CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041989
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Epithelial cell transforming sequence 2 oncogene, isoform CRA_b 
Protein Synonyms/Alias
 Protein ECT2 
Gene Name
 ECT2 
Gene Synonyms/Alias
 hCG_1811567 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
208SLGTPIMKPEWIYKAubiquitination[1]
268MTEMQGGKYLPLGDEubiquitination[2]
353NRKRRRLKETLAQLSubiquitination[1]
418SSTPVPSKQSARWQVubiquitination[1, 3]
580ALLLNDLKKHTADENubiquitination[1, 2]
678EIARKRHKVIGTFRSubiquitination[1]
766HVANTICKADAENLIubiquitination[1]
786ESFEVNTKDMDSTLSubiquitination[2, 4]
814TRAFSFSKTPKRALRubiquitination[1, 3]
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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 927 AA 
Protein Sequence
MAENSVLTST TGRTSLADSS IFDSKVTEIS KENLLIGSTS YVEEEMPQIE TRVILVQEAG 60
KQEELIKALK DIKVGFVKME SVEEFEGLDS PEFENVFVVT DFQDSVFNDL YKADCRVIGP 120
PVVLNCSQKG EPLPFSCRPL YCTSMMNLVL CFTGFRKKEE LVRLVTLVHH MGGVIRKDFN 180
SKVTHLVANC TQGEKFRVAV SLGTPIMKPE WIYKAWERRN EQDFYAAVDD FRNEFKVPPF 240
QDCILSFLGF SDEEKTNMEE MTEMQGGKYL PLGDERCTHL VVEENIVKDL PFEPSKKLYV 300
VKQEWFWGSI QMDARAGETM YLYEKANTPE LKKSVSMLSL NTPNSNRKRR RLKETLAQLS 360
RETDVSPFPP RKRPSAEHSL SIGSLLDISN TPESSINYGD TPKSCTKSSK SSTPVPSKQS 420
ARWQVAKELY QTESNYVNIL ATIIQLFQVP LEEEGQRGGP ILAPEEIKTI FGSIPDIFDV 480
HTKIKDDLED LIVNWDESKS IGDIFLKYSK DLVKTYPPFV NFFEMSKETI IKCEKQKPRF 540
HAFLKINQAK PECGRQSLVE LLIRPVQRLP SVALLLNDLK KHTADENPDK STLEKAIGSL 600
KEVMTHINED KRKTEAQKQI FDVVYEVDGC PANLLSSHRS LVQRVETISL GEHPCDRGEQ 660
VTLFLFNDCL EIARKRHKVI GTFRSPHGQT RPPASLKHIH LMPLSQIKKV LDIRETEDCH 720
NAFALLVRPP TEQANVLLSF QMTSDELPKE NWLKMLCRHV ANTICKADAE NLIYTADPES 780
FEVNTKDMDS TLSRASRAIK KTSKKVTRAF SFSKTPKRAL RRALMTSHGS VEGRSPSSND 840
KHVMSRLSST SSLAITHSVS TSNVIGFTKH VYVQRLNSTG GRSQYSWFQS VRHSAFRASF 900
SEILEGNTDF SNFKKVLSKS SLTFVKN 927 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0005096; F:GTPase activator activity; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0000902; P:cell morphogenesis; IEA:InterPro.
 GO:0000910; P:cytokinesis; IEA:InterPro.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0045666; P:positive regulation of neuron differentiation; IEA:InterPro.
 GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. 
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 
PRINTS