PARP1

Functionⁱ

Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair.UniRule annotation

Catalytic activityⁱ

L-aspartyl-[protein]
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Search chemical reactions in Rhea for this molecule.
+
NAD⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
4-O-(ADP-D-ribosyl)-L-aspartyl-[protein]
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Search chemical reactions in Rhea for this molecule.
+
nicotinamide
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
UniRule annotation
Automatic assertion according to rulesⁱ
- PIRNR:PIRNR000489
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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L-aspartyl-[protein]
L-aspartate residue
zoom
+
NAD⁺
zoom
=
4-O-(ADP-D-ribosyl)-L-aspartyl-[protein]
4-O-(ADP-D-ribosyl)-L-aspartyl residue
zoom
+
nicotinamide
zoom
L-glutamyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
NAD⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
5-O-(ADP-D-ribosyl)-L-glutamyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
nicotinamide
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
UniRule annotation
Automatic assertion according to rulesⁱ
- PIRNR:PIRNR000489
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-glutamyl-[protein]
L-glutamate residue
zoom
+
NAD⁺
zoom
=
5-O-(ADP-D-ribosyl)-L-glutamyl-[protein]
5-O-(ADP-D-ribosyl)-L-glutamate residue
zoom
+
nicotinamide
zoom

NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
UniRule annotation
Automatic assertion according to rulesⁱ
- PIRNR:PIRNR000489
ARBA annotation
Automatic assertion according to rulesⁱ
- ARBA:ARBA00001645
EC:2.4.2.30

GO - Molecular functionⁱ

DNA binding Source: UniProtKB-UniRule
estrogen receptor binding Source: Ensembl
histone deacetylase binding Source: Ensembl
NAD+ ADP-ribosyltransferase activity Source: UniProtKB-UniRule
NAD binding Source: UniProtKB-UniRule
R-SMAD binding Source: Ensembl
zinc ion binding Source: InterPro

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to amyloid-beta Source: Ensembl
cellular response to zinc ion Source: Ensembl
DNA damage response, detection of DNA damage Source: Ensembl
DNA repair Source: UniProtKB-KW
positive regulation of cardiac muscle hypertrophy Source: Ensembl
positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
positive regulation of mitochondrial depolarization Source: Ensembl
positive regulation of myofibroblast differentiation Source: Ensembl
positive regulation of neuron death Source: Ensembl
positive regulation of protein localization to nucleus Source: Ensembl
positive regulation of SMAD protein signal transduction Source: Ensembl
positive regulation of transcription by RNA polymerase II Source: Ensembl
positive regulation of transcription regulatory region DNA binding Source: Ensembl
protein autoprocessing Source: Ensembl
protein poly-ADP-ribosylation Source: Ensembl
regulation of DNA methylation Source: Ensembl
regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: Ensembl
regulation of SMAD protein complex assembly Source: Ensembl
response to aldosterone Source: Ensembl
response to gamma radiation Source: Ensembl
signal transduction involved in regulation of gene expression Source: Ensembl
transforming growth factor beta receptor signaling pathway Source: Ensembl

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-bindingUniRule annotationARBA annotation, GlycosyltransferaseUniRule annotationARBA annotation, Transferase
Biological process	DNA damage, DNA repairARBA annotation
Ligand	Metal-binding, NADUniRule annotationARBA annotation, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Poly [ADP-ribose] polymeraseUniRule annotation (EC:2.4.2.30UniRule annotation)
Gene namesⁱ	Name:PARP1Imported ORF Names:hCG_14746Imported
Organismⁱ	Homo sapiens (Human)Imported
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000143799.12

EuPathDBⁱ

HostDB:ENSG00000143799.12

Keywords - Cellular componentⁱ

ChromosomeUniRule annotation, NucleusUniRule annotationARBA annotation

PTM / Processingⁱ

Keywords - PTMⁱ

ADP-ribosylationARBA annotation

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000143799, Expressed in ventricular zone and 246 other tissues
ExpressionAtlasⁱ	A0A024R3T8, baseline and differential

Interactionⁱ

GO - Molecular functionⁱ

estrogen receptor binding Source: Ensembl
histone deacetylase binding Source: Ensembl
R-SMAD binding Source: Ensembl

Complete GO annotation on QuickGO ...

Structureⁱ

3D structure databases

SMRⁱ	A0A024R3T8
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	9 – 93	PARP-typeInterPro annotationAdd BLAST	85
Domainⁱ	113 – 203	PARP-typeInterPro annotationAdd BLAST	91
Domainⁱ	385 – 461	BRCTInterPro annotationAdd BLAST	77
Domainⁱ	662 – 779	PARP alpha-helicalInterPro annotationAdd BLAST	118
Domainⁱ	788 – 1014	PARP catalyticInterPro annotationAdd BLAST	227

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	198 – 233	DisorderedSequence analysisAdd BLAST		36
Regionⁱ	361 – 385	DisorderedSequence analysisAdd BLAST		25

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	429 – 456	Sequence analysisAdd BLAST		28

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	366 – 385	PolarSequence analysisAdd BLAST		20

Keywords - Domainⁱ

Coiled coilSequence analysis, RepeatARBA annotation, Zinc-fingerARBA annotation

Phylogenomic databases

HOGENOMⁱ	CLU_004841_0_0_1
KEGG Orthology (KO) More...KOⁱ	K24070
OMAⁱ	AISDKCT
Database of Orthologous Groups More...OrthoDBⁱ	909382at2759
PhylomeDBⁱ	A0A024R3T8

Family and domain databases

Gene3Dⁱ	1.20.142.10, 1 hit 2.20.140.10, 1 hit 2.20.25.630, 1 hit 3.30.1740.10, 2 hits 3.40.50.10190, 1 hit
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR012982, PADR1 IPR038650, PADR1_dom_sf IPR008288, PARP IPR012317, Poly(ADP-ribose)pol_cat_dom IPR004102, Poly(ADP-ribose)pol_reg_dom IPR036616, Poly(ADP-ribose)pol_reg_dom_sf IPR036930, WGR_dom_sf IPR008893, WGR_domain IPR001510, Znf_PARP IPR036957, Znf_PARP_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00533, BRCT, 1 hit PF08063, PADR1, 1 hit PF00644, PARP, 1 hit PF02877, PARP_reg, 1 hit PF05406, WGR, 1 hit PF00645, zf-PARP, 2 hits
PIRSFⁱ	PIRSF000489, NAD_ADPRT, 1 hit
SMARTⁱ	View protein in SMART SM00292, BRCT, 1 hit SM01335, PADR1, 1 hit SM00773, WGR, 1 hit SM01336, zf-PARP, 2 hits
SUPFAMⁱ	SSF142921, SSF142921, 1 hit SSF47587, SSF47587, 1 hit SSF52113, SSF52113, 1 hit
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 1 hit PS51060, PARP_ALPHA_HD, 1 hit PS51059, PARP_CATALYTIC, 1 hit PS00347, PARP_ZN_FINGER_1, 1 hit PS50064, PARP_ZN_FINGER_2, 2 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

A0A024R3T8-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH 
        60         70         80         90        100
WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD 
       110        120        130        140        150
GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ 
       160        170        180        190        200
LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP 
       210        220        230        240        250
GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD 
       260        270        280        290        300
ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG 
       310        320        330        340        350
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV 
       360        370        380        390        400
KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK 
       410        420        430        440        450
LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN 
       460        470        480        490        500
IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG 
       510        520        530        540        550
AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG 
       560        570        580        590        600
KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK 
       610        620        630        640        650
LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE 
       660        670        680        690        700
AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK 
       710        720        730        740        750
LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP 
       760        770        780        790        800
LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD 
       810        820        830        840        850
IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP 
       860        870        880        890        900
FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 
       910        920        930        940        950
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG 
       960        970        980        990       1000
LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK 
      1010 
YLLKLKFNFK TSLW

Length:1,014

Mass (Da):113,084

Last modified:July 9, 2014 - v1

Checksum:ⁱ6A5FC01EB91C046B

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH471098 Genomic DNA Translation: EAW69784.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001609.2, NM_001618.3

Genome annotation databases

GeneIDⁱ	142
KEGGⁱ	hsa:142

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
A0A024R3T8	Poly [ADP-ribose] polymerase 1	)	HUMAN		1014	UniRef100_P09874
+4

Protein	Similar proteins		Species	Score	Length	Source
A0A024R3T8	Poly [ADP-ribose] polymerase 1	)	HUMAN		1014	UniRef90_P09874
Poly [ADP-ribose] polymerase		PANTR		1049
Poly [ADP-ribose] polymerase		PANPA		1014
Poly [ADP-ribose] polymerase		GORGO		1014
Poly [ADP-ribose] polymerase		HUMAN		1014
+8

Protein	Similar proteins		Species	Score	Length	Source
A0A024R3T8	Poly [ADP-ribose] polymerase 1	)	HUMAN		1014	UniRef50_P09874
Poly [ADP-ribose] polymerase 1 (Fragment)		XENLA		998
Poly [ADP-ribose] polymerase		PANTR		1049
Poly [ADP-ribose] polymerase		GORGO		1014
Poly [ADP-ribose] polymerase		PANPA		1014
+223

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH471098 Genomic DNA Translation: EAW69784.1
RefSeqⁱ	NP_001609.2, NM_001618.3

3D structure databases

SMRⁱ	A0A024R3T8
ModBaseⁱ	Search...

Protocols and materials databases

Antibodypediaⁱ	3545, 1827 antibodies

Antibodypediaⁱ

3545, 1827 antibodies

Genome annotation databases

GeneIDⁱ	142
KEGGⁱ	hsa:142

Organism-specific databases

CTDⁱ	142
EuPathDBⁱ	HostDB:ENSG00000143799.12

Phylogenomic databases

HOGENOMⁱ	CLU_004841_0_0_1
KOⁱ	K24070
OMAⁱ	AISDKCT
OrthoDBⁱ	909382at2759
PhylomeDBⁱ	A0A024R3T8

Miscellaneous databases

BioGRID-ORCSⁱ	142, 10 hits in 876 CRISPR screens
ChiTaRSⁱ	PARP1, human
GenomeRNAiⁱ	142

Gene expression databases

Bgeeⁱ	ENSG00000143799, Expressed in ventricular zone and 246 other tissues
ExpressionAtlasⁱ	A0A024R3T8, baseline and differential

Family and domain databases

Gene3Dⁱ	1.20.142.10, 1 hit 2.20.140.10, 1 hit 2.20.25.630, 1 hit 3.30.1740.10, 2 hits 3.40.50.10190, 1 hit
InterProⁱ	View protein in InterPro IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR012982, PADR1 IPR038650, PADR1_dom_sf IPR008288, PARP IPR012317, Poly(ADP-ribose)pol_cat_dom IPR004102, Poly(ADP-ribose)pol_reg_dom IPR036616, Poly(ADP-ribose)pol_reg_dom_sf IPR036930, WGR_dom_sf IPR008893, WGR_domain IPR001510, Znf_PARP IPR036957, Znf_PARP_sf
Pfamⁱ	View protein in Pfam PF00533, BRCT, 1 hit PF08063, PADR1, 1 hit PF00644, PARP, 1 hit PF02877, PARP_reg, 1 hit PF05406, WGR, 1 hit PF00645, zf-PARP, 2 hits
PIRSFⁱ	PIRSF000489, NAD_ADPRT, 1 hit
SMARTⁱ	View protein in SMART SM00292, BRCT, 1 hit SM01335, PADR1, 1 hit SM00773, WGR, 1 hit SM01336, zf-PARP, 2 hits
SUPFAMⁱ	SSF142921, SSF142921, 1 hit SSF47587, SSF47587, 1 hit SSF52113, SSF52113, 1 hit
PROSITEⁱ	View protein in PROSITE PS50172, BRCT, 1 hit PS51060, PARP_ALPHA_HD, 1 hit PS51059, PARP_CATALYTIC, 1 hit PS00347, PARP_ZN_FINGER_1, 1 hit PS50064, PARP_ZN_FINGER_2, 2 hits
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	A0A024R3T8_HUMAN
Accessionⁱ	A0A024R3T8Primary (citable) accession number: A0A024R3T8
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	July 9, 2014
	Last sequence update:	July 9, 2014
	Last modified:	October 7, 2020
	This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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UniProtKB - A0A024R3T8 (A0A024R3T8_HUMAN)

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Poly [ADP-ribose] polymerase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Keywords - PTMi

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Coiled coil

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ