CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023633
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclease EXOG, mitochondrial 
Protein Synonyms/Alias
 Endonuclease G-like 1; Endo G-like 1 
Gene Name
 EXOG 
Gene Synonyms/Alias
 ENDOGL1; ENDOGL2; ENGL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MAIKSIASRLRubiquitination[1, 2]
230AVPSHLYKVILARRSubiquitination[3]
327RSVLRLEKIMENLKNubiquitination[3]
333EKIMENLKNAEIEPDubiquitination[3, 4]
349YFMSRYEKKLEELKAubiquitination[3]
350FMSRYEKKLEELKAKubiquitination[3]
355EKKLEELKAKEQSGTubiquitination[5]
Reference
 [1] 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]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] 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]
 [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] 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
 Endo/exonuclease with nicking activity towards supercoiled DNA, a preference for single stranded DNA and 5'-3' exonuclease activity. 
Sequence Annotation
 ACT_SITE 140 140 Proton acceptor.
 METAL 171 171 Divalent metal cation; catalytic (By  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Nuclease; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 368 AA 
Protein Sequence
MAIKSIASRL RGSRRFLSGF VAGAVVGAAG AGLAALQFFR SQGAEGALTG KQPDGSAEKA 60
VLEQFGFPLT GTEARCYTNH ALSYDQAKRV PRWVLEHISK SKIMGDADRK HCKFKPDPNI 120
PPTFSAFNED YVGSGWSRGH MAPAGNNKFS SKAMAETFYL SNIVPQDFDN NSGYWNRIEM 180
YCRELTERFE DVWVVSGPLT LPQTRGDGKK IVSYQVIGED NVAVPSHLYK VILARRSSVS 240
TEPLALGAFV VPNEAIGFQP QLTEFQVSLQ DLEKLSGLVF FPHLDRTSDI RNICSVDTCK 300
LLDFQEFTLY LSTRKIEGAR SVLRLEKIME NLKNAEIEPD DYFMSRYEKK LEELKAKEQS 360
GTQIRKPS 368 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0004519; F:endonuclease activity; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro. 
Interpro
 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