PARP3 poly(ADP-ribose) polymerase family member 3 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PARP3provided by HGNC
Official Full Name: poly(ADP-ribose) polymerase family member 3provided by HGNC
Primary source: HGNC:HGNC:273
See related: Ensembl:ENSG00000041880 MIM:607726; AllianceGenome:HGNC:273
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: IRT1; ARTD3; ADPRT3; ADPRTL2; ADPRTL3; PADPRT-3
Summary: 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]
Expression: Ubiquitous expression in duodenum (RPKM 12.4), small intestine (RPKM 11.6) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 3p21.2

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	3	NC_000003.12 (51942363..51948867)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	3	NC_060927.1 (51975282..51981786)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	3	NC_000003.11 (51976379..51982883)

Chromosome 3 - NC_000003.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Progress and outlook in studying the substrate specificities of PARPs and related enzymes.
Title: Progress and outlook in studying the substrate specificities of PARPs and related enzymes.
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.
Title: PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.
gapped DNA that was ADP-ribosylated by PARP3 could be ligated to double-stranded DNA by DNA ligases. Moreover, this ADP-ribosylated DNA could serve as a primed DNA substrate for PAR chain elongation by the purified proteins PARP1 and PARP2 as well as by cell-free extracts.
Title: Dna is a New Target of Parp3.
The integral roles of PARP3 in DNA damage repair.
Title: The Development of a Biotinylated NAD(+)-Applied Human Poly(ADP-Ribose) Polymerase 3 (PARP3) Enzymatic Assay.
PARP3 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5'- and 3'-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks.
Title: Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation.
Our results indicated this approach with PARP3 inhibitors and vinorelbine is unique and promising for breast cancer patients with metastases. This combination could significantly increase the survival of breast cancer patients with metastases
Title: PARP3 inhibitors ME0328 and olaparib potentiate vinorelbine sensitization in breast cancer cell lines.
These data identify PARP3 as a molecular sensor of nicked nucleosomes.
Title: PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2B(Glu2).
PARP3 controls of TGFbeta-induced epithelial mesenchymal transformation and acquisition of stem-like cell features by stimulation transglutaminase 2/SNAI1 signaling.
Title: PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis.
Data indicate that PARP3, a DNA damage-activated ADP-ribosyltransferase, can mono-ADP-ribosylate double-stranded DNA ends.
Title: Reversible mono-ADP-ribosylation of DNA breaks.
In a process of single-strand DNA repair, PARP3 mono-ADP-ribosylates nucleosomal histone H2B.
Title: Nick Your DNA, Mark Your Chromatin.

Submit: New GeneRIF Correction See all GeneRIFs (22)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH45748 (e-PCR)
- UniSTS:41923

SGC30878 (e-PCR)
- UniSTS:25342

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables NAD DNA ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD+-histone H2BE18 glutamate ADP-ribosyltransferase activity	IEA Inferred from Electronic Annotation more info
enables NAD+-histone H2BE2 glutamate ADP-ribosyltransferase activity	IEA Inferred from Electronic Annotation more info
enables NAD+-histone H2BE35 glutamate ADP-ribosyltransferase activity	IEA Inferred from Electronic Annotation more info
enables NAD+-protein ADP-ribosyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables NAD+-protein ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD+-protein poly-ADP-ribosyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables NAD+-protein poly-ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD+-protein-aspartate ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD+-protein-glutamate ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD+-protein-lysine ADP-ribosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables catalytic activity	TAS Traceable Author Statement more info
enables nucleotidyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA ADP-ribosylation	IDA Inferred from Direct Assay more info	PubMed
involved_in double-strand break repair	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within double-strand break repair	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within double-strand break repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of isotype switching	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of telomere maintenance via telomerase	TAS Traceable Author Statement more info	PubMed
acts_upstream_of_or_within positive regulation of DNA ligation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of double-strand break repair via nonhomologous end joining	IDA Inferred from Direct Assay more info	PubMed
involved_in protein auto-ADP-ribosylation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within protein localization to site of double-strand break	IMP Inferred from Mutant Phenotype more info	PubMed
NOT involved_in protein poly-ADP-ribosylation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within regulation of mitotic spindle organization	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within telomere maintenance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in centriole	IEA Inferred from Electronic Annotation more info
located_in centrosome	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in intercellular bridge	IDA Inferred from Direct Assay more info
located_in nuclear body	IDA Inferred from Direct Assay more info
is_active_in nucleolus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
is_active_in site of double-strand break	IBA Inferred from Biological aspect of Ancestor more info
located_in site of double-strand break	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: protein mono-ADP-ribosyltransferase PARP3

Names: ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)-like 2; ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)-like 3; ADP-ribosyltransferase diphtheria toxin-like 3; ADPRT-3; DNA ADP-ribosyltransferase PARP3; NAD(+) ADP-ribosyltransferase 3; NAD+ ADP-ribosyltransferase 3; poly [ADP-ribose] polymerase 3; poly(ADP-ribose) synthetase-3; poly[ADP-ribose] synthase 3; poly[ADP-ribose] synthetase 3

NP_001003931.4

EC 2.4.2.30

NP_001357168.1

EC 2.4.2.30

NP_001357169.1

EC 2.4.2.30

NP_005476.4

EC 2.4.2.30

XP_047303043.1

EC 2.4.2.30

XP_054200797.1

EC 2.4.2.30

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001003931.4 → NP_001003931.4 protein mono-ADP-ribosyltransferase PARP3 isoform a

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes isoform b.

Source sequence(s)

CA309713, CA394313, Y16836

Consensus CDS

CCDS43097.1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

UniProtKB/TrEMBL

Q59HF6

Related

ENSP00000381740.4, ENST00000398755.8

Conserved Domains (2) summary

cd08002
Location:58 → 157

WGR_PARP3_like; WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins

cd01437
Location:182 → 532

parp_like; Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a ...
NM_001370239.1 → NP_001357168.1 protein mono-ADP-ribosyltransferase PARP3 isoform a

Status: REVIEWED

Source sequence(s)

AC115284, KF459622

Consensus CDS

CCDS43097.1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

UniProtKB/TrEMBL

Q59HF6

Related

ENSP00000395951.2, ENST00000417220.6

Conserved Domains (2) summary

cd08002
Location:58 → 157

WGR_PARP3_like; WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins

cd01437
Location:182 → 532

parp_like; Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a ...
NM_001370240.1 → NP_001357169.1 protein mono-ADP-ribosyltransferase PARP3 isoform a

Status: REVIEWED

Source sequence(s)

AC115284, KF459622

Consensus CDS

CCDS43097.1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

UniProtKB/TrEMBL

Q59HF6

Related

ENSP00000417396.2, ENST00000471971.6

Conserved Domains (2) summary

cd08002
Location:58 → 157

WGR_PARP3_like; WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins

cd01437
Location:182 → 532

parp_like; Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a ...
NM_005485.6 → NP_005476.4 protein mono-ADP-ribosyltransferase PARP3 isoform a

See identical proteins and their annotated locations for NP_005476.4

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and uses a downstream translational start codon, compared to variant 1. The resulting isoform (b) is shorter at the N-terminus, compared to isoform a.

Source sequence(s)

BI554046, CA309713, CA394313, Y16836

Consensus CDS

CCDS43097.1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

UniProtKB/TrEMBL

Q59HF6

Related

ENSP00000401511.1, ENST00000431474.6

Conserved Domains (2) summary

cd08002
Location:58 → 157

WGR_PARP3_like; WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins

cd01437
Location:182 → 532

parp_like; Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000003.12 Reference GRCh38.p14 Primary Assembly

Range

51942363..51948867

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047447087.1 → XP_047303043.1 protein mono-ADP-ribosyltransferase PARP3 isoform X1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

Alternate T2T-CHM13v2.0

Genomic

NC_060927.1 Alternate T2T-CHM13v2.0

Range

51975282..51981786

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054344822.1 → XP_054200797.1 protein mono-ADP-ribosyltransferase PARP3 isoform X1

UniProtKB/Swiss-Prot

Q8NER9, Q96CG2, Q9UG81, Q9Y6F1

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_001003935.2: Suppressed sequence

Description

NM_001003935.2: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript and the protein.