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Protein

Poly [ADP-ribose] polymerase 10

Gene

PARP10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May play a role in cell proliferation. May be required for the maintenance of cell cycle progression.2 Publications

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

GO - Molecular functioni

  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB
  • NAD+ ADP-ribosyltransferase activity Source: UniProtKB

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 poly-ADP-ribosylation Source: UniProtKB
  • regulation of chromatin assembly Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandNAD

Enzyme and pathway databases

ReactomeiR-HSA-197264 Nicotinamide salvaging

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 10 (EC:2.4.2.30)
Short name:
PARP-10
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 10
Short name:
ARTD10
Gene namesi
Name:PARP10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000178685.13
HGNCiHGNC:25895 PARP10
MIMi609564 gene
neXtProtiNX_Q53GL7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi888G → W: Abolishes catalytic activity; abolishes interaction with PARP14. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000178685
PharmGKBiPA134892853

Chemistry databases

ChEMBLiCHEMBL2429708

Polymorphism and mutation databases

BioMutaiPARP10
DMDMi116248563

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002524351 – 1025Poly [ADP-ribose] polymerase 10Add BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101Phosphothreonine1 Publication1
Modified residuei378PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1
Modified residuei431PhosphoserineCombined sources1
Modified residuei663PhosphoserineCombined sources1
Modified residuei916N6-acetyllysineCombined sources1
Modified residuei1011PhosphoserineCombined sources1

Post-translational modificationi

Stimulated through its phosphorylation by CDK2. Acquires CDK-dependent phosphorylation through late-G1 to S phase, and from prometaphase to cytokinesis in the nucleolar organizing regions. Phosphorylation is suppressed in growth-arrested cells.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ53GL7
MaxQBiQ53GL7
PaxDbiQ53GL7
PeptideAtlasiQ53GL7
PRIDEiQ53GL7
ProteomicsDBi62485

PTM databases

iPTMnetiQ53GL7
PhosphoSitePlusiQ53GL7

Expressioni

Tissue specificityi

Highly expressed in spleen and thymus. Intermediate levels in liver, kidney, pancreas, prostate, testis, ovary, intestine, and leukocytes. Low expression in heart, brain, placenta, lung, skeletal muscle, and colon.1 Publication

Gene expression databases

BgeeiENSG00000178685
CleanExiHS_PARP10
ExpressionAtlasiQ53GL7 baseline and differential
GenevisibleiQ53GL7 HS

Organism-specific databases

HPAiHPA028122
HPA052427

Interactioni

Subunit structurei

Interacts with MYC (PubMed:15674325). Interacts with PARP14 (PubMed:23473667).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OARD1Q9Y5303EBI-2857573,EBI-8502288

GO - Molecular functioni

  • K63-linked polyubiquitin modification-dependent protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi124320, 21 interactors
IntActiQ53GL7, 4 interactors
MINTiQ53GL7
STRINGi9606.ENSP00000325618

Chemistry databases

BindingDBiQ53GL7

Structurei

Secondary structure

11025
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Helixi24 – 32Combined sources9
Turni34 – 37Combined sources4
Beta strandi43 – 48Combined sources6
Beta strandi51 – 55Combined sources5
Helixi59 – 66Combined sources8
Beta strandi72 – 77Combined sources6
Beta strandi79 – 82Combined sources4
Beta strandi819 – 822Combined sources4
Beta strandi825 – 827Combined sources3
Helixi828 – 839Combined sources12
Helixi842 – 844Combined sources3
Turni845 – 847Combined sources3
Beta strandi848 – 856Combined sources9
Helixi859 – 875Combined sources17
Beta strandi883 – 889Combined sources7
Helixi891 – 893Combined sources3
Helixi894 – 900Combined sources7
Helixi904 – 906Combined sources3
Beta strandi916 – 923Combined sources8
Helixi924 – 927Combined sources4
Turni930 – 932Combined sources3
Beta strandi941 – 948Combined sources8
Beta strandi952 – 955Combined sources4
Beta strandi961 – 963Combined sources3
Beta strandi971 – 974Combined sources4
Beta strandi976 – 980Combined sources5
Beta strandi982 – 984Combined sources3
Beta strandi987 – 990Combined sources4
Beta strandi995 – 1006Combined sources12

3D structure databases

ProteinModelPortaliQ53GL7
SMRiQ53GL7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53GL7

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini806 – 1025PARP catalyticPROSITE-ProRule annotationAdd BLAST220

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni700 – 907Myc bindingAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi650 – 667Ubiquitin-interactingAdd BLAST18
Motifi673 – 690Ubiquitin-interactingAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi186 – 193Poly-Leu8
Compositional biasi588 – 697Glu-richAdd BLAST110

Phylogenomic databases

eggNOGiENOG410IH3S Eukaryota
ENOG411034Y LUCA
GeneTreeiENSGT00760000119084
HOVERGENiHBG068843
InParanoidiQ53GL7
KOiK15261
PhylomeDBiQ53GL7
TreeFamiTF328965

Family and domain databases

CDDicd12547 RRM1_2_PAR10, 2 hits
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034464 PAR10_RRM1_2
IPR012317 Poly(ADP-ribose)pol_cat_dom
PfamiView protein in Pfam
PF00644 PARP, 1 hit
PROSITEiView protein in PROSITE
PS51059 PARP_CATALYTIC, 1 hit

Sequencei

Sequence statusi: Complete.

Q53GL7-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:1,025
Mass (Da):109,998
Last modified:October 17, 2006 - v2
Checksum:iAC9CCFCF9B83A989
GO

Sequence cautioni

The sequence BAC11498 differs from that shown. Reason: Frameshift at position 965.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti313M → I in BAB55067 (PubMed:14702039).Curated1
Sequence conflicti518P → S in BAB55067 (PubMed:14702039).Curated1
Sequence conflicti813L → P in AAH14229 (PubMed:15489334).Curated1
Sequence conflicti922R → K in BAB55067 (PubMed:14702039).Curated1
Sequence conflicti1013D → G in BAD96634 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027859249I → V. Corresponds to variant dbSNP:rs11136344Ensembl.1
Natural variantiVAR_027860395L → P. Corresponds to variant dbSNP:rs11136343Ensembl.1
Natural variantiVAR_027861630V → 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
CCDSiCCDS34960.1
RefSeqiNP_116178.2, NM_032789.4
UniGeneiHs.348609

Genome annotation databases

EnsembliENST00000313028; ENSP00000325618; ENSG00000178685
GeneIDi84875
KEGGihsa:84875
UCSCiuc003zal.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPAR10_HUMAN
AccessioniPrimary (citable) accession number: Q53GL7
Secondary accession number(s): Q8N2I0
, Q8WV05, Q96CH7, Q96K72
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 18, 2018
This is version 123 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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