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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
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
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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 ]