Details for: ADPRS
Associated with
Other Information
Genular Protein ID: 4093453914
Symbol: ADPRS_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 12070318
Title: The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse.
PubMed ID: 12070318
DOI: 10.1110/ps.0200602
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 16710414
Title: The DNA sequence and biological annotation of human chromosome 1.
PubMed ID: 16710414
DOI: 10.1038/nature04727
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 16278211
Title: Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase.
PubMed ID: 16278211
PubMed ID: 17075046
Title: The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases.
PubMed ID: 17075046
PubMed ID: 17991898
Title: Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix.
PubMed ID: 17991898
DOI: 10.1128/mcb.01766-07
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21498885
Title: Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.
PubMed ID: 21498885
PubMed ID: 22433848
Title: ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).
PubMed ID: 22433848
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 28650317
Title: Serine ADP-ribosylation reversal by the hydrolase ARH3.
PubMed ID: 28650317
DOI: 10.7554/elife.28533
PubMed ID: 29234005
Title: Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase.
PubMed ID: 29234005
PubMed ID: 29480802
Title: Serine is the major residue for ADP-ribosylation upon DNA damage.
PubMed ID: 29480802
DOI: 10.7554/elife.34334
PubMed ID: 31599159
Title: The ARH and Macrodomain Families of alpha-ADP-ribose-acceptor Hydrolases Catalyze alpha-NAD+ Hydrolysis.
PubMed ID: 31599159
PubMed ID: 30830864
Title: PARP1 inhibition alleviates injury in ARH3-deficient mice and human cells.
PubMed ID: 30830864
PubMed ID: 33769608
Title: Molecular Tools for the Study of ADP-Ribosylation: A Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides.
PubMed ID: 33769608
PubMed ID: 17015823
Title: The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation.
PubMed ID: 17015823
PubMed ID: 21892188
Title: The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase.
PubMed ID: 21892188
DOI: 10.1038/nature10404
PubMed ID: 33186521
Title: An HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation.
PubMed ID: 33186521
PubMed ID: 34625544
Title: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
PubMed ID: 34625544
PubMed ID: 16511307
Title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
PubMed ID: 16511307
PubMed ID: 17327674
Title: On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
PubMed ID: 17327674
PubMed ID: 30045870
Title: Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.
PubMed ID: 30045870
PubMed ID: 29907568
Title: Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition.
PubMed ID: 29907568
PubMed ID: 33894202
Title: Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
PubMed ID: 33894202
PubMed ID: 34321462
Title: Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
PubMed ID: 34321462
PubMed ID: 30100084
Title: Biallelic mutations in ADPRHL2, encoding ADP-ribosylhydrolase 3, lead to a degenerative pediatric stress-induced epileptic ataxia syndrome.
PubMed ID: 30100084
PubMed ID: 30401461
Title: Bi-allelic ADPRHL2 mutations cause neurodegeneration with developmental delay, ataxia, and axonal neuropathy.
PubMed ID: 30401461
PubMed ID: 34479984
Title: Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response.
PubMed ID: 34479984
PubMed ID: 34019811
Title: Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.
PubMed ID: 34019811
Sequence Information:
- Length: 363
- Mass: 38947
- Checksum: 5FD99F59F27CD29F
- Sequence:
MAAAAMAAAA GGGAGAARSL SRFRGCLAGA LLGDCVGSFY EAHDTVDLTS VLRHVQSLEP DPGTPGSERT EALYYTDDTA MARALVQSLL AKEAFDEVDM AHRFAQEYKK DPDRGYGAGV VTVFKKLLNP KCRDVFEPAR AQFNGKGSYG NGGAMRVAGI SLAYSSVQDV QKFARLSAQL THASSLGYNG AILQALAVHL ALQGESSSEH FLKQLLGHME DLEGDAQSVL DARELGMEER PYSSRLKKIG ELLDQASVTR EEVVSELGNG IAAFESVPTA IYCFLRCMEP DPEIPSAFNS LQRTLIYSIS LGGDTDTIAT MAGAIAGAYY GMDQVPESWQ QSCEGYEETD ILAQSLHRVF QKS
Genular Protein ID: 4159266152
Symbol: B7ZAN4_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11181995
Sequence Information:
- Length: 209
- Mass: 22755
- Checksum: CF1AE30A9A3228F0
- Sequence:
MRVAGISLAY SSVQDVQKFA RLSAQLTHAS SLGYNGAILQ ALAVHLALQG ESSSEHFLKQ LLGHMEDLEG DAQSVLDARE LGMEERPYSS RLKKIGELLD QASVTREEVV SELGNGIAAF ESVPTAIYCF LRCMEPDPEI PSAFNSLQRT LIYSISLGGD TDTIATMAGA IAGAYYGMDQ VPESWQQSCE GYEETDILAQ SLHRVFQKS
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.