Search Results

Overview

Uniprot IDQ9BQ69
Protein NameADP-ribose glycohydrolase MACROD1
Gene NameMACROD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 KEAKSFLKGLSDKQR
211 SCKTGKAKITGGYRL
96 LSTSTDWKEAKSFLK

Function

Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety (PubMed:23474712, PubMed:23474714). Inactive towards proteins bearing poly-ADP-ribose (PubMed:23474712, PubMed:23474714). 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)

Protein Sequence

10 MSLQSRLSGR 20 LAQLRAAGQL 30 LVPPRPRPGH 40 LAGATRTRSS 50 TCGPPAFLGV 60 FGRRARTSAG 70 VGAWGAAAVG 80 RTAGVRTWAP 90 LAMAAKVDLS 100 TSTDWKEAKS 110 FLKGLSDKQR 120 EEHYFCKDFV 130 RLKKIPTWKE 140 MAKGVAVKVE 150 EPRYKKDKQL 160 NEKISLLRSD 170 ITKLEVDAIV 180 NAANSSLLGG 190 GGVDGCIHRA 200 AGPLLTDECR 210 TLQSCKTGKA 220 KITGGYRLPA 230 KYVIHTVGPI 240 AYGEPSASQA 250 AELRSCYLSS 260 LDLLLEHRLR 270 SVAFPCISTG 280 VFGYPCEAAA 290 EIVLATLREW 300 LEQHKDKVDR 310 LIICVFLEKD 320 EDIYRSRLPH YFPVA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0140293 ADP-ribosylglutamate hydrolase activity
Molecular Function GO:0019213 deacetylase activity
Molecular Function GO:0016798 hydrolase activity, acting on glycosyl bonds
Molecular Function GO:0061463 O-acetyl-ADP-ribose deacetylase activity
Biological Process GO:0006974 DNA damage response
Biological Process GO:0140291 peptidyl-glutamate ADP-deribosylation
Biological Process GO:0051725 protein de-ADP-ribosylation
Biological Process GO:0042278 purine nucleoside metabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.