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ADPRHL2

Gene
adprhl2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Danio rerio
Length
370 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
40.103 kDa
Sequence
MSAAARVVAPVMMLSRFRGALVGSVLGDCIGGEFEGAVDVPLDRVLQHLSALEDDTRGDGILQYSDDTAMMRCVADSLLTRMTFDERDMAQRFAKEYSHSPGRGYGSGVVQVLRKLASPHLKDVFQPAQAQFGGRGSFGNGGAMRAVPFALAFRSRADVRKYSRFGAMLTHSCSLGYNGAALQALAVHLSLQGALALPKDFIDKLISEMEELEKDETAKHDAKALNLSEFPYCSRLHRVKELMDKTSVSIEEVISELGNGIAALQSVPTAIFCVLYCLEPQDGLPERFGGLERTIAYSLALGGDTDTIACMAGAIAGAHYGIDSIPLSWQVSCEGVDEADDLARRLYDLYCLPQHNEDRGNNQPHTTNTD

Gene
Adprhl2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Mus musculus
Length
370 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (By similarity). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:24191052). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
39.414 kDa
Sequence
MAVAAAAAATAMSAAGGGGASAARSISRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKKLLNPKCRDVYEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLEQLLGHMEELEGDAQSVLDAKELGMEERPYSSRLKKVGELLDQDVVSREEVVSELGNGIAAFESVPTAIYCFLRCMEPHPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGFEETDVLAQSLHRVFQESS

Gene
ADPRHL2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Gallus gallus
Length
367 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
39.909 kDa
Sequence
MAAAGAGSGRAAVSRSRPPPARFRGCLAGALLGDCLGAVFEGRSVVKLPDLLSFLRGLEPPGGEGEPAGSARRETLSYTDDTAMSRCVVQSLLAKREFDEVDMAKRFAEEYKKEPNRGYGMAVVNVFKKLLSPQCSDVFEPARAQFNGKGSYGNGGAMRVAGIPLTYSDVQDVKKFAKLSAELTHANSLGYNGAILQALAVHLALQGEVSRETFLEQLISHMEDIEADDKSLTDARALGFEDLPFSRRLKKIKEFLELSSVPKEDVLFELGNGIAALRSVPTAIYSFLRCMEADPDIPEHYNNLQRTIIYCISLGGDTNTIATMAGAIAGAYYGEEQVPPSWEQSCEAFQETQKMANSLHELYCQQL

Gene
ADPRHL2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Bos taurus
Length
365 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
39.221 kDa
Sequence
MAAAAAMTAAGCGGAGAARSLSRFRGCLAGALLGDCVGAVYEARDTVDLTSVLRQVQDLEPDPGSPGSARTEALCYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFRKHLSPRCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLEQLLGHMEELESDAQSVLDARELGMEERPYSSRLKKIGELLEQDSVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSTFNSLQRTLVYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGYEETDVLAQSLHRVFQKSL

Gene
ADPRHL2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Homo sapiens
Length
363 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:21498885, PubMed:30045870, PubMed:29907568, PubMed:30401461). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:28650317, PubMed:29234005, PubMed:30045870). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed:16278211). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed:22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed:17075046, PubMed:21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed:21498885).
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
38.947 kDa
Sequence
MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEPDPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS

Gene
adprhl2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Latimeria chalumnae
Length
356 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:30472116). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:30472116). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:30472116). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
38.819 kDa
Sequence
MSAVGRLAAVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAGTLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVVQVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVIKFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMERIEGGEMSASDAGEHDRPNEVKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFLHCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQVTPSWKRSCEAIVETEESAVKLYELYCKQLKTP

Gene
adprhl2
Protein
ADP-ribose glycohydrolase ARH3
Organism
Xenopus tropicalis
Length
350 amino acids
Function
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
39.034 kDa
Sequence
MMAAGVSRFRGSLLGALLGDCIGAVFEGHTNVTKEFLFDYMKSLDKGERLKRVLTYTDDTAMARSIVQSVLENYEFNIEDLANRFTTEYNRDPDRGYGMAVVHVFEKLGSGEYKHVFSPAREQFDGKGSYGNGAAMRVVGISLAYPRIPDIIEYARTSGMLTHASSLGYNGAILQALAVHYALQGELAPETFLDQLLDHMKEVETDKKSRSDALELEMDEFPYCNKLRKIKAFLAREDVTRKDIVKELGNGIQAFESVPTAIYSFLRCLKPVSELPSELTNLQRTIAFCILLGGDTDTIATMAAAIAGAYHGEEQIPLNWKLSAEGYKDAEDWGEKLHQLYCRRLQSTTS