine1 Publication
Modified residuei846 – 8461Phosphothreonine; by CDK11 Publication

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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H8V3.
PaxDbiQ9H8V3.
PRIDEiQ9H8V3.

PTM databases

PhosphoSiteiQ9H8V3.

Expressioni

Tissue specificityi

Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma.1 Publication

Inductioni

Up-regulated by calcium in cells forming cell-cell contact sites. Up-regulated by DNA damaging agents like H2O2 or ionizing radiation (IR).2 Publications

Gene expression databases

BgeeiQ9H8V3.
CleanExiHS_ECT2.
ExpressionAtlasiQ9H8V3. baseline and differential.
GenevisibleiQ9H8V3. HS.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-1054039,EBI-389883
RACGAP1Q9H0H58EBI-1054039,EBI-717233

Protein-protein interaction databases

BioGridi108223. 141 interactions.
DIPiDIP-47496N.
IntActiQ9H8V3. 7 interactions.
MINTiMINT-6166617.
STRINGi9606.ENSP00000232458.

Structurei

Secondary structure

1
914
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 566Combined sources
Helixi57 – 593Combined sources
Helixi63 – 708Combined sources
Beta strandi107 – 1126Combined sources
Helixi115 – 1195Combined sources
Beta strandi124 – 1296Combined sources
Helixi136 – 1438Combined sources
Beta strandi147 – 1493Combined sources
Helixi151 – 1599Combined sources
Turni175 – 1784Combined sources
Beta strandi183 – 1853Combined sources
Helixi189 – 20012Combined sources
Turni201 – 2033Combined sources
Beta strandi218 – 2203Combined sources
Helixi225 – 2339Combined sources
Helixi241 – 2477Combined sources
Turni248 – 2514Combined sources
Helixi260 – 2667Combined sources
Turni270 – 2734Combined sources
Beta strandi278 – 2803Combined sources
Helixi283 – 29513Combined sources
Beta strandi309 – 3135Combined sources
Turni315 – 3173Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi330 – 3334Combined sources
Helixi334 – 34310Combined sources
Helixi349 – 3513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L46X-ray1.48A/B268-361[»]
4N40X-ray3.11A45-356[»]
ProteinModelPortaliQ9H8V3.
SMRiQ9H8V3. Positions 45-361, 443-730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H8V3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 26090BRCT 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 signal
Motifi401 – 4055Nuclear localization signal

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.

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

eggNOGiCOG5422.
GeneTreeiENSGT00730000110849.
HOGENOMiHOG000012876.
HOVERGENiHBG005563.
InParanoidiQ9H8V3.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR16777. PTHR16777. 1 hit.
PfamiPF00533. BRCT. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H8V3-1) [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
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE
60 70 80 90 100
TRVILVQEAG KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN
110 120 130 140 150
MDIKVGFVKM ESVEEFEGLD SPEFENVFVV TDFQDSVFND LYKADCRVIG
160 170 180 190 200
PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV LCFTGFRKKE ELVRLVTLVH
210 220 230 240 250
HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP EWIYKAWERR
260 270 280 290 300
NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY
310 320 330 340 350
LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET
360 370 380 390 400
MYLYEKANTP ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP
410 420 430 440 450
PRKRPSAEHS LSIGSLLDIS NTPESSINYG DTPKSCTKSS KSSTPVPSKQ
460 470 480 490 500
SARWQVAKEL YQTESNYVNI LATIIQLFQV PLEEEGQRGG PILAPEEIKT
510 520 530 540 550
IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS KDLVKTYPPF
560 570 580 590 600
VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL
610 620 630 640 650
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ
660 670 680 690 700
IFDVVYEVDG CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC
710 720 730 740 750
LEIARKRHKV IGTFRSPHGQ TRPPASLKHI HLMPLSQIKK VLDIRETEDC
760 770 780 790 800
HNAFALLVRP PTEQANVLLS FQMTSDELPK ENWLKMLCRH VANTICKADA
810 820 830 840 850
ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA FSFSKTPKRA
860 870 880 890 900
LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAGIPSP SLVSLPSFFE
910
RRSHTLSRST THLI
Length:914
Mass (Da):103,505
Last modified:November 16, 2011 - v4
Checksum:iF40FC4F982FB8C78
GO
Isoform 2 (identifier: Q9H8V3-2) [UniParc]FASTAAdd to basket

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

Show »
Length:882
Mass (Da):99,921
Checksum:iAAD4483A503D086C
GO
Isoform 3 (identifier: Q9H8V3-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:958
Mass (Da):108,529
Checksum:iF505EBBF2E1BBE23
GO
Isoform 4 (identifier: Q9H8V3-4) [UniParc]FASTAAdd to basket

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

Show »
Length:883
Mass (Da):100,051
Checksum:iBAEFC693495C50E1
GO

Sequence cautioni

The sequence BAA91624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661I → T in BAB14498 (PubMed:16641997).Curated
Sequence conflicti276 – 2761L → F in BAB14498 (PubMed:16641997).Curated
Sequence conflicti393 – 3931E → D in BAB14498 (PubMed:16641997).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151S → T.
Corresponds to variant rs34703432 [ dbSNP | Ensembl ].
VAR_047064
Natural varianti833 – 8331T → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_035975

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei44 – 441Missing in isoform 2. 4 PublicationsVSP_041976
Alternative sequencei71 – 10131Missing in isoform 2 and isoform 4. 4 PublicationsVSP_041977Add
BLAST
Alternative sequencei886 – 91429GIPSP…TTHLI → ITHSVSTSNVIGFTKHVYVQ RLNSTGGRSQYSWFQSVRHS AFRASFSEILEGNTDFSNFK KVLSKSSLTFVKN in isoform 3. 1 PublicationVSP_041978Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3220.1. [Q9H8V3-4]
CCDS58860.1. [Q9H8V3-1]
RefSeqiNP_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_006713523.2. [Q9H8V3-3]
UniGeneiHs.518299.

Genome annotation databases

EnsembliENST00000232458; ENSP00000232458; ENSG00000114346. [Q9H8V3-4]
ENST00000392692; ENSP00000376457; ENSG00000114346. [Q9H8V3-1]
ENST00000417960; ENSP00000415876; ENSG00000114346. [Q9H8V3-2]
ENST00000441497; ENSP00000412259; ENSG00000114346. [Q9H8V3-4]
ENST00000540509; ENSP00000443160; ENSG00000114346. [Q9H8V3-4]
GeneIDi1894.
KEGGihsa:1894.
UCSCiuc003fih.3. human. [Q9H8V3-2]
uc003fil.2. human. [Q9H8V3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3220.1. [Q9H8V3-4]
CCDS58860.1. [Q9H8V3-1]
RefSeqiNP_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_006713523.2. [Q9H8V3-3]
UniGeneiHs.518299.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L46X-ray1.48A/B268-361[»]
4N40X-ray3.11A45-356[»]
ProteinModelPortaliQ9H8V3.
SMRiQ9H8V3. Positions 45-361, 443-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108223. 141 interactions.
DIPiDIP-47496N.
IntActiQ9H8V3. 7 interactions.
MINTiMINT-6166617.
STRINGi9606.ENSP00000232458.

PTM databases

PhosphoSiteiQ9H8V3.

Polymorphism and mutation databases

BioMutaiECT2.
DMDMi357529579.

Proteomic databases

MaxQBiQ9H8V3.
PaxDbiQ9H8V3.
PRIDEiQ9H8V3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232458; ENSP00000232458; ENSG00000114346. [Q9H8V3-4]
ENST00000392692; ENSP00000376457; ENSG00000114346. [Q9H8V3-1]
ENST00000417960; ENSP00000415876; ENSG00000114346. [Q9H8V3-2]
ENST00000441497; ENSP00000412259; ENSG00000114346. [Q9H8V3-4]
ENST00000540509; ENSP00000443160; ENSG00000114346. [Q9H8V3-4]
GeneIDi1894.
KEGGihsa:1894.
UCSCiuc003fih.3. human. [Q9H8V3-2]
uc003fil.2. human. [Q9H8V3-1]

Organism-specific databases

CTDi1894.
GeneCardsiGC03P172468.
HGNCiHGNC:3155. ECT2.
MIMi600586. gene.
neXtProtiNX_Q9H8V3.
PharmGKBiPA27600.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00730000110849.
HOGENOMiHOG000012876.
HOVERGENiHBG005563.
InParanoidiQ9H8V3.
TreeFamiTF101161.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_13638. NRAGE signals death through JNK.
REACT_18407. G alpha (12/13) signalling events.
SignaLinkiQ9H8V3.

Miscellaneous databases

ChiTaRSiECT2. human.
EvolutionaryTraceiQ9H8V3.
GeneWikiiECT2.
GenomeRNAii1894.
NextBioi7725.
PROiQ9H8V3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H8V3.
CleanExiHS_ECT2.
ExpressionAtlasiQ9H8V3. baseline and differential.
GenevisibleiQ9H8V3. HS.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PANTHERiPTHR16777. PTHR16777. 1 hit.
PfamiPF00533. BRCT. 1 hit.
PF12738. PTCB-BRCT. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 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. "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.
    , 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.
    , 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-833.

Entry informationi

Entry nameiECT2_HUMAN
AccessioniPrimary (citable) accession number: Q9H8V3
Secondary accession number(s): Q0MT80
, Q2M269, Q6U836, Q9NSV8, Q9NVW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 16, 2011
Last modified: June 24, 2015
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.