UniProtKB - Q53GL7 (PAR10_HUMAN)
Protein
Protein mono-ADP-ribosyltransferase PARP10
Gene
PARP10
Organism
Homo sapiens (Human)
Status
Functioni
ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate and aspartate residues on target proteins (PubMed:18851833, PubMed:23332125, PubMed:23474714, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:18851833). Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively regulate GSK3B kinase activity (PubMed:23332125). Involved in translesion DNA synthesis in response to DNA damage via its interaction with PCNA (PubMed:24695737).5 Publications
Catalytic activityi
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward2 Publications direction.
GO - Molecular functioni
- K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
- NAD+ ADP-ribosyltransferase activity Source: UniProtKB
- protein ADP-ribosylase activity Source: UniProtKB
- transcription corepressor activity Source: GO_Central
GO - Biological processi
- NAD biosynthesis via nicotinamide riboside salvage pathway Source: Reactome
- negative regulation of fibroblast proliferation Source: UniProtKB
- negative regulation of gene expression Source: UniProtKB
- negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
- negative regulation of protein K63-linked ubiquitination Source: UniProtKB
- negative regulation of viral genome replication Source: UniProtKB
- protein ADP-ribosylation Source: UniProtKB
- protein auto-ADP-ribosylation Source: UniProtKB
- protein mono-ADP-ribosylation Source: UniProtKB
- protein poly-ADP-ribosylation Source: UniProtKB
- regulation of chromatin assembly Source: UniProtKB
- translesion synthesis Source: UniProtKB
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | DNA damage, DNA repair |
Ligand | NAD |
Enzyme and pathway databases
PathwayCommonsi | Q53GL7 |
Reactomei | R-HSA-197264, Nicotinamide salvaging R-HSA-9683610, Maturation of nucleoprotein |
Names & Taxonomyi
Protein namesi | Recommended name: Protein mono-ADP-ribosyltransferase PARP10Curated (EC:2.4.2.-2 Publications)Alternative name(s): ADP-ribosyltransferase diphtheria toxin-like 101 Publication Short name: ARTD101 Publication Poly [ADP-ribose] polymerase 101 Publication Short name: PARP-101 Publication |
Gene namesi | Name:PARP10Imported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000178685.13 |
HGNCi | HGNC:25895, PARP10 |
MIMi | 609564, gene |
neXtProti | NX_Q53GL7 |
Subcellular locationi
Cytosol
- cytosol Source: HPA
Golgi apparatus
- Golgi apparatus Source: HPA
Nucleus
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 650 – 690 | Missing : Decreased interaction with PCNA. 1 PublicationAdd BLAST | 41 | |
Mutagenesisi | 831 – 838 | QEVVRAFY → AEVARAAA: Abolishes interaction with PCNA. 1 Publication | 8 | |
Mutagenesisi | 882 | E → A: Decreased auto-mono-ADP-ribosylation. 1 Publication | 1 | |
Mutagenesisi | 888 | G → W: Abolishes catalytic activity; abolishes interaction with PARP14. 3 Publications | 1 | |
Mutagenesisi | 980 – 982 | DCI → ACA: Strongly decreased catalytic activity. 1 Publication | 3 | |
Mutagenesisi | 985 | P → A: Strongly decreased catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 987 | I → E: Decreased catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 999 | T → A: Does not affect catalytic activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 84875 |
OpenTargetsi | ENSG00000178685 |
PharmGKBi | PA134892853 |
Miscellaneous databases
Pharosi | Q53GL7, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2429708 |
DrugCentrali | Q53GL7 |
Polymorphism and mutation databases
BioMutai | PARP10 |
DMDMi | 116248563 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000252435 | 1 – 1025 | Protein mono-ADP-ribosyltransferase PARP10Add BLAST | 1025 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 101 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 106 | ADP-ribosyl glutamic acid1 Publication | 1 | |
Modified residuei | 140 | N6-(ADP-ribosyl)lysine1 Publication | 1 | |
Modified residuei | 378 | PhosphoserineCombined sources | 1 | |
Modified residuei | 423 | PhosphoserineCombined sources | 1 | |
Modified residuei | 431 | PhosphoserineCombined sources | 1 | |
Modified residuei | 663 | PhosphoserineCombined sources | 1 | |
Modified residuei | 882 | ADP-ribosyl glutamic acid1 Publication | 1 | |
Modified residuei | 916 | N6-(ADP-ribosyl)lysine1 Publication | 1 | |
Modified residuei | 916 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1011 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Stimulated through its phosphorylation by CDK2 (PubMed:16455663). Acquires CDK-dependent phosphorylation through late-G1 to S phase, and from prometaphase to cytokinesis in the nucleolar organizing regions (PubMed:16455663). Phosphorylation is suppressed in growth-arrested cells (PubMed:16455663).1 Publication
Auto-mono-ADP-ribosylated on glutamate and lysine residues.2 Publications
Keywords - PTMi
Acetylation, ADP-ribosylation, PhosphoproteinProteomic databases
EPDi | Q53GL7 |
jPOSTi | Q53GL7 |
MassIVEi | Q53GL7 |
MaxQBi | Q53GL7 |
PaxDbi | Q53GL7 |
PeptideAtlasi | Q53GL7 |
PRIDEi | Q53GL7 |
ProteomicsDBi | 62485 |
PTM databases
iPTMneti | Q53GL7 |
PhosphoSitePlusi | Q53GL7 |
Expressioni
Tissue specificityi
Highly expressed in spleen and thymus (PubMed:15674325). Intermediate levels in liver, kidney, pancreas, prostate, testis, ovary, intestine, and leukocytes (PubMed:15674325). Low expression in heart, brain, placenta, lung, skeletal muscle, and colon (PubMed:15674325).1 Publication
Gene expression databases
Bgeei | ENSG00000178685, Expressed in tendon of biceps brachii and 202 other tissues |
ExpressionAtlasi | Q53GL7, baseline and differential |
Genevisiblei | Q53GL7, HS |
Organism-specific databases
HPAi | ENSG00000178685, Low tissue specificity |
Interactioni
Subunit structurei
Binary interactionsi
Q53GL7
With | #Exp. | IntAct |
---|---|---|
OARD1 [Q9Y530] | 3 | EBI-2857573,EBI-8502288 |
GO - Molecular functioni
- K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 124320, 27 interactors |
IntActi | Q53GL7, 8 interactors |
MINTi | Q53GL7 |
STRINGi | 9606.ENSP00000325618 |
Chemistry databases
BindingDBi | Q53GL7 |
Miscellaneous databases
RNActi | Q53GL7, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q53GL7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q53GL7 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 806 – 1025 | PARP catalyticPROSITE-ProRule annotationAdd BLAST | 220 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 700 – 907 | Myc binding1 PublicationAdd BLAST | 208 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 650 – 667 | Ubiquitin-interacting1 PublicationAdd BLAST | 18 | |
Motifi | 673 – 690 | Ubiquitin-interacting1 PublicationAdd BLAST | 18 | |
Motifi | 831 – 838 | PIP-box1 Publication | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 588 – 697 | Glu-richAdd BLAST | 110 |
Domaini
The PIP-box mediates the interaction with PCNA.1 Publication
Phylogenomic databases
eggNOGi | ENOG502R572, Eukaryota |
GeneTreei | ENSGT00940000162035 |
InParanoidi | Q53GL7 |
PhylomeDBi | Q53GL7 |
TreeFami | TF328965 |
Family and domain databases
CDDi | cd12547, RRM1_2_PAR10, 1 hit |
Gene3Di | 3.30.70.330, 2 hits |
InterProi | View protein in InterPro IPR012677, Nucleotide-bd_a/b_plait_sf IPR034464, PAR10_RRM1_2 IPR012317, Poly(ADP-ribose)pol_cat_dom |
Pfami | View protein in Pfam PF00644, PARP, 1 hit |
PROSITEi | View protein in PROSITE PS51059, PARP_CATALYTIC, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 14 potential isoforms that are computationally mapped.Show allAlign All
Q53GL7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC
60 70 80 90 100
GGVLTFREPA DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT
110 120 130 140 150
TPQRLEQHVQ ALLRASGLPV QPCCALASPR PDRALVQLPK PLSEADVRVL
160 170 180 190 200
EEQAQNLGLE GTLVSLARVP QARAVRVVGD GASVDLLLLE LYLENERRSG
210 220 230 240 250
GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE LSLVPHYDIL
260 270 280 290 300
EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE
310 320 330 340 350
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS
360 370 380 390 400
SMPMGSLEHE GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL
410 420 430 440 450
VEIAMDSPEQ EGLVGPMEIT MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM
460 470 480 490 500
EPGAMRFLQL YHEDLLAGLG DVALLPLEGP DMTGFRLCGA QASCQAAEEF
510 520 530 540 550
LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF QCVFGTERLA
560 570 580 590 600
TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA
610 620 630 640 650
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL
660 670 680 690 700
EEEAALQLAL HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD
710 720 730 740 750
GGTDGKAQLV VHSAFEQDVE ELDRALRAAL EVHVQEETVG PWRRTLPAEL
760 770 780 790 800
RARLERCHGV SVALRGDCTI LRGFGAHPAR AARHLVALLA GPWDQSLAFP
810 820 830 840 850
LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT LDAARSSIRV
860 870 880 890 900
VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH
910 920 930 940 950
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT
960 970 980 990 1000
GDYGQGRRGL RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH
1010 1020
LITCEHVPRA SPDDPSGLPG RSPDT
Computationally mapped potential isoform sequencesi
There are 14 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE9PK67 | E9PK67_HUMAN | Poly [ADP-ribose] polymerase | PARP10 | 1,016 | Annotation score: | ||
E9PNI7 | E9PNI7_HUMAN | Poly [ADP-ribose] polymerase | PARP10 | 1,037 | Annotation score: | ||
E9PJI2 | E9PJI2_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 172 | Annotation score: | ||
E9PPV8 | E9PPV8_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 178 | Annotation score: | ||
E9PIK9 | E9PIK9_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 146 | Annotation score: | ||
E9PQQ6 | E9PQQ6_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 106 | Annotation score: | ||
F8W8G7 | F8W8G7_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 339 | Annotation score: | ||
E9PIA6 | E9PIA6_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 144 | Annotation score: | ||
E9PM86 | E9PM86_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 128 | Annotation score: | ||
E9PPE7 | E9PPE7_HUMAN | Protein mono-ADP-ribosyltransferase... | PARP10 | 764 | Annotation score: | ||
There are more potential isoformsShow all |
Sequence cautioni
The sequence BAC11498 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 313 | M → I in BAB55067 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 518 | P → S in BAB55067 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 813 | L → P in AAH14229 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 922 | R → K in BAB55067 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 1013 | D → G in BAD96634 (Ref. 2) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_027859 | 249 | I → V. Corresponds to variant dbSNP:rs11136344Ensembl. | 1 | |
Natural variantiVAR_027860 | 395 | L → P. Corresponds to variant dbSNP:rs11136343Ensembl. | 1 | |
Natural variantiVAR_027861 | 630 | V → A1 PublicationCorresponds to variant dbSNP:rs11544989Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK027370 mRNA Translation: BAB55067.1 AK075250 mRNA Translation: BAC11498.1 Sequence problems. AK222914 mRNA Translation: BAD96634.1 BC014229 mRNA Translation: AAH14229.2 BC019030 mRNA Translation: AAH19030.2 |
CCDSi | CCDS34960.1 |
RefSeqi | NP_116178.2, NM_032789.4 |
Genome annotation databases
Ensembli | ENST00000313028; ENSP00000325618; ENSG00000178685 |
GeneIDi | 84875 |
KEGGi | hsa:84875 |
UCSCi | uc003zal.5, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK027370 mRNA Translation: BAB55067.1 AK075250 mRNA Translation: BAC11498.1 Sequence problems. AK222914 mRNA Translation: BAD96634.1 BC014229 mRNA Translation: AAH14229.2 BC019030 mRNA Translation: AAH19030.2 |
CCDSi | CCDS34960.1 |
RefSeqi | NP_116178.2, NM_032789.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2DHX | NMR | - | A | 10-100 | [»] | |
3HKV | X-ray | 2.10 | A/B | 809-1017 | [»] | |
5LX6 | X-ray | 1.25 | A/B | 819-1007 | [»] | |
6FXI | X-ray | 2.60 | A/B | 819-1007 | [»] | |
SMRi | Q53GL7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 124320, 27 interactors |
IntActi | Q53GL7, 8 interactors |
MINTi | Q53GL7 |
STRINGi | 9606.ENSP00000325618 |
Chemistry databases
BindingDBi | Q53GL7 |
ChEMBLi | CHEMBL2429708 |
DrugCentrali | Q53GL7 |
PTM databases
iPTMneti | Q53GL7 |
PhosphoSitePlusi | Q53GL7 |
Polymorphism and mutation databases
BioMutai | PARP10 |
DMDMi | 116248563 |
Proteomic databases
EPDi | Q53GL7 |
jPOSTi | Q53GL7 |
MassIVEi | Q53GL7 |
MaxQBi | Q53GL7 |
PaxDbi | Q53GL7 |
PeptideAtlasi | Q53GL7 |
PRIDEi | Q53GL7 |
ProteomicsDBi | 62485 |
Protocols and materials databases
Antibodypediai | 28206, 100 antibodies |
Genome annotation databases
Ensembli | ENST00000313028; ENSP00000325618; ENSG00000178685 |
GeneIDi | 84875 |
KEGGi | hsa:84875 |
UCSCi | uc003zal.5, human |
Organism-specific databases
CTDi | 84875 |
DisGeNETi | 84875 |
EuPathDBi | HostDB:ENSG00000178685.13 |
GeneCardsi | PARP10 |
HGNCi | HGNC:25895, PARP10 |
HPAi | ENSG00000178685, Low tissue specificity |
MIMi | 609564, gene |
neXtProti | NX_Q53GL7 |
OpenTargetsi | ENSG00000178685 |
PharmGKBi | PA134892853 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502R572, Eukaryota |
GeneTreei | ENSGT00940000162035 |
InParanoidi | Q53GL7 |
PhylomeDBi | Q53GL7 |
TreeFami | TF328965 |
Enzyme and pathway databases
PathwayCommonsi | Q53GL7 |
Reactomei | R-HSA-197264, Nicotinamide salvaging R-HSA-9683610, Maturation of nucleoprotein |
Miscellaneous databases
BioGRID-ORCSi | 84875, 19 hits in 848 CRISPR screens |
ChiTaRSi | PARP10, human |
EvolutionaryTracei | Q53GL7 |
GeneWikii | PARP10 |
GenomeRNAii | 84875 |
Pharosi | Q53GL7, Tchem |
PROi | PR:Q53GL7 |
RNActi | Q53GL7, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000178685, Expressed in tendon of biceps brachii and 202 other tissues |
ExpressionAtlasi | Q53GL7, baseline and differential |
Genevisiblei | Q53GL7, HS |
Family and domain databases
CDDi | cd12547, RRM1_2_PAR10, 1 hit |
Gene3Di | 3.30.70.330, 2 hits |
InterProi | View protein in InterPro IPR012677, Nucleotide-bd_a/b_plait_sf IPR034464, PAR10_RRM1_2 IPR012317, Poly(ADP-ribose)pol_cat_dom |
Pfami | View protein in Pfam PF00644, PARP, 1 hit |
PROSITEi | View protein in PROSITE PS51059, PARP_CATALYTIC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PAR10_HUMAN | |
Accessioni | Q53GL7Primary (citable) accession number: Q53GL7 Secondary accession number(s): Q8N2I0 Q96K72 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 17, 2006 |
Last sequence update: | October 17, 2006 | |
Last modified: | December 2, 2020 | |
This is version 141 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations