PARG
Poly(ADP-ribose) glycohydrolase
Also known as: PARG_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q86W56
- Gene
- PARG
- Ensembl
- ENSG00000227345
- Chromosome
- 10
- Canonical length
- 976 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies,Cytosol
OverviewNCBI Gene
Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2015]
Canonical amino-acid sequenceUniProt
976 residues, UniProt reviewed canonical sequence.
>Q86W56|PARG
1 MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG
61 RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ
121 HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE
181 QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS
241 CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP
301 ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK
361 GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA
421 EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH
481 TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ
541 TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI
601 ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN
661 FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV
721 TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC
781 LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK
841 MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF
901 TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV
961 ESCAETADHS GQRTGTLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PARG can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.45
- Highest tissue expression
- 12 nTPM
Expression across tissuesHPA
Tissue
- kidney: 12 nTPM
- skeletal muscle: 11 nTPM
- lymph node: 8.5 nTPM
- thymus: 8.5 nTPM
- tonsil: 8.5 nTPM
- parathyroid gland: 8.4 nTPM
Single-cell type
- cardiomyocytes: 417 nCPM
- epicardial cells: 364 nCPM
- myonuclei: 188 nCPM
- adipocytes: 158 nCPM
- proximal tubule cells: 138 nCPM
- distal convoluted tubule cells: 133 nCPM
Immune cell
- basophil: 6.1 nTPM
- NK-cell: 3.9 nTPM
- naive CD4 T-cell: 3.7 nTPM
- naive CD8 T-cell: 3.5 nTPM
- non-classical monocyte: 3.5 nTPM
- MAIT T-cell: 3.2 nTPM
Brain region
- cerebellum: 21 nTPM
- cerebral cortex: 14 nTPM
- hypothalamus: 14 nTPM
- white matter: 14 nTPM
- pons: 14 nTPM
- thalamus: 13 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.42
- gnomAD pLI
- 0.39
- gnomAD missense Z
- 2.11
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- ATP generation from poly-ADP-D-ribose
- base-excision repair, gap-filling
- carbohydrate metabolic process
- nucleotide-sugar metabolic process
- regulation of DNA repair
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Poly(ADP-ribose) glycohydrolase
- Poly (ADP-ribose) glycohydrolase (PARG), catalytic domain
- Poly (ADP-ribose) glycohydrolase, helical domain
- Poly (ADP-ribose) glycohydrolase (PARG), Macro domain fold
- Poly (ADP-ribose) glycohydrolase (PARG), helical domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PARG in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PARG as an antibody target. Whether an autoantibody or antibody against PARG could matter depends on whether native PARG is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PARG is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PARG as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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