PARP2
Poly [ADP-ribose] polymerase 2
Also known as: ADPRTL2, ARTD2, PARP2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9UGN5
- Gene
- PARP2
- Ensembl
- ENSG00000129484
- Chromosome
- 14
- Canonical length
- 583 aa
- Protein class
- Enzymes, FDA approved drug targets, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nucleoli
OverviewNCBI Gene
This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
583 residues, UniProt reviewed canonical sequence.
>Q9UGN5|PARP2
1 MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM PVAGGKANKD
61 RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA KVGKAHVYCE GNDVYDVMLN
121 QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR WGRVGKMGQH SLVACSGNLN KAKEIFQKKF
181 LDKTKNNWED REKFEKVPGK YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE
241 LIKLICNVQA MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME
301 ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE LQSPEHPLDQ
361 HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT LLDLFEVEKD GEKEAFREDL
421 HNRMLLWHGS RMSNWVGILS HGLRIAPPEA PITGYMFGKG IYFADMSSKS ANYCFASRLK
481 NTGLLLLSEV ALGQCNELLE ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP
541 ASDTGILNPD GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLWLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PARP2 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)
- 0.32
- Highest tissue expression
- 46 nTPM
Expression across tissuesHPA
Tissue
- cerebellum: 46 nTPM
- cerebral cortex: 34 nTPM
- skeletal muscle: 30 nTPM
- basal ganglia: 26 nTPM
- bone marrow: 25 nTPM
- tongue: 25 nTPM
Single-cell type
- differentiating spermatogonia: 61 nCPM
- myonuclei: 45 nCPM
- oocytes: 41 nCPM
- erythrocyte progenitors: 36 nCPM
- cytotrophoblasts: 35 nCPM
- extravillous trophoblasts: 32 nCPM
Immune cell
- MAIT T-cell: 12 nTPM
- naive CD4 T-cell: 9 nTPM
- gdT-cell: 8.9 nTPM
- naive CD8 T-cell: 8.7 nTPM
- memory CD4 T-cell: 8.4 nTPM
- memory CD8 T-cell: 7.9 nTPM
Brain region
- cerebral cortex: 25 nTPM
- white matter: 21 nTPM
- basal ganglia: 20 nTPM
- cerebellum: 20 nTPM
- hypothalamus: 19 nTPM
- pons: 16 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)
- 0.99
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.49
- DepMap mean gene effect
- -0.08
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- base-excision repair
- decidualization
- DNA ADP-ribosylation
- DNA damage response
- DNA repair
- DNA repair-dependent chromatin remodeling
- double-strand break repair
- extrinsic apoptotic signaling pathway
- hippocampal neuron apoptotic process
- positive regulation of cell growth involved in cardiac muscle cell development
- protein auto-ADP-ribosylation
- protein poly-ADP-ribosylation
- response to oxygen-glucose deprivation
Molecular functions
- chromatin binding
- damaged DNA binding
- 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-serine ADP-ribosyltransferase activity
- nucleosome binding
- nucleotidyltransferase activity
- poly-ADP-D-ribose binding
- poly-ADP-D-ribose modification-dependent protein binding
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 PARP2 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 PARP2 as an antibody target. Whether an autoantibody or antibody against PARP2 could matter depends on whether native PARP2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PARP2 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 PARP2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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