CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020036
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 O-acetyl-ADP-ribose deacetylase MACROD1 
Protein Synonyms/Alias
 MACRO domain-containing protein 1; Protein LRP16; [Protein ADP-ribosylglutamate] hydrolase 
Gene Name
 MACROD1 
Gene Synonyms/Alias
 LRP16 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
103KEAKSFLKGLSDKQRacetylation[1]
163LLRSDITKLEVDAIVacetylation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
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. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity. 
Sequence Annotation
 DOMAIN 141 322 Macro.
 REGION 159 161 Substrate binding (By similarity).
 REGION 172 174 Substrate binding (By similarity).
 REGION 179 184 Substrate binding (By similarity).
 REGION 267 273 Substrate binding (Probable).
 BINDING 306 306 Substrate (By similarity).  
Keyword
 3D-structure; Chromosomal rearrangement; Complete proteome; DNA damage; Hydrolase; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 325 AA 
Protein Sequence
MSLQSRLSGR LAQLRAAGQL LVPPRPRPGH LAGATRTRSS TCGPPAFLGV FGRRARTSAG 60
VGAWGAAAVG RTAGVRTWAP LAMAAKVDLS TSTDWKEAKS FLKGLSDKQR EEHYFCKDFV 120
RLKKIPTWKE MAKGVAVKVE EPRYKKDKQL NEKISLLRSD ITKLEVDAIV NAANSSLLGG 180
GGVDGCIHRA AGPLLTDECR TLQSCKTGKA KITGGYRLPA KYVIHTVGPI AYGEPSASQA 240
AELRSCYLSS LDLLLEHRLR SVAFPCISTG VFGYPCEAAA EIVLATLREW LEQHKDKVDR 300
LIICVFLEKD EDIYRSRLPH YFPVA 325 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 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: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