ADPRM
entrez
56985
canonical
uniprot
Q3LIE5
canonical
ensembl
ENSG00000170222
resolver
ensp
ENSP00000369099
resolver
genesymbol
ADPRM
resolver
genesymbol_syn
C17orf48
resolver
hgnc
HGNC:30925
resolver
uniprot
A8K9B4
resolver
uniprot
D3DTS4
resolver
uniprot
Q9BVD4
resolver
uniprot
Q9NRU8
resolver
uniprot
W0NWJ0
resolver
uniprot_entry
ADPRM_HUMAN
resolver
uniprot_sec
A8K9B4
resolver
uniprot_sec
D3DTS4
resolver
uniprot_sec
Q9BVD4
resolver
uniprot_sec
Q9NRU8
resolver
uniprot_sec
W0NWJ0
resolver
amino_acid_sequence
MDDKPNPEALSDSSERLFSFGVIADVQFADLEDGFNFQGTRRRYYRHSLLHLQGAIEDWNNESSMPCCVLQLGDIIDGYNAQYNASKKSLELVMDMFKRLKVPVHHTWGNHEFYNFSREYLTHSKLNTKFLEDQIVHHPETMPSEDYYAYHFVPFPKFRFILLDAYDLSVLGVDQSSPKYEQCMKILREHNPNTELNSPQGLSEPQFVQFNGGFSQEQLNWLNEVLTFSDTNQEKVVIVSHLPIYPDASDNVCLAWNYRDALAVIWSHECVVCFFAGHTHDGGYSEDPFGVYHVNLEGVIETAPDSQAFGTVHVYPDKMMLKGRGRVPDRIMNYKKERAFHC
uniprot
proteins
ec_number
3.6.1.16
uniprot
proteins
ec_number
3.6.1.53
uniprot
proteins
function
FUNCTION: Hydrolyzes ADP-ribose, ADP, CDP-glycerol, CDP-choline, CDP-ethanolamine and cyclic ADP-ribose (cADPR), but not other non-reducing ADP-sugars or CDP-glucose (PubMed:25692488). May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity). {ECO:0000250|UniProtKB:Q5M886, ECO:0000269|PubMed:25692488}.
uniprot
proteins
mass_dalton
39529
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="Q->H: Catalytic efficiency is reduced 11-fold with ADP-D-ribose or CDP-choline as substrate."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 37; /note="F->A: Catalytic efficiency is reduced 50-fold with ADP-D-ribose and 4-fold with CDP-choline as substrates. Catalytic efficiency is reduced 100-fold with ADP-D-ribose as substrate; when associated with A-196."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 37; /note="F->Y: Does not affect enzymatic activity."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 43; /note="R->A: Loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 110; /note="N->A: Catalytic efficiency is reduced 40-fold with ADP-D-ribose and 100-fold with CDP-choline as substrates."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 111; /note="H->A: Catalytic efficiency is reduced 200-fold with ADP-D-ribose and 500-fold with CDP-choline as substrates."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 111; /note="H->N: Catalytic efficiency is reduced 20-fold with ADP-D-ribose and 75-fold with CDP-choline as substrates."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 196; /note="L->A: Catalytic efficiency is reduced 5-fold with ADP-D-ribose and 2-fold with CDP-choline as substrates. Catalytic efficiency is reduced 100-fold with ADP-D-ribose; when associated with A-37."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 210; /note="F->A: Catalytic efficiency is reduced 70-fold with ADP-D-ribose and 40-fold with CDP-choline as substrates."; /evidence="ECO:0000269|PubMed:25692488"; MUTAGEN 253; /note="C->A: Has a very mild effect on enzymatic activity; catalytic efficiency is increased 1.7-fold with ADP-D-ribose and is unchanged with CDP-choline as substrates."; /evidence="ECO:0000269|PubMed:25692488
uniprot
proteins
protein_family
ADPRibase-Mn family
uniprot
proteins
pubmed
12880961
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
25692488
uniprot
proteins
sequence_length
342
uniprot
proteins