CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018741
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Engulfment and cell motility protein 1 
Protein Synonyms/Alias
 Protein ced-12 homolog 
Gene Name
 ELMO1 
Gene Synonyms/Alias
 KIAA0281 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9PPPADIVKVAIEWPGubiquitination[1]
20EWPGAYPKLMEIDQKubiquitination[1]
70EKNRNEIKNGTILRLubiquitination[1]
100QSSSMDAKLEALKDLacetylation[2]
100QSSSMDAKLEALKDLubiquitination[1]
105DAKLEALKDLASLSRacetylation[2]
105DAKLEALKDLASLSRubiquitination[1, 3]
218NSHDLYQKVAQEITIubiquitination[4]
269MANILAQKQLRSIILubiquitination[1]
312LEDRMMTKMDPQDQAubiquitination[1]
347NSSGSMEKRKSMYTRubiquitination[1]
422RSSIELTKMLCEILKubiquitination[1]
468QLLNKTWKEMRATSEubiquitination[1]
503PSSLDQFKSKLQNLSubiquitination[1]
516LSYTEILKIRQSERMubiquitination[1, 4, 5, 6]
537SRPILELKEKIQPEIubiquitination[1]
539PILELKEKIQPEILEubiquitination[1, 5]
549PEILELIKQQRLNRLubiquitination[1, 5]
584CRLSPNHKVLHYGDLubiquitination[1]
607PHDSLQDKLPVADIKubiquitination[1]
620IKAVVTGKDCPHMKEubiquitination[1, 6]
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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] 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]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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] 
Functional Description
 Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in assocation with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1. 
Sequence Annotation
 DOMAIN 319 492 ELMO.
 DOMAIN 555 676 PH.
 MOTIF 707 714 SH3-binding.
 MOD_RES 18 18 Phosphotyrosine; by HCK.
 MOD_RES 100 100 N6-acetyllysine.
 MOD_RES 105 105 N6-acetyllysine.
 MOD_RES 216 216 Phosphotyrosine; by HCK.
 MOD_RES 395 395 Phosphotyrosine; by HCK.
 MOD_RES 511 511 Phosphotyrosine; by HCK.
 MOD_RES 720 720 Phosphotyrosine; by HCK.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane; Complete proteome; Cytoplasm; Membrane; Phagocytosis; Phosphoprotein; Polymorphism; Reference proteome; SH3-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 727 AA 
Protein Sequence
MPPPADIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY 60
ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF 120
INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF 180
IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGSDQEIQ 240
TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL 300
TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG 360
FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL 420
TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV 480
MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI 540
QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP 600
HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH 660
EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY 720
DFVYDCN 727 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0030036; P:actin cytoskeleton organization; IGI:UniProtKB.
 GO:0006915; P:apoptotic process; NAS:UniProtKB.
 GO:0006928; P:cellular component movement; IGI:UniProtKB.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0006911; P:phagocytosis, engulfment; IGI:UniProtKB.
 GO:0016601; P:Rac protein signal transduction; IGI:UniProtKB.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR024574; DUF3361.
 IPR006816; Engulfment_cell_motility_ELMO.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF11841; DUF3361
 PF04727; ELMO_CED12 
SMART
 SM00233; PH 
PROSITE
 PS51335; ELMO
 PS50003; PH_DOMAIN 
PRINTS