Hmdb loader
Identification
HMDB Protein ID HMDBP12404
Secondary Accession Numbers None
Name ADP-ribose glycohydrolase MACROD1
Synonyms
  1. MACRO domain-containing protein 1
  2. O-acetyl-ADP-ribose deacetylase MACROD1
  3. Protein LRP16
  4. [Protein ADP-ribosylaspartate] hydrolase MACROD1
  5. [Protein ADP-ribosylglutamate] hydrolase MACROD1
Gene Name MACROD1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Removes ADP-ribose from asparatate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474714, PubMed:23474712). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474714, PubMed:23474712). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21257746). Plays a role in estrogen signaling (PubMed:17893710, PubMed:17914104, PubMed:19403568). Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen (PubMed:19022849). May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation (PubMed:17893710, PubMed:17914104). Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction (PubMed:17914104). Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells (PubMed:17893710). Enhances ESR1-mediated transcription activity (PubMed:17914104).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
protein de-ADP-ribosylation
response to DNA damage stimulus
purine nucleoside metabolic process
peptidyl-glutamate ADP-deribosylation
Cellular Component
nucleus
nucleoplasm
Molecular Function
hydrolase activity, acting on glycosyl bonds
deacetylase activity
ADP-ribosylglutamate hydrolase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 325
Molecular Weight 35504.7
Theoretical pI 9.506
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9BQ69
UniProtKB/Swiss-Prot Entry Name MACD1_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Han WD, Zhao YL, Meng YG, Zang L, Wu ZQ, Li Q, Si YL, Huang K, Ba JM, Morinaga H, Nomura M, Mu YM: Estrogenically regulated LRP16 interacts with estrogen receptor alpha and enhances the receptor's transcriptional activity. Endocr Relat Cancer. 2007 Sep;14(3):741-53. [PubMed:17914104 ]
  3. Meng YG, Han WD, Zhao YL, Huang K, Si YL, Wu ZQ, Mu YM: Induction of the LRP16 gene by estrogen promotes the invasive growth of Ishikawa human endometrial cancer cells through the downregulation of E-cadherin. Cell Res. 2007 Oct;17(10):869-80. [PubMed:17893710 ]
  4. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460 ]
  5. Han WD, Yu L, Lou FD, Wang QS, Zhao Y, Shi ZJ, Jin HJ: [The Application of RACE Technique to Clone the Full-Length cDNA of A Novel Leukemia Associated Gene LRP16] Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2001 Mar;9(1):18-21. [PubMed:12578638 ]
  6. Han WD, Mu YM, Lu XC, Xu ZM, Li XJ, Yu L, Song HJ, Li M, Lu JM, Zhao YL, Pan CY: Up-regulation of LRP16 mRNA by 17beta-estradiol through activation of estrogen receptor alpha (ERalpha), but not ERbeta, and promotion of human breast cancer MCF-7 cell proliferation: a preliminary report. Endocr Relat Cancer. 2003 Jun;10(2):217-24. doi: 10.1677/erc.0.0100217. [PubMed:12790785 ]
  7. Imagama S, Abe A, Suzuki M, Hayakawa F, Katsumi A, Emi N, Kiyoi H, Naoe T: LRP16 is fused to RUNX1 in monocytic leukemia cell line with t(11;21)(q13;q22). Eur J Haematol. 2007 Jul;79(1):25-31. doi: 10.1111/j.1600-0609.2007.00858.x. Epub 2007 May 28. [PubMed:17532767 ]
  8. Yang J, Zhao YL, Wu ZQ, Si YL, Meng YG, Fu XB, Mu YM, Han WD: The single-macro domain protein LRP16 is an essential cofactor of androgen receptor. Endocr Relat Cancer. 2009 Mar;16(1):139-53. doi: 10.1677/ERC-08-0150. Epub 2008 Nov 20. [PubMed:19022849 ]
  9. Tian L, Wu Z, Zhao Y, Meng Y, Si Y, Fu X, Mu Y, Han W: Differential induction of LRP16 by liganded and unliganded estrogen receptor alpha in SKOV3 ovarian carcinoma cells. J Endocrinol. 2009 Jul;202(1):167-77. doi: 10.1677/JOE-09-0054. Epub 2009 Apr 29. [PubMed:19403568 ]
  10. Rosenthal F, Feijs KL, Frugier E, Bonalli M, Forst AH, Imhof R, Winkler HC, Fischer D, Caflisch A, Hassa PO, Luscher B, Hottiger MO: Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases. Nat Struct Mol Biol. 2013 Apr;20(4):502-7. doi: 10.1038/nsmb.2521. Epub 2013 Mar 10. [PubMed:23474714 ]
  11. Jankevicius G, Hassler M, Golia B, Rybin V, Zacharias M, Timinszky G, Ladurner AG: A family of macrodomain proteins reverses cellular mono-ADP-ribosylation. Nat Struct Mol Biol. 2013 Apr;20(4):508-14. doi: 10.1038/nsmb.2523. Epub 2013 Mar 10. [PubMed:23474712 ]
  12. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712 ]
  13. Hendriks IA, Lyon D, Young C, Jensen LJ, Vertegaal AC, Nielsen ML: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat Struct Mol Biol. 2017 Mar;24(3):325-336. doi: 10.1038/nsmb.3366. Epub 2017 Jan 23. [PubMed:28112733 ]
  14. Chen D, Vollmar M, Rossi MN, Phillips C, Kraehenbuehl R, Slade D, Mehrotra PV, von Delft F, Crosthwaite SK, Gileadi O, Denu JM, Ahel I: Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J Biol Chem. 2011 Apr 15;286(15):13261-71. doi: 10.1074/jbc.M110.206771. Epub 2011 Jan 21. [PubMed:21257746 ]