CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021518
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein ECT2 
Protein Synonyms/Alias
 Epithelial cell-transforming sequence 2 oncogene 
Gene Name
 ECT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61ILVQEAGKQEELIKAubiquitination[1]
239SLGTPIMKPEWIYKAubiquitination[1]
384NRKRRRLKETLAQLSubiquitination[1]
449SSTPVPSKQSARWQVubiquitination[1]
611ALLLNDLKKHTADENubiquitination[1]
612LLLNDLKKHTADENPubiquitination[1]
709EIARKRHKVIGTFRSubiquitination[1]
797HVANTICKADAENLIubiquitination[1]
845TRAFSFSKTPKRALRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 171 260 BRCT 1.
 DOMAIN 266 354 BRCT 2.
 DOMAIN 452 641 DH.
 DOMAIN 675 794 PH.
 MOTIF 378 382 Nuclear localization signal.
 MOTIF 401 405 Nuclear localization signal.
 MOD_RES 359 359 Phosphothreonine; by PKC/PRKCI.
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 370 370 Phosphoserine.
 MOD_RES 373 373 Phosphothreonine; by CDK1.
 MOD_RES 376 376 Phosphoserine.
 MOD_RES 444 444 Phosphothreonine; by CDK1.
 MOD_RES 842 842 Phosphoserine.
 MOD_RES 846 846 Phosphothreonine; by CDK1.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Differentiation; Guanine-nucleotide releasing factor; Neurogenesis; Nucleus; Oncogene; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Tight junction; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 914 AA 
Protein Sequence
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE TRVILVQEAG 60
KQEELIKALK TIKIMEVPVI KIKESCPGKS DEKLIKSVIN MDIKVGFVKM ESVEEFEGLD 120
SPEFENVFVV TDFQDSVFND LYKADCRVIG PPVVLNCSQK GEPLPFSCRP LYCTSMMNLV 180
LCFTGFRKKE ELVRLVTLVH HMGGVIRKDF NSKVTHLVAN CTQGEKFRVA VSLGTPIMKP 240
EWIYKAWERR NEQDFYAAVD DFRNEFKVPP FQDCILSFLG FSDEEKTNME EMTEMQGGKY 300
LPLGDERCTH LVVEENIVKD LPFEPSKKLY VVKQEWFWGS IQMDARAGET MYLYEKANTP 360
ELKKSVSMLS LNTPNSNRKR RRLKETLAQL SRETDVSPFP PRKRPSAEHS LSIGSLLDIS 420
NTPESSINYG DTPKSCTKSS KSSTPVPSKQ SARWQVAKEL YQTESNYVNI LATIIQLFQV 480
PLEEEGQRGG PILAPEEIKT IFGSIPDIFD VHTKIKDDLE DLIVNWDESK SIGDIFLKYS 540
KDLVKTYPPF VNFFEMSKET IIKCEKQKPR FHAFLKINQA KPECGRQSLV ELLIRPVQRL 600
PSVALLLNDL KKHTADENPD KSTLEKAIGS LKEVMTHINE DKRKTEAQKQ IFDVVYEVDG 660
CPANLLSSHR SLVQRVETIS LGEHPCDRGE QVTLFLFNDC LEIARKRHKV IGTFRSPHGQ 720
TRPPASLKHI HLMPLSQIKK VLDIRETEDC HNAFALLVRP PTEQANVLLS FQMTSDELPK 780
ENWLKMLCRH VANTICKADA ENLIYTADPE SFEVNTKDMD STLSRASRAI KKTSKKVTRA 840
FSFSKTPKRA LRRALMTSHG SVEGRSPSSN DKHVMSRLSS TSSLAITHSV STSNVIGFTK 900
HVYVQRLNST GGRSQYSWFQ SVRHSAFRAS FSEILEGNTD FSNFKKVLSK SSLTFVKN 958 
Gene Ontology
 GO:0097149; C:centralspindlin complex; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005923; C:tight junction; IDA:UniProtKB.
 GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
 GO:0032863; P:activation of Rac GTPase activity; IMP:UniProtKB.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0000902; P:cell morphogenesis; IEA:Compara.
 GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
 GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
 GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
 GO:0000910; P:cytokinesis; IMP:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0043089; P:positive regulation of Cdc42 GTPase activity; IDA:UniProtKB.
 GO:0032467; P:positive regulation of cytokinesis; IDA:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
 GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0070830; P:tight junction assembly; IMP:UniProtKB. 
Interpro
 IPR001357; BRCT_dom.
 IPR000219; DH-domain.
 IPR026817; Ect2.
 IPR001331; GDS_CDC24_CS.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF00533; BRCT
 PF12738; PTCB-BRCT
 PF00621; RhoGEF 
SMART
 SM00292; BRCT
 SM00233; PH
 SM00325; RhoGEF 
PROSITE
 PS50172; BRCT
 PS00741; DH_1
 PS50010; DH_2
 PS50003; PH_DOMAIN 
PRINTS