CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024302
UniProt Accession
Genbank Protein ID
 EF159161; AK131348; AK125899; AC006198; AL035073; AL049867; AL050324; AL118503; AL118510; AL132826; AL133462; AL136992; AL138808; AL139825; AL161800; AL355133; AL121582; AL049633; AL079338; AL117333; AL121584; AL136991; AL158088; AL353798; AL354773; AL357654; AL353798; AL049633; AL079338; AL117333; AL121582; AL121584; AL136991; AL158088; AL354773; AL357654; AL136991; AL049633; AL079338; AL117333; AL121582; AL121584; AL158088; AL353798; AL354773; AL357654; AL121584; AL049633; AL079338; AL117333; AL121582; AL136991; AL158088; AL353798; AL354773; AL357654; AL158088; AL049633; AL079338; AL117333; AL121582; AL121584; AL136991; AL353798; AL354773; AL357654; AL357654; AL049633; AL079338; AL117333; AL121582; AL121584; AL136991; AL158088; AL353798; AL354773; AL049633; AL079338; AL117333; AL121582; AL121584; AL136991; AL158088; AL353798; AL354773; AL357654; AL117333; AL049633; AL079338; AL121582; AL121584; AL136991; AL158088; AL353798; AL354773; AL357654; AL079338; AL049633; AL117333; AL121582; AL121584; AL136991; AL158088; AL353798; AL354773; AL357654; AL354773; AL049633; AL079338; AL117333; AL121582; AL121584; AL136991; AL158088; AL353798; AL357654; AL357654; AL079338; AL136991; AL357654; AL136991; AL079338; AL136991; AL357654; AL136991; AL079338; AL357654; AL136991; AL357654; CH471133; CH471133; BC018687; BC101216; BC101217; BC101218; BC101219; BC126936; BC035876 
Genbank Nucleotide ID
 ABM46908.1; BAD18504.1; BAG54262.1; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAH71976.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAI16368.2; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM14046.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM18337.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM26942.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27056.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM27329.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28281.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28328.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAM28330.1; CAQ06880.1; CAQ06880.1; CAQ06880.1; CAQ06881.1; CAQ06881.1; CAQ07295.1; CAQ07295.1; CAQ07295.1; CAQ08720.1; CAQ08720.1; CAQ08720.1; CAQ08721.1; CAQ08721.1; EAX10293.1; EAX10302.1; AAH18687.1 
Protein Name
 O-acetyl-ADP-ribose deacetylase MACROD2 
Protein Synonyms/Alias
 MACRO domain-containing protein 2; [Protein ADP-ribosylglutamate] hydrolase 
Gene Name
 MACROD2 
Gene Synonyms/Alias
 C20orf133 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
170NCYKSSLKLVKENNIubiquitination[1]
Reference
 [1] Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells.
 Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X.
 Proteomics. 2008 Jul;8(14):2885-96. [PMID: 18655026] 
Functional Description
 Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. 
Sequence Annotation
 DOMAIN 59 240 Macro.
 REGION 77 79 Substrate binding.
 REGION 90 92 Substrate binding.
 REGION 97 102 Substrate binding.
 REGION 185 191 Substrate binding.
 BINDING 224 224 Substrate.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; DNA damage; Hydrolase; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 448 AA 
Protein Sequence
MYPSNKKKKV WREEKERLLK MTLEERRKEY LRDYIPLNSI LSWKEEMKGK GQNDEENTQE 60
TSQVKKSLTE KVSLYRGDIT LLEVDAIVNA ANASLLGGGG VDGCIHRAAG PCLLAECRNL 120
NGCDTGHAKI TCGYDLPAKY VIHTVGPIAR GHINGSHKED LANCYKSSLK LVKENNIRSV 180
AFPCISTGIY GFPNEPAAVI ALNTIKEWLA KNHHEVDRII FCVFLEVDFK IYKKKMNEFF 240
SVDDNNEEEE DVEMKEDSDE NGPEEKQSVE EMEEQSQDAD GVNTVTVPGP ASEEAVEDCK 300
DEDFAKDENI TKGGEVTDHS VRDQDHPDGQ ENDSTKNEIK IETESQSSYM ETEELSSNQE 360
DAVIVEQPEV IPLTEDQEEK EGEKAPGEDT PRMPGKSEGS SDLENTPGPD VEMNSQVDKV 420
NDPTESQQED QLIAGAQDEA KEQRNGTK 448 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0019213; F:deacetylase activity; IDA:UniProtKB.
 GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
 GO:0042278; P:purine nucleoside metabolic process; IDA:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IMP:UniProtKB. 
Interpro
 IPR002589; A1pp. 
Pfam
 PF01661; Macro 
SMART
 SM00506; A1pp 
PROSITE
 PS51154; MACRO 
PRINTS