Hmdb loader
Identification
HMDB Protein ID HMDBP10630
Secondary Accession Numbers
  • 16859
Name [Protein ADP-ribosylarginine] hydrolase
Synonyms
  1. ADP-ribose-L-arginine cleaving enzyme
  2. ADP-ribosylarginine hydrolase
Gene Name ADPRH
Protein Type Enzyme
Biological Properties
General Function Involved in magnesium ion binding
Specific Function Catalyzes the reverse reaction of mono-ADP-ribosylation.
Pathways Not Available
Reactions
Protein-N(omega)-(ADP-D-ribosyl)-L-arginine + Water → Adenosine diphosphate ribose + protein-L-arginine details
ADP-Ribosyl-L-arginine + Water → Adenosine diphosphate ribose + L-Arginine details
GO Classification
Biological Process
cellular protein modification process
protein de-ADP-ribosylation
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
magnesium ion binding
hydrolase activity, hydrolyzing n-glycosyl compounds
adp-ribosylarginine hydrolase activity
Molecular Function
magnesium ion binding
ADP-ribosylarginine hydrolase activity
Process
metabolic process
macromolecule metabolic process
post-translational protein modification
macromolecule modification
protein amino acid de-adp-ribosylation
protein modification process
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location 3
Locus 3q13.31-q13.33
SNPs ADPRH
Gene Sequence
>1074 bp
ATGGAGAAGTATGTGGCTGCTATGGTGCTGAGTGCAGCTGGAGATGCCCTGGGGTACTAC
AATGGGAAGTGGGAGTTCCTCCAGGATGGGGAGAAGATACACCGGCAGTTGGCCCAGCTG
GGCGGCTTGGATGCCCTAGACGTGGGAAGGTGGAGAGTTAGTGACGACACAGTGATGCAC
TTGGCCACAGCAGAAGCTCTTGTGGAAGCTGGGAAAGCCCCTAAGTTGACTCAACTGTAT
TACCTCCTTGCTAAGCATTACCAAGACTGCATGGAAGACATGGATGGGCGGGCACCAGGT
GGTGCCTCGGTGCACAACGCCATGCAGCTGAAGCCGGGCAAGCCCAATGGCTGGAGGATT
CCCTTCAACAGCCATGAGGGCGGCTGTGGGGCTGCCATGCGGGCCATGTGCATCGGTCTC
AGGTTCCCACACCATAGCCAACTGGACACACTGATCCAAGTGAGCATCGAGAGTGGTCGG
ATGACCCACCACCACCCAACAGGCTACCTGGGGGCCCTTGCGTCTGCTCTTTTTACAGCC
TATGCTGTGAATAGCAGACCACCCTTGCAGTGGGGAAAAGGACTGATGGAGCTGCTACCA
GAAGCTAAAAAGTACATTGTCCAATCAGGCTACTTTGTAGAGGAAAATCTTCAACACTGG
TCCTACTTCCAAACCAAATGGGAAAATTACCTAAAACTTAGAGGGATTTTGGATGGAGAA
TCAGCCCCTACCTTCCCTGAGTCTTTCGGTGTGAAGGAGAGGGATCAGTTCTACACCTCC
CTGAGCTACTCTGGCTGGGGTGGCAGCAGTGGGCACGATGCCCCCATGATTGCCTACGAT
GCTGTTCTTGCTGCAGGAGACTCCTGGAAGGAGCTTGCCCACCGAGCCTTTTTCCATGGT
GGAGACAGTGATTCTACAGCTGCCATTGCTGGCTGCTGGTGGGGAGTTATGTATGGTTTT
AAAGGAGTGAGTCCCTCCAACTATGAGAAACTAGAATACAGAAACCGGCTGGAAGAGACA
GCTAGGGCTTTATATTCTCTCGGGTCAAAAGAAGACACTGTAATTTCCCTTTAG
Protein Properties
Number of Residues 357
Molecular Weight 39506.34
Theoretical pI 6.526
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>[Protein ADP-ribosylarginine] hydrolase
MEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDALDVGRWRVSDDTVMH
LATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDGRAPGGASVHNAMQLKPGKPNGWRI
PFNSHEGGCGAAMRAMCIGLRFPHHSQLDTLIQVSIESGRMTHHHPTGYLGALASALFTA
YAVNSRPPLQWGKGLMELLPEAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGE
SAPTFPESFGVKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRAFFHG
GDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLGSKEDTVISL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P54922
UniProtKB/Swiss-Prot Entry Name ADPRH_HUMAN
PDB IDs
GenBank Gene ID L13291
GeneCard ID ADPRH
GenAtlas ID ADPRH
HGNC ID HGNC:269
References
General References
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  3. Takada T, Iida K, Moss J: Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J Biol Chem. 1993 Aug 25;268(24):17837-43. [PubMed:8349667 ]