CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012298
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endonuclease G, mitochondrial 
Protein Synonyms/Alias
 Endo G 
Gene Name
 ENDOG 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66RGPGELAKYGLPGLAubiquitination[1, 2]
76LPGLAQLKSRESYVLubiquitination[1, 2, 3, 4, 5]
153ANHRWSQKAMDDTFYubiquitination[1, 2, 3, 4]
181NAWNNLEKYSRSLTRubiquitination[1, 2]
210PRTEADGKSYVKYQVubiquitination[1, 2]
214ADGKSYVKYQVIGKNubiquitination[1, 2, 3, 4, 5, 6]
220VKYQVIGKNHVAVPTubiquitination[2, 6]
290LARAGSLKAITAGSKubiquitination[1, 2, 3, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [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
 Cleaves DNA at double-stranded (DG)n.(DC)n and at single-stranded (DC)n tracts. In addition to deoxyribonuclease activities, also has ribonuclease (RNase) and RNase H activities. Capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA (By similarity). 
Sequence Annotation
 ACT_SITE 141 141 Proton acceptor (By similarity).
 METAL 172 172 Magnesium or manganese; catalytic (By  
Keyword
 Complete proteome; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; Nuclease; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 297 AA 
Protein Sequence
MRALRAGLTL ASGAGLGAVV EGWRRRREDA RAAPGLLGRL PVLPVAAAAE LPPVPGGPRG 60
PGELAKYGLP GLAQLKSRES YVLCYDPRTR GALWVVEQLR PERLRGDGDR RECDFREDDS 120
VHAYHRATNA DYRGSGFDRG HLAAAANHRW SQKAMDDTFY LSNVAPQVPH LNQNAWNNLE 180
KYSRSLTRSY QNVYVCTGPL FLPRTEADGK SYVKYQVIGK NHVAVPTHFF KVLILEAAGG 240
QIELRTYVMP NAPVDEAIPL ERFLVPIESI ERASGLLFVP NILARAGSLK AITAGSK 297 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006309; P:apoptotic DNA fragmentation; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0046677; P:response to antibiotic; IEA:Compara.
 GO:0034612; P:response to tumor necrosis factor; IEA:Compara. 
Interpro
 IPR018524; DNA/RNA_endonuclease_AS.
 IPR001604; DNA/RNA_non-sp_Endonuclease.
 IPR020821; Extracellular_endonuc_su_A. 
Pfam
 PF01223; Endonuclease_NS 
SMART
 SM00892; Endonuclease_NS
 SM00477; NUC 
PROSITE
 PS01070; NUCLEASE_NON_SPEC 
PRINTS