Ect2
entrez
13605
canonical
uniprot
Q07139
canonical
ensembl
ENSMUSG00000027699
resolver
ensp
ENSMUSP00000103933
resolver
ensp
ENSMUSP00000103935
resolver
ensp
ENSMUSP00000135740
resolver
ensp
ENSMUSP00000241788
resolver
ensp
ENSMUSP00000241789
resolver
ensp
ENSMUSP00000241790
resolver
ensp
ENSMUSP00000241791
resolver
ensp
ENSMUSP00000241792
resolver
ensp
ENSMUSP00000241793
resolver
ensp
ENSMUSP00000241794
resolver
ensp
ENSMUSP00000345612
resolver
ensp
ENSMUSP00000345615
resolver
ensp
ENSMUSP00000345617
resolver
ensp
ENSMUSP00000345619
resolver
genesymbol
Ect2
resolver
genesymbol_syn
mKIAA4037
resolver
uniprot
Q3TZP2
resolver
uniprot
Q5DTR8
resolver
uniprot
Q80VE4
resolver
uniprot
Q8CIH2
resolver
uniprot
Q8K2A0
resolver
uniprot
Q8R3E2
resolver
uniprot_entry
ECT2_MOUSE
resolver
uniprot_sec
Q3TZP2
resolver
uniprot_sec
Q5DTR8
resolver
uniprot_sec
Q80VE4
resolver
uniprot_sec
Q8CIH2
resolver
uniprot_sec
Q8K2A0
resolver
uniprot_sec
Q8R3E2
resolver
activity_regulation
ACTIVITY REGULATION: Autoinhibited by the C-terminal PH domain which folds back and binds to the surface of the DH domain, blocking binding of RHOA to the catalytic center of the DH domain. The 2nd BRCT domain is also involved in inhibition, probably by helping to impede RHOA binding. Allosterically activated by binding of activated GTP-bound RHOA to the PH domain which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the catalytic center. Binding of phosphorylated RACGAP1 to the N-terminal BRCT domain-containing region also releases autoinhibition. {ECO:0000250|UniProtKB:Q9H8V3}.
uniprot
proteins
amino_acid_sequence
MADDSVLPSPSEITSLADSSVFDSKVAEMSKENLCLASTSNVDEEMPQVEARVIMVQDAGKQEELLKALKTIKIMEVPVIKIKESCPGKSEEKLIKSIINMEMKVPCVKMDSMEEFESLDSPEFENIFVVTDFQNSVFNDLYKADCRIVGPPVILNCAQRGEPLPFSCRPLYCTSMLNLVLCFTGFRKKEELVKLVTLVHHMGGVIRKECNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQCFCAAVDDFRNEFKVPPFQDCILSFLGFSDEEKHSMEEMTEMQGGSYLPVGDERCTHLIVEENTVKDLPFEPSKKLFVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSLLSLSTPNSNRKRRRLKETLAQLSRETDLSPFPPRKRPSAEHSLSIGSLLDISNTPESSIHYGETPKSCAKSSRSSTPVPPKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHMKIKDDLEDLIANWDESRSIGDIFLKYAKDLVKTYPPFVNFFEMSKEMIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETVSLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHDRTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSEELPKESWLKMLCRHVANTICKADAENLMYVADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRMALSSSHSSEGRSPPSSGKLAVSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI
uniprot
proteins
function
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. {ECO:0000269|PubMed:17904126, ECO:0000269|PubMed:21350944}.
uniprot
proteins
mass_dalton
103131
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17904126
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21350944
uniprot
proteins
pubmed
8464478
uniprot
proteins
sequence_length
913
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17904126}. Cytoplasm {ECO:0000269|PubMed:17904126}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9H8V3}. Cleavage furrow {ECO:0000250|UniProtKB:Q9H8V3}. Midbody {ECO:0000250|UniProtKB:Q9H8V3}. Cell junction {ECO:0000250|UniProtKB:Q9H8V3}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9H8V3}. Note=Sequestered within the nucleus during interphase (By similarity). Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis (By similarity). 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 (By similarity). Colocalized with RhoA at the midbody (By similarity). Its subcellular localization to tight junction is increased by calcium (By similarity). {ECO:0000250|UniProtKB:Q9H8V3}.
uniprot
proteins