MACROD1
entrez
28992
canonical
uniprot
Q9BQ69
canonical
ensembl
ENSG00000133315
resolver
ensp
ENSP00000255681
resolver
ensp
ENSP00000502549
resolver
ensp
ENSP00000579184
resolver
ensp
ENSP00000660137
resolver
ensp
ENSP00000780941
resolver
enst
ENST00000255681
resolver
enst
ENST00000675777
resolver
enst
ENST00000909125
resolver
genesymbol
MACROD1
resolver
genesymbol_syn
LRP16
resolver
hgnc
HGNC:29598
resolver
uniprot
A0A6Q8PH91
resolver
uniprot
Q9UH96
resolver
uniprot_entry
A0A6Q8PH91_HUMAN
resolver
uniprot_entry
MACD1_HUMAN
resolver
uniprot_sec
Q9UH96
resolver
activity_regulation
ACTIVITY REGULATION: Subject to competitive inhibition by the product ADP-ribose. {ECO:0000269|PubMed:21257746}.
uniprot
proteins
amino_acid_sequence
MSLQSRLSGRLAQLRAAGQLLVPPRPRPGHLAGATRTRSSTCGPPAFLGVFGRRARTSAGVGAWGAAAVGRTAGVRTWAPLAMAAKVDLSTSTDWKEAKSFLKGLSDKQREEHYFCKDFVRLKKIPTWKEMAKGVAVKVEEPRYKKDKQLNEKISLLRSDITKLEVDAIVNAANSSLLGGGGVDGCIHRAAGPLLTDECRTLQSCKTGKAKITGGYRLPAKYVIHTVGPIAYGEPSASQAAELRSCYLSSLDLLLEHRLRSVAFPCISTGVFGYPCEAAAEIVLATLREWLEQHKDKVDRLIICVFLEKDEDIYRSRLPHYFPVA
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving MACROD1 is found in acute leukemia. Translocation t(11;21)(q13;q22) that forms a RUNX1-MACROD1 fusion protein. {ECO:0000269|PubMed:17532767}.
uniprot
proteins
ec_number
3.1.1.106
uniprot
proteins
ec_number
3.2.2.-
uniprot
proteins
function
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). {ECO:0000269|PubMed:17893710, ECO:0000269|PubMed:17914104, ECO:0000269|PubMed:19022849, ECO:0000269|PubMed:19403568, ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}.
uniprot
proteins
mass_dalton
35505
uniprot
proteins
mutagenesis
MUTAGEN 160; /note="D->A: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:21257746"; MUTAGEN 167; /note="D->A: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:21257746"; MUTAGEN 171; /note="N->A: Reduced enzyme activity. No significant effect on affinity for substrate."; /evidence="ECO:0000269|PubMed:21257746"; MUTAGEN 174; /note="N->A: Slightly reduced ADP-ribosyl hydrolase activity; when associated with A-184. Reduces O-acetyl-ADP-ribose deacetylase activity by 93%; when associated with A-184. No significant effect on affinity for substrate."; /evidence="ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712"; MUTAGEN 184; /note="D->A: Slightly reduced ADP-ribosyl hydrolase activity; when associated with A-174. Reduces O-acetyl-ADP-ribose deacetylase activity by 93%; when associated with A-174. No significant effect on affinity for substrate."; /evidence="ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714"; MUTAGEN 188; /note="H->A: Reduced enzyme activity."; /evidence="ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474714"; MUTAGEN 268; /note="S->A: No significant effect on enzyme activity."; /evidence="ECO:0000269|PubMed:21257746"; MUTAGEN 270; /note="G->E: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:21257746, ECO:0000269|PubMed:23474712
uniprot
proteins
protein_family
MacroD-type family
uniprot
proteins
protein_family
MacroD1/2-like subfamily
uniprot
proteins
pubmed
12578638
uniprot
proteins
pubmed
12790785
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17532767
uniprot
proteins
pubmed
17893710
uniprot
proteins
pubmed
17914104
uniprot
proteins
pubmed
19022849
uniprot
proteins
pubmed
19403568
uniprot
proteins
pubmed
21257746
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23474712
uniprot
proteins
pubmed
23474714
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
31599159
uniprot
proteins
sequence_length
325
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}.
uniprot
proteins