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Q53GL7 (PAR10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 10

Short name=PARP-10
EC=2.4.2.30
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 10
Short name=ARTD10
Gene names
Name:PARP10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in cell proliferation. May be required for the maintenance of cell cycle progression. Ref.4 Ref.5

Catalytic activity

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

Subunit structure

Interacts with MYC. Ref.4

Subcellular location

Nucleusnucleolus. Cytoplasm. Note: Shuttles between the nuclear and cytoplasmic compartment. A subpopulation concentrates in the nucleolus during late G1/S phase. Ref.4

Tissue specificity

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. Ref.4

Post-translational modification

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.

Sequence similarities

Contains 1 PARP catalytic domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandNAD
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

negative regulation of fibroblast proliferation

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of gene expression

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

negative regulation of protein K63-linked ubiquitination

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

negative regulation of protein import into nucleus, translocation

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

negative regulation of viral genome replication

Inferred from mutant phenotype PubMed 22176891. Source: UniProt

protein ADP-ribosylation

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

protein auto-ADP-ribosylation

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

protein poly-ADP-ribosylation

Inferred from direct assay Ref.4. Source: UniProtKB

regulation of chromatin assembly

Inferred from direct assay Ref.4. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay Ref.4. Source: UniProtKB

nucleus

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionK63-linked polyubiquitin binding

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

NAD+ ADP-ribosyltransferase activity

Inferred from mutant phenotype PubMed 23575687. Source: UniProt

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OARD1Q9Y5303EBI-2857573,EBI-8502288

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Poly [ADP-ribose] polymerase 10
PRO_0000252435

Regions

Domain806 – 1025220PARP catalytic
Region700 – 907208Myc binding
Motif650 – 66718Ubiquitin-interacting
Motif673 – 69018Ubiquitin-interacting
Compositional bias186 – 1938Poly-Leu
Compositional bias588 – 697110Glu-rich

Amino acid modifications

Modified residue1011Phosphothreonine Ref.5
Modified residue9161N6-acetyllysine Ref.6

Natural variations

Natural variant2491I → V.
Corresponds to variant rs11136344 [ dbSNP | Ensembl ].
VAR_027859
Natural variant3951L → P.
Corresponds to variant rs11136343 [ dbSNP | Ensembl ].
VAR_027860
Natural variant6301V → A. Ref.1
Corresponds to variant rs11544989 [ dbSNP | Ensembl ].
VAR_027861

Experimental info

Sequence conflict3131M → I in BAB55067. Ref.1
Sequence conflict5181P → S in BAB55067. Ref.1
Sequence conflict8131L → P in AAH14229. Ref.3
Sequence conflict9221R → K in BAB55067. Ref.1
Sequence conflict10131D → G in BAD96634. Ref.2

Secondary structure

........................................................ 1025
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q53GL7 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: AC9CCFCF9B83A989

FASTA1,025109,998
        10         20         30         40         50         60 
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC GGVLTFREPA 

        70         80         90        100        110        120 
DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT TPQRLEQHVQ ALLRASGLPV 

       130        140        150        160        170        180 
QPCCALASPR PDRALVQLPK PLSEADVRVL EEQAQNLGLE GTLVSLARVP QARAVRVVGD 

       190        200        210        220        230        240 
GASVDLLLLE LYLENERRSG GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE 

       250        260        270        280        290        300 
LSLVPHYDIL EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE 

       310        320        330        340        350        360 
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS SMPMGSLEHE 

       370        380        390        400        410        420 
GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL VEIAMDSPEQ EGLVGPMEIT 

       430        440        450        460        470        480 
MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM EPGAMRFLQL YHEDLLAGLG DVALLPLEGP 

       490        500        510        520        530        540 
DMTGFRLCGA QASCQAAEEF LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF 

       550        560        570        580        590        600 
QCVFGTERLA TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA 

       610        620        630        640        650        660 
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL EEEAALQLAL 

       670        680        690        700        710        720 
HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD GGTDGKAQLV VHSAFEQDVE 

       730        740        750        760        770        780 
ELDRALRAAL EVHVQEETVG PWRRTLPAEL RARLERCHGV SVALRGDCTI LRGFGAHPAR 

       790        800        810        820        830        840 
AARHLVALLA GPWDQSLAFP LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT 

       850        860        870        880        890        900 
LDAARSSIRV VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH 

       910        920        930        940        950        960 
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT GDYGQGRRGL 

       970        980        990       1000       1010       1020 
RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH LITCEHVPRA SPDDPSGLPG 


RSPDT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation."
Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E., Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y., Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.
Oncogene 24:1982-1993(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34960.1.
RefSeqNP_116178.2. NM_032789.3.
UniGeneHs.348609.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DHXNMR-A10-100[»]
3HKVX-ray2.10A/B809-1017[»]
ProteinModelPortalQ53GL7.
SMRQ53GL7. Positions 11-101, 817-1008.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124320. 9 interactions.
IntActQ53GL7. 4 interactions.
MINTMINT-8408778.
STRING9606.ENSP00000325618.

Chemistry

ChEMBLCHEMBL2429708.

PTM databases

PhosphoSiteQ53GL7.

Polymorphism databases

DMDM116248563.

Proteomic databases

MaxQBQ53GL7.
PaxDbQ53GL7.
PRIDEQ53GL7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313028; ENSP00000325618; ENSG00000178685.
ENST00000568154; ENSP00000456537; ENSG00000261660.
GeneID84875.
KEGGhsa:84875.
UCSCuc003zal.4. human.

Organism-specific databases

CTD84875.
GeneCardsGC08M145051.
H-InvDBHIX0201285.
HGNCHGNC:25895. PARP10.
HPAHPA028122.
MIM609564. gene.
neXtProtNX_Q53GL7.
PharmGKBPA134892853.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42948.
HOVERGENHBG068843.
InParanoidQ53GL7.
KOK15261.
PhylomeDBQ53GL7.
TreeFamTF328965.

Gene expression databases

ArrayExpressQ53GL7.
BgeeQ53GL7.
CleanExHS_PARP10.
GenevestigatorQ53GL7.

Family and domain databases

Gene3D3.90.228.10. 1 hit.
InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamPF00644. PARP. 1 hit.
[Graphical view]
SMARTSM00726. UIM. 3 hits.
[Graphical view]
PROSITEPS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ53GL7.
GeneWikiPARP10.
GenomeRNAi84875.
NextBio75175.
PROQ53GL7.
SOURCESearch...

Entry information

Entry namePAR10_HUMAN
AccessionPrimary (citable) accession number: Q53GL7
Secondary accession number(s): Q8N2I0 expand/collapse secondary AC list , Q8WV05, Q96CH7, Q96K72
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM