CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030133
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 REX2, RNA exonuclease 2 homolog (S. cerevisiae) 
Protein Synonyms/Alias
 REX2, RNA exonuclease 2 homolog (S. cerevisiae), isoform CRA_b; cDNA, FLJ92319, highly similar to Homo sapiens REX2, RNA exonuclease 2 homolog (S. cerevisiae) (REXO2), mRNA 
Gene Name
 REXO2 
Gene Synonyms/Alias
 hCG_38016 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
160KYMPQFMKHLHYRIIubiquitination[1]
173IIDVSTVKELCRRWYubiquitination[1, 2]
205DDISESIKELQFYRNubiquitination[1, 2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Exonuclease; Hydrolase; Nuclease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 237 AA 
Protein Sequence
MLGGSLGSRL LRGVGGSHGR FGARGVREGG AAMAAGESMA QRMVWVDLEM TGLDIEKDQI 60
IEMACLITDS DLNILAEGPN LIIKQPDELL DSMSDWCKEH HGKSGLTKAV KESTITLQQA 120
EYEFLSFVRQ QTPPGLCPLA GNSVHEDKKF LDKYMPQFMK HLHYRIIDVS TVKELCRRWY 180
PEEYEFAPKK AASHRALDDI SESIKELQFY RNNIFKKKID EKKRKIIENG ENEKTVS 237 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro. 
Interpro
 IPR006055; Exonuclease.
 IPR013520; Exonuclease_RNaseT/DNA_pol3.
 IPR022894; Oligoribonuclease.
 IPR012337; RNaseH-like_dom. 
Pfam
 PF00929; RNase_T 
SMART
 SM00479; EXOIII 
PROSITE
  
PRINTS