CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021465
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exonuclease V 
Protein Synonyms/Alias
 Exo V; hExo5; Defects in morphology protein 1 homolog 
Gene Name
 EXO5 
Gene Synonyms/Alias
 C1orf176; DEM1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110PGFLAPEKAAVLDTGubiquitination[1]
198ELELAELKTRRRPMLubiquitination[2]
243ASLIHHTKLCLEKPLubiquitination[1]
248HTKLCLEKPLGPSVLubiquitination[1]
356ADICEWRKGSGVLSSubiquitination[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]
 [2] 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
 Single-stranded DNA (ssDNA) bidirectional exonuclease involved in DNA repair. Probably involved in DNA repair following ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage. Has both 5'-3' and 3'-5' exonuclease activities with a strong preference for 5'-ends. Acts as a sliding exonuclease that loads at ssDNA ends and then slides along the ssDNA prior to cutting; however the sliding and the 3'-5' exonuclease activities are abolished upon binding to the replication protein A (RPA) complex that enforces 5'-directionality activity. 
Sequence Annotation
 METAL 92 92 Iron-sulfur (4Fe-4S).
 METAL 343 343 Iron-sulfur (4Fe-4S).
 METAL 346 346 Iron-sulfur (4Fe-4S).
 METAL 352 352 Iron-sulfur (4Fe-4S).  
Keyword
 4Fe-4S; Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA-binding; Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium; Metal-binding; Nuclease; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 373 AA 
Protein Sequence
MAETREEETV SAEASGFSDL SDSEFLEFLD LEDAQESKAL VNMPGPSSES LGKDDKPISL 60
QNWKRGLDIL SPMERFHLKY LYVTDLATQN WCELQTAYGK ELPGFLAPEK AAVLDTGASI 120
HLARELELHD LVTVPVTTKE DAWAIKFLNI LLLIPTLQSE GHIREFPVFG EGEGVLLVGV 180
IDELHYTAKG ELELAELKTR RRPMLPLEAQ KKKDCFQVSL YKYIFDAMVQ GKVTPASLIH 240
HTKLCLEKPL GPSVLRHAQQ GGFSVKSLGD LMELVFLSLT LSDLPVIDIL KIEYIHQETA 300
TVLGTEIVAF KEKEVRAKVQ HYMAYWMGHR EPQGVDVEEA WKCRTCTYAD ICEWRKGSGV 360
LSSTLAPQVK KAK 373 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
 GO:0008310; F:single-stranded DNA specific 3'-5' exodeoxyribonuclease activity; TAS:UniProtKB.
 GO:0045145; F:single-stranded DNA specific 5'-3' exodeoxyribonuclease activity; IDA:UniProtKB.
 GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB. 
Interpro
 IPR019190; EXOV. 
Pfam
 PF09810; Morph_protein1 
SMART
  
PROSITE
  
PRINTS