CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018664
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
94LSTSTDWKEAKSFLKacetylation[1, 2, 3]
94LSTSTDWKEAKSFLKsuccinylation[3]
94LSTSTDWKEAKSFLKubiquitination[4]
97STDWKEAKSFLKGLSacetylation[1]
101KEAKSFLKGLSDKQRacetylation[1, 2, 3]
101KEAKSFLKGLSDKQRsuccinylation[3]
119YFCKDFIKLKKIPTWacetylation[1]
127LKKIPTWKETAKGLAacetylation[1, 2, 3]
127LKKIPTWKETAKGLAsuccinylation[3]
136TAKGLAVKVEDPKYKacetylation[2]
141AVKVEDPKYKKDKQLacetylation[1]
146DPKYKKDKQLNEKISacetylation[1, 5]
151KDKQLNEKISLYRGDacetylation[1]
161LYRGDITKLEVDAIVacetylation[2, 6, 7]
207LQNCETGKAKITCGYacetylation[3]
207LQNCETGKAKITCGYsuccinylation[3]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
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 (By similarity). 
Sequence Annotation
 DOMAIN 139 320 Macro.
 REGION 157 159 Substrate binding (By similarity).
 REGION 170 172 Substrate binding (By similarity).
 REGION 177 182 Substrate binding (By similarity).
 REGION 265 271 Substrate binding (By similarity).
 BINDING 304 304 Substrate (By similarity).  
Keyword
 Complete proteome; DNA damage; Hydrolase; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 323 AA 
Protein Sequence
MSLQSQVSGR LAQLRAAGQL LVSLRPWPGR SAGGPRPRGS ACGPLVALGE HGYCAWLSAG 60
VGAWGAAGRG AWVRTWAPLA MAAKVDLSTS TDWKEAKSFL KGLSDKQREE HYFCKDFIKL 120
KKIPTWKETA KGLAVKVEDP KYKKDKQLNE KISLYRGDIT KLEVDAIVNA ANSSLLGGGG 180
VDGCIHRAAG SLLTDECRTL QNCETGKAKI TCGYRLPAKY VIHTVGPIAV GQPTASQAAE 240
LRSCYLSSLD LLLEHRLRSV AFPCISTGVF GYPNEEAAEV VLASLREWLE QHKDKVDRLI 300
ICVFLEKDEG IYRERLPHYF PVA 323 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0019213; F:deacetylase activity; IEA:Compara.
 GO:0016798; F:hydrolase activity, acting on glycosyl bonds; ISS:UniProtKB.
 GO:0051725; P:protein de-ADP-ribosylation; ISS:UniProtKB.
 GO:0042278; P:purine nucleoside metabolic process; IEA:Compara.
 GO:0006974; P:response to DNA damage stimulus; ISS:UniProtKB. 
Interpro
 IPR002589; A1pp. 
Pfam
 PF01661; Macro 
SMART
 SM00506; A1pp 
PROSITE
 PS51154; MACRO 
PRINTS