PARP3
Protein mono-ADP-ribosyltransferase PARP3
Also known as: ADPRT3, ADPRTL3, ARTD3, hPARP-3, IRT1, pADPRT-3, PARP3_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y6F1
- Gene
- PARP3
- Ensembl
- ENSG00000041880
- Chromosome
- 3
- Canonical length
- 533 aa
- Protein class
- FDA approved drug targets, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies
OverviewNCBI Gene
The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
533 residues, UniProt reviewed canonical sequence.
>Q9Y6F1|PARP3
1 MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP TCPLSSNPGT
61 QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNR WGRVGEVGQS KINHFTRLED
121 AKKDFEKKFR EKTKNNWAER DHFVSHPGKY TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV
181 QPCSLDPATQ KLITNIFSKE MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL
241 KGPTDGGQSL EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
301 VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH RCPTLQHIWK
361 VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR IMPHSGGRVG KGIYFASENS
421 KSAGYVIGMK CGAHHVGYMF LGEVALGREH HINTDNPSLK SPPPGFDSVI ARGHTEPDPT
481 QDTELELDGQ QVVVPQGQPV PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHLLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PARP3 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)
- 0.29
- Highest tissue expression
- 34 nTPM
Expression across tissuesHPA
Tissue
- parathyroid gland: 34 nTPM
- adrenal gland: 33 nTPM
- liver: 29 nTPM
- duodenum: 27 nTPM
- small intestine: 24 nTPM
- kidney: 22 nTPM
Single-cell type
- enterocytes: 31 nCPM
- foveolar cells: 22 nCPM
- late spermatids: 21 nCPM
- adrenal cortex cells: 18 nCPM
- epididymal basal cells: 18 nCPM
- enteric stem cells: 17 nCPM
Immune cell
- memory B-cell: 6.4 nTPM
- NK-cell: 5.7 nTPM
- naive CD4 T-cell: 3.6 nTPM
- naive CD8 T-cell: 3.5 nTPM
- T-reg: 3.2 nTPM
- intermediate monocyte: 3 nTPM
Brain region
- thalamus: 19 nTPM
- midbrain: 18 nTPM
- choroid plexus: 17 nTPM
- hypothalamus: 17 nTPM
- medulla oblongata: 16 nTPM
- pons: 16 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about PARP3.
Disease | ImmuneIEDB
Conditions an epitope on PARP3 was assayed in.
- chronic lymphocytic leukemia T cell
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)
- 1.24
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.31
- DepMap mean gene effect
- -0.02
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- DNA ADP-ribosylation
- double-strand break repair
- double-strand break repair via nonhomologous end joining
- negative regulation of telomere maintenance via telomerase
- positive regulation of double-strand break repair via nonhomologous end joining
- protein auto-ADP-ribosylation
- protein localization to site of double-strand break
- regulation of mitotic spindle organization
- telomere maintenance
- negative regulation of isotype switching
Molecular functions
- catalytic activity
- NAD DNA ADP-ribosyltransferase activity
- NAD+ poly-ADP-ribosyltransferase activity
- NAD+-protein mono-ADP-ribosyltransferase activity
- NAD+-protein-aspartate ADP-ribosyltransferase activity
- NAD+-protein-glutamate ADP-ribosyltransferase activity
- NAD+-protein-lysine ADP-ribosyltransferase activity
- nucleotidyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Poly(ADP-ribose) polymerase, regulatory domain
- WGR domain
- Poly(ADP-ribose) polymerase, catalytic domain
- Poly(ADP-ribose) polymerase, regulatory domain superfamily
- WGR domain superfamily
- ADP-ribosyltransferase diphtheria toxin-like
- Poly(ADP-ribose) polymerase catalytic domain
- Poly(ADP-ribose) polymerase, regulatory domain
- WGR domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PARP3 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 PARP3 as an antibody target. Whether an autoantibody or antibody against PARP3 could matter depends on whether native PARP3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PARP3 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 PARP3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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