Details for: BPHL
Associated with
Other Information
Genular Protein ID: 3004489553
Symbol: PARG_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14527731
Title: Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23).
PubMed ID: 14527731
PubMed ID: 15212953
Title: Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments.
PubMed ID: 15212953
PubMed ID: 10449915
Title: Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization.
PubMed ID: 10449915
DOI: 10.1159/000015310
PubMed ID: 17509564
Title: Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity.
PubMed ID: 17509564
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: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
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: 15450800
Title: A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): application to inhibitor identification and evaluation.
PubMed ID: 15450800
PubMed ID: 16460818
Title: Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage.
PubMed ID: 16460818
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19105632
Title: Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase.
PubMed ID: 19105632
DOI: 10.1021/pr800810n
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21892188
Title: The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase.
PubMed ID: 21892188
DOI: 10.1038/nature10404
PubMed ID: 21398629
Title: PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms.
PubMed ID: 21398629
DOI: 10.1093/nar/gkr099
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23102699
Title: Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression.
PubMed ID: 23102699
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23481255
Title: Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease.
PubMed ID: 23481255
PubMed ID: 23474714
Title: Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.
PubMed ID: 23474714
DOI: 10.1038/nsmb.2521
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24906880
Title: PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress.
PubMed ID: 24906880
DOI: 10.1093/nar/gku505
PubMed ID: 27257257
Title: ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.
PubMed ID: 27257257
PubMed ID: 33186521
Title: An HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation.
PubMed ID: 33186521
PubMed ID: 34019811
Title: Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.
PubMed ID: 34019811
PubMed ID: 34321462
Title: Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
PubMed ID: 34321462
PubMed ID: 23251397
Title: Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives.
PubMed ID: 23251397
PubMed ID: 30472116
Title: (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
PubMed ID: 30472116
Sequence Information:
- Length: 976
- Mass: 111110
- Checksum: D6646353C6D0180E
- Sequence:
MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV ESCAETADHS GQRTGT
Genular Protein ID: 1350870542
Symbol: BPHL_HUMAN
Name: Valacyclovir hydrolase
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 7759552
Title: Cloning and expression analysis of a novel human serine hydrolase with sequence similarity to prokaryotic enzymes involved in the degradation of aromatic compounds.
PubMed ID: 7759552
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
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: 2393862
Title: Cloning and sequencing of a complementary DNA encoding a M(r) 70,000 human breast epithelial mucin-associated antigen.
PubMed ID: 2393862
PubMed ID: 12732646
Title: Identification of a human valacyclovirase: biphenyl hydrolase-like protein as valacyclovir hydrolase.
PubMed ID: 12732646
PubMed ID: 9721218
Title: Structural characterization and chromosomal localization of the gene encoding human biphenyl hydrolase-related protein (BPHL).
PubMed ID: 9721218
PubMed ID: 15832508
Title: A novel nucleoside prodrug-activating enzyme: substrate specificity of biphenyl hydrolase-like protein.
PubMed ID: 15832508
DOI: 10.1021/mp0499757
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 18256025
Title: Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
PubMed ID: 18256025
Sequence Information:
- Length: 291
- Mass: 32543
- Checksum: 830B948492160244
- Sequence:
MVAVLGGRGV LRLRLLLSAL KPGIHVPRAG PAAAFGTSVT SAKVAVNGVQ LHYQQTGEGD HAVLLLPGML GSGETDFGPQ LKNLNKKLFT VVAWDPRGYG HSRPPDRDFP ADFFERDAKD AVDLMKALKF KKVSLLGWSD GGITALIAAA KYPSYIHKMV IWGANAYVTD EDSMIYEGIR DVSKWSERTR KPLEALYGYD YFARTCEKWV DGIRQFKHLP DGNICRHLLP RVQCPALIVH GEKDPLVPRF HADFIHKHVK GSRLHLMPEG KHNLHLRFAD EFNKLAEDFL Q
Genular Protein ID: 4284508385
Symbol: Q49AI2_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11181995
PubMed ID: 14574404
Title: The DNA sequence and analysis of human chromosome 6.
PubMed ID: 14574404
DOI: 10.1038/nature02055
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: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
Sequence Information:
- Length: 194
- Mass: 21532
- Checksum: 544E78D231E6C81B
- Sequence:
MPRNLLYSLL SSHLSPHFST SVTSAKVAVN GVQLHYQQTG EGDHAVLLLP GMLGSGETDF GPQLKNLNKK LFTVVAWDPR GYGHSRPPDR DFPADFFERD AKDAVDLMKA LKFKKVSLLG WSDGGITALI AAAKYPSYIH KMVIWGANAY VTDEDSMIYE GIRDVSKWSE RTRKPLEALY GWSLTLSPGW NAMA
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.