ECT2_MOUSE
ID ECT2_MOUSE Reviewed; 913 AA.
AC Q07139; Q3TZP2; Q5DTR8; Q80VE4; Q8CIH2; Q8K2A0; Q8R3E2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein ECT2;
DE AltName: Full=Epithelial cell-transforming sequence 2 oncogene;
GN Name=Ect2; Synonyms=mKIAA4037;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=8464478; DOI=10.1038/362462a0;
RA Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RT "Oncogene ect2 is related to regulators of small GTP-binding proteins.";
RL Nature 362:462-465(1993).
RN [2]
RP ERRATUM OF PUBMED:8464478.
RA Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RL Nature 364:737-737(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, INTERACTION WITH NR1I3, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17904126; DOI=10.1016/j.febslet.2007.09.024;
RA Hosseinpour F., Timsit Y., Koike C., Matsui K., Yamamoto Y., Moore R.,
RA Negishi M.;
RT "Overexpression of the Rho-guanine nucleotide exchange factor ECT2 inhibits
RT nuclear translocation of nuclear receptor CAR in the mouse liver.";
RL FEBS Lett. 581:4937-4942(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-373 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=21350944; DOI=10.1007/s10571-011-9668-3;
RA Tsuji T., Higashida C., Yoshida Y., Islam M.S., Dohmoto M., Koizumi K.,
RA Higashida H.;
RT "Ect2, an ortholog of Drosophila's pebble, negatively regulates neurite
RT outgrowth in neuroblastoma x glioma hybrid NG108-15 cells.";
RL Cell. Mol. Neurobiol. 31:663-668(2011).
RN [11]
RP STRUCTURE BY NMR OF 266-361.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second BRCT domain of epithelial cell
RT transforming 2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) that catalyzes the
CC exchange of GDP for GTP. Promotes guanine nucleotide exchange on the
CC Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42.
CC Required for signal transduction pathways involved in the regulation of
CC cytokinesis. Component of the centralspindlin complex that serves as a
CC microtubule-dependent and Rho-mediated signaling required for the
CC myosin contractile ring formation during the cell cycle cytokinesis.
CC Regulates the translocation of RHOA from the central spindle to the
CC equatorial region. Plays a role in the control of mitotic spindle
CC assembly; regulates the activation of CDC42 in metaphase for the
CC process of spindle fibers attachment to kinetochores before chromosome
CC congression. Involved in the regulation of epithelial cell polarity;
CC participates in the formation of epithelial tight junctions in a
CC polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner.
CC Plays a role in the regulation of neurite outgrowth. Inhibits
CC phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the
CC activity of RAC1 through its association with the oncogenic PARD6A-
CC PRKCI complex in cancer cells, thereby acting to coordinately drive
CC tumor cell proliferation and invasion. Also stimulates genotoxic
CC stress-induced RHOB activity in breast cancer cells leading to their
CC cell death. {ECO:0000269|PubMed:17904126, ECO:0000269|PubMed:21350944}.
CC -!- ACTIVITY REGULATION: Autoinhibited by the C-terminal PH domain which
CC folds back and binds to the surface of the DH domain, blocking binding
CC of RHOA to the catalytic center of the DH domain. The 2nd BRCT domain
CC is also involved in inhibition, probably by helping to impede RHOA
CC binding. Allosterically activated by binding of activated GTP-bound
CC RHOA to the PH domain which stimulates the release of PH inhibition and
CC promotes the binding of substrate RHOA to the catalytic center. Binding
CC of phosphorylated RACGAP1 to the N-terminal BRCT domain-containing
CC region also releases autoinhibition. {ECO:0000250|UniProtKB:Q9H8V3}.
CC -!- SUBUNIT: Homodimer (By similarity). Homooligomer (By similarity). Found
CC in the centralspindlin complex (By similarity). Interacts with NR1I3
CC (PubMed:17904126). Interacts (Thr-359 phosphorylated form) with PARD6A;
CC the interaction is observed in cancer cells (By similarity). Interacts
CC (Thr-359 phosphorylated form) with PRKCI; the interaction is observed
CC in cancer cells (By similarity). Interacts with PKP4; the interaction
CC is observed at the midbody (By similarity). Interacts with RACGAP1; the
CC interaction is direct, occurs in a microtubule-dependent manner, occurs
CC at anaphase and during cytokinesis, is inhibited in metaphase by
CC phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase
CC by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity
CC (By similarity). Interacts with PLK1; the interaction is stimulated
CC upon its phosphorylation on Thr-444 (By similarity). Interacts with
CC RHOA; the interaction results in allosteric activation of ECT2 (By
CC similarity). Interacts with KIF23, PARD3, PARD6B and PRKCQ (By
CC similarity). {ECO:0000250|UniProtKB:Q9H8V3,
CC ECO:0000269|PubMed:17904126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17904126}. Cytoplasm
CC {ECO:0000269|PubMed:17904126}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}.
CC Cell junction {ECO:0000250}. Cell junction, tight junction
CC {ECO:0000250}. Note=Sequestered within the nucleus during interphase.
CC Dispersed throughout the cytoplasm upon breakdown of the nuclear
CC envelope during mitosis. Colocalizes with the centralspindlin complex
CC to the mitotic spindles during anaphase/metaphase, the cleavage furrow
CC during telophase and at the midbody at the end of cytokinesis.
CC Colocalized with RhoA at the midbody. Its subcellular localization to
CC tight junction is increased by calcium. Localized predominantly in the
CC cytoplasm of numerous carcinoma cells (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q07139-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07139-2; Sequence=VSP_041981;
CC Name=3;
CC IsoId=Q07139-3; Sequence=VSP_041979, VSP_041980;
CC -!- TISSUE SPECIFICITY: Highest expression in testis. Also detectable in
CC brain, kidney, liver and spleen. {ECO:0000269|PubMed:21350944}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo at 16 dpc.
CC {ECO:0000269|PubMed:21350944}.
CC -!- INDUCTION: Up-regulated by phenobarbital in the nucleus and cytoplasm
CC of the liver. {ECO:0000269|PubMed:17904126}.
CC -!- DOMAIN: The BRCT domain 1 and 2 are required for the intramolecular
CC interaction, but not for the intermolecular oligomerization. The BRCT
CC domains negatively inhibit its GEF activity in interphase cells. The
CC same BRCT domains may act as a positive regulatory motif for the
CC completion of cytokinesis after the breakdown of nuclear membrane
CC during mitosis (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by PLK1 in vitro. Hyperphosphorylated during the G2
CC phase of the cell cycle. Phosphorylation at Thr-373 occurs during the
CC G2/M phase, relieves its auto-inhibition status and stimulates its GEF
CC activity. Phosphorylation at Thr-444 in G2/M phase is required for
CC subsequent binding with PLK1 and Rho exchange activation.
CC Dephosphorylated at the time of cytokinesis. Phosphorylation at Thr-359
CC is required for its transformation activity in cancer cells (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37536.1; Type=Miscellaneous discrepancy; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
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DR EMBL; L11316; AAA37536.1; ALT_SEQ; mRNA.
DR EMBL; AK157718; BAE34166.1; -; mRNA.
DR EMBL; AK220452; BAD90277.1; -; mRNA.
DR EMBL; AC121099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466530; EDL34919.1; -; Genomic_DNA.
DR EMBL; CH466530; EDL34920.1; -; Genomic_DNA.
DR EMBL; BC023881; AAH23881.1; -; mRNA.
DR EMBL; BC025565; AAH25565.1; -; mRNA.
DR EMBL; BC032155; AAH32155.1; -; mRNA.
DR EMBL; BC045614; AAH45614.1; -; mRNA.
DR CCDS; CCDS17270.2; -. [Q07139-1]
DR CCDS; CCDS50875.1; -. [Q07139-2]
DR PIR; S32372; S32372.
DR RefSeq; NP_001171096.1; NM_001177625.1. [Q07139-2]
DR RefSeq; NP_001171097.1; NM_001177626.1. [Q07139-2]
DR RefSeq; NP_031926.2; NM_007900.3. [Q07139-1]
DR RefSeq; XP_006535448.1; XM_006535385.3. [Q07139-1]
DR RefSeq; XP_006535449.1; XM_006535386.3. [Q07139-1]
DR PDB; 2COU; NMR; -; A=266-361.
DR PDBsum; 2COU; -.
DR AlphaFoldDB; Q07139; -.
DR SMR; Q07139; -.
DR BioGRID; 199370; 47.
DR IntAct; Q07139; 27.
DR STRING; 10090.ENSMUSP00000103935; -.
DR iPTMnet; Q07139; -.
DR PhosphoSitePlus; Q07139; -.
DR EPD; Q07139; -.
DR jPOST; Q07139; -.
DR MaxQB; Q07139; -.
DR PaxDb; Q07139; -.
DR PeptideAtlas; Q07139; -.
DR PRIDE; Q07139; -.
DR ProteomicsDB; 277440; -. [Q07139-1]
DR ProteomicsDB; 277441; -. [Q07139-2]
DR Antibodypedia; 33733; 387 antibodies from 32 providers.
DR DNASU; 13605; -.
DR Ensembl; ENSMUST00000108298; ENSMUSP00000103933; ENSMUSG00000027699. [Q07139-2]
DR Ensembl; ENSMUST00000108300; ENSMUSP00000103935; ENSMUSG00000027699. [Q07139-1]
DR Ensembl; ENSMUST00000176242; ENSMUSP00000135740; ENSMUSG00000027699. [Q07139-2]
DR GeneID; 13605; -.
DR KEGG; mmu:13605; -.
DR UCSC; uc008oth.2; mouse. [Q07139-1]
DR UCSC; uc008oti.2; mouse. [Q07139-2]
DR CTD; 1894; -.
DR MGI; MGI:95281; Ect2.
DR VEuPathDB; HostDB:ENSMUSG00000027699; -.
DR eggNOG; KOG3524; Eukaryota.
DR GeneTree; ENSGT00940000156299; -.
DR HOGENOM; CLU_008187_0_0_1; -.
DR InParanoid; Q07139; -.
DR OMA; WFWISVQ; -.
DR OrthoDB; 557169at2759; -.
DR PhylomeDB; Q07139; -.
DR TreeFam; TF101161; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 13605; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Ect2; mouse.
DR EvolutionaryTrace; Q07139; -.
DR PRO; PR:Q07139; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q07139; protein.
DR Bgee; ENSMUSG00000027699; Expressed in medial ganglionic eminence and 189 other tissues.
DR ExpressionAtlas; Q07139; baseline and differential.
DR Genevisible; Q07139; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0097149; C:centralspindlin complex; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.10190; -; 3.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR026817; Ect2.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16777; PTHR16777; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Cytoplasm; Cytoskeleton; Differentiation;
KW Guanine-nucleotide releasing factor; Isopeptide bond; Neurogenesis;
KW Nucleus; Phosphoprotein; Protein transport; Proto-oncogene;
KW Reference proteome; Repeat; Tight junction; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT CHAIN 2..913
FT /note="Protein ECT2"
FT /id="PRO_0000080939"
FT DOMAIN 176..260
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 266..354
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 452..641
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 675..794
FT /note="PH"
FT REGION 389..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 378..382
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 401..405
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 359
FT /note="Phosphothreonine; by PKC/PRKCI"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 846
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H8V3"
FT VAR_SEQ 49..52
FT /note="VEAR -> LKQE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8464478"
FT /id="VSP_041979"
FT VAR_SEQ 53..913
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8464478"
FT /id="VSP_041980"
FT VAR_SEQ 71..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4"
FT /id="VSP_041981"
FT CONFLICT 11
FT /note="S -> T (in Ref. 7; AAH32155)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> G (in Ref. 7; AAH32155)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> S (in Ref. 7; AAH23881)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="E -> K (in Ref. 7; AAH45614)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="L -> V (in Ref. 7; AAH32155)"
FT /evidence="ECO:0000305"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:2COU"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2COU"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:2COU"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2COU"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2COU"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2COU"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:2COU"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2COU"
SQ SEQUENCE 913 AA; 103131 MW; 2F0CC71DBF9D8280 CRC64;
MADDSVLPSP SEITSLADSS VFDSKVAEMS KENLCLASTS NVDEEMPQVE ARVIMVQDAG
KQEELLKALK TIKIMEVPVI KIKESCPGKS EEKLIKSIIN MEMKVPCVKM DSMEEFESLD
SPEFENIFVV TDFQNSVFND LYKADCRIVG PPVILNCAQR GEPLPFSCRP LYCTSMLNLV
LCFTGFRKKE ELVKLVTLVH HMGGVIRKEC NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP
EWIYKAWERR NEQCFCAAVD DFRNEFKVPP FQDCILSFLG FSDEEKHSME EMTEMQGGSY
LPVGDERCTH LIVEENTVKD LPFEPSKKLF VVKQEWFWGS IQMDARAGET MYLYEKANTP
ELKKSVSLLS LSTPNSNRKR RRLKETLAQL SRETDLSPFP PRKRPSAEHS LSIGSLLDIS
NTPESSIHYG ETPKSCAKSS RSSTPVPPKQ SARWQVAKEL YQTESNYVNI LATIIQLFQV
PLEEEGQRGG PILAPEEIKT IFGSIPDIFD VHMKIKDDLE DLIANWDESR SIGDIFLKYA
KDLVKTYPPF VNFFEMSKEM IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ IFDVVYEVDG
CPANLLSSHR SLVQRVETVS LGEHPCDRGE QVTLFLFNDC LEIARKRHKV IGTFRSPHDR
TRPPASLKHI HLMPLSQIKK VLDIRETEDC HNAFALLVRP PTEQANVLLS FQMTSEELPK
ESWLKMLCRH VANTICKADA ENLMYVADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA
FSFSKTPKRA LRMALSSSHS SEGRSPPSSG KLAVSRLSST SSLAGIPSPS LVSLPSFFER
RSHTLSRSTT HLI
