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Q53GL7

- PAR10_HUMAN

UniProt

Q53GL7 - PAR10_HUMAN

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Protein

Poly [ADP-ribose] polymerase 10

Gene

PARP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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

  1. K63-linked polyubiquitin binding Source: UniProt
  2. NAD+ ADP-ribosyltransferase activity Source: UniProt

GO - Biological processi

  1. negative regulation of fibroblast proliferation Source: UniProtKB
  2. negative regulation of gene expression Source: UniProt
  3. negative regulation of NF-kappaB transcription factor activity Source: UniProt
  4. negative regulation of protein import into nucleus, translocation Source: UniProt
  5. negative regulation of protein K63-linked ubiquitination Source: UniProt
  6. negative regulation of viral genome replication Source: UniProt
  7. protein ADP-ribosylation Source: UniProt
  8. protein auto-ADP-ribosylation Source: UniProt
  9. protein poly-ADP-ribosylation Source: UniProtKB
  10. regulation of chromatin assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

NAD

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
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:25895. PARP10.

Subcellular locationi

Nucleusnucleolus 1 Publication. Cytoplasm 1 Publication
Note: Shuttles between the nuclear and cytoplasmic compartment. A subpopulation concentrates in the nucleolus during late G1/S phase.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. Golgi apparatus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134892853.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Poly [ADP-ribose] polymerase 10PRO_0000252435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011Phosphothreonine1 Publication
Modified residuei916 – 9161N6-acetyllysine1 Publication

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

MaxQBiQ53GL7.
PaxDbiQ53GL7.
PRIDEiQ53GL7.

PTM databases

PhosphoSiteiQ53GL7.

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

BgeeiQ53GL7.
CleanExiHS_PARP10.
ExpressionAtlasiQ53GL7. baseline and differential.
GenevestigatoriQ53GL7.

Organism-specific databases

HPAiHPA028122.

Interactioni

Subunit structurei

Interacts with MYC.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi124320. 9 interactions.
IntActiQ53GL7. 4 interactions.
MINTiMINT-8408778.
STRINGi9606.ENSP00000325618.

Structurei

Secondary structure

1
1025
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176
Helixi24 – 329
Turni34 – 374
Beta strandi43 – 486
Beta strandi51 – 555
Helixi59 – 668
Beta strandi72 – 776
Beta strandi79 – 824
Beta strandi820 – 8223
Beta strandi825 – 8273
Helixi828 – 83912
Helixi842 – 8465
Beta strandi848 – 8569
Helixi859 – 87517
Beta strandi881 – 8899
Helixi891 – 8933
Helixi894 – 9007
Turni904 – 9063
Beta strandi916 – 9238
Helixi924 – 9274
Turni930 – 9323
Beta strandi939 – 94911
Beta strandi952 – 9554
Beta strandi961 – 9633
Beta strandi971 – 9744
Beta strandi976 – 9805
Beta strandi982 – 9843
Beta strandi987 – 9904
Beta strandi995 – 100612

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DHXNMR-A10-100[»]
3HKVX-ray2.10A/B809-1017[»]
ProteinModelPortaliQ53GL7.
SMRiQ53GL7. Positions 11-101, 817-1008.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53GL7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini806 – 1025220PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni700 – 907208Myc bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi650 – 66718Ubiquitin-interactingAdd
BLAST
Motifi673 – 69018Ubiquitin-interactingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 1938Poly-Leu
Compositional biasi588 – 697110Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG42948.
GeneTreeiENSGT00760000119084.
HOVERGENiHBG068843.
InParanoidiQ53GL7.
KOiK15261.
PhylomeDBiQ53GL7.
TreeFamiTF328965.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
[Graphical view]
SMARTiSM00726. UIM. 3 hits.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

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 BAC11498.1 differs from that shown. Reason: Frameshift at position 965.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131M → I in BAB55067. (PubMed:14702039)Curated
Sequence conflicti518 – 5181P → S in BAB55067. (PubMed:14702039)Curated
Sequence conflicti813 – 8131L → P in AAH14229. (PubMed:15489334)Curated
Sequence conflicti922 – 9221R → K in BAB55067. (PubMed:14702039)Curated
Sequence conflicti1013 – 10131D → G in BAD96634. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti249 – 2491I → V.
Corresponds to variant rs11136344 [ dbSNP | Ensembl ].
VAR_027859
Natural varianti395 – 3951L → P.
Corresponds to variant rs11136343 [ dbSNP | Ensembl ].
VAR_027860
Natural varianti630 – 6301V → A.1 Publication
Corresponds to variant rs11544989 [ dbSNP | Ensembl ].
VAR_027861

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_032789.3.
UniGeneiHs.348609.

Genome annotation databases

EnsembliENST00000313028; ENSP00000325618; ENSG00000178685.
GeneIDi84875.
KEGGihsa:84875.
UCSCiuc003zal.4. human.

Polymorphism databases

DMDMi116248563.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_032789.3.
UniGenei Hs.348609.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DHX NMR - A 10-100 [» ]
3HKV X-ray 2.10 A/B 809-1017 [» ]
ProteinModelPortali Q53GL7.
SMRi Q53GL7. Positions 11-101, 817-1008.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124320. 9 interactions.
IntActi Q53GL7. 4 interactions.
MINTi MINT-8408778.
STRINGi 9606.ENSP00000325618.

Chemistry

ChEMBLi CHEMBL2429708.

PTM databases

PhosphoSitei Q53GL7.

Polymorphism databases

DMDMi 116248563.

Proteomic databases

MaxQBi Q53GL7.
PaxDbi Q53GL7.
PRIDEi Q53GL7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313028 ; ENSP00000325618 ; ENSG00000178685 .
GeneIDi 84875.
KEGGi hsa:84875.
UCSCi uc003zal.4. human.

Organism-specific databases

CTDi 84875.
GeneCardsi GC08M145051.
H-InvDB HIX0201285.
HGNCi HGNC:25895. PARP10.
HPAi HPA028122.
MIMi 609564. gene.
neXtProti NX_Q53GL7.
PharmGKBi PA134892853.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42948.
GeneTreei ENSGT00760000119084.
HOVERGENi HBG068843.
InParanoidi Q53GL7.
KOi K15261.
PhylomeDBi Q53GL7.
TreeFami TF328965.

Miscellaneous databases

EvolutionaryTracei Q53GL7.
GeneWikii PARP10.
GenomeRNAii 84875.
NextBioi 75175.
PROi Q53GL7.
SOURCEi Search...

Gene expression databases

Bgeei Q53GL7.
CleanExi HS_PARP10.
ExpressionAtlasi Q53GL7. baseline and differential.
Genevestigatori Q53GL7.

Family and domain databases

Gene3Di 3.90.228.10. 1 hit.
InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
Pfami PF00644. PARP. 1 hit.
[Graphical view ]
SMARTi SM00726. UIM. 3 hits.
[Graphical view ]
PROSITEi PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-630.
    Tissue: Mammary gland and Thyroid.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1025.
    Tissue: Skin and Uterus.
  4. Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MYC.
  5. "CDK-dependent activation of poly(ADP-ribose) polymerase member 10 (PARP10)."
    Chou H.Y., Chou H.T., Lee S.C.
    J. Biol. Chem. 281:15201-15207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-101.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-916, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
    Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
    Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  8. "Solution structure of the RRM domain in the human poly (ADP-ribose) polymerase family, member 10 variant."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 7-101.
  9. "Human poly(ADP-ribose) polymerase 10, catalytic fragment in complex with an inhibitor 3-aminobenzamide."
    Structural genomics consortium (SGC)
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 809-1017.

Entry informationi

Entry nameiPAR10_HUMAN
AccessioniPrimary (citable) accession number: Q53GL7
Secondary accession number(s): Q8N2I0
, Q8WV05, Q96CH7, Q96K72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 94 of the entry and version 2 of the sequence. [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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3