Q53GL7 (PAR10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. 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 component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of fibroblast proliferation Inferred from direct assay Ref.4. Source: UniProtKB 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_component	Golgi apparatus Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1025

1025

Poly [ADP-ribose] polymerase 10

PRO_0000252435

Regions

Domain

806 – 1025

220

PARP catalytic

Region

700 – 907

208

Myc binding

Motif

650 – 667

18

Ubiquitin-interacting

Motif

673 – 690

18

Ubiquitin-interacting

Compositional bias

186 – 193

8

Poly-Leu

Compositional bias

588 – 697

110

Glu-rich

Amino acid modifications

Modified residue

101

1

Phosphothreonine Ref.5

Modified residue

916

1

N6-acetyllysine Ref.6

Natural variations

Natural variant

249

1

I → V.
Corresponds to variant rs11136344 [ dbSNP | Ensembl ].

VAR_027859

Natural variant

395

1

L → P.
Corresponds to variant rs11136343 [ dbSNP | Ensembl ].

VAR_027860

Natural variant

630

1

V → A. Ref.1
Corresponds to variant rs11544989 [ dbSNP | Ensembl ].

VAR_027861

Experimental info

Sequence conflict

313

1

M → I in BAB55067. Ref.1

Sequence conflict

518

1

P → S in BAB55067. Ref.1

Sequence conflict

813

1

L → P in AAH14229. Ref.3

Sequence conflict

922

1

R → K in BAB55067. Ref.1

Sequence conflict

1013

1

D → G in BAD96634. Ref.2

Secondary structure

1

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1025

Helix Strand Turn

Details...

Beta strand

12 – 17

6

Helix

24 – 32

9

Turn

34 – 37

4

Beta strand

43 – 48

6

Beta strand

51 – 55

5

Helix

59 – 66

8

Beta strand

72 – 77

6

Beta strand

79 – 82

4

Beta strand

820 – 822

3

Beta strand

825 – 827

3

Helix

828 – 839

12

Helix

842 – 846

5

Beta strand

848 – 856

9

Helix

859 – 875

17

Beta strand

881 – 889

9

Helix

891 – 893

3

Helix

894 – 900

7

Turn

904 – 906

3

Beta strand

916 – 923

8

Helix

924 – 927

4

Turn

930 – 932

3

Beta strand

939 – 949

11

Beta strand

952 – 955

4

Beta strand

961 – 963

3

Beta strand

971 – 974

4

Beta strand

976 – 980

5

Beta strand

982 – 984

3

Beta strand

987 – 990

4

Beta strand

995 – 1006

12

Sequences

	Sequence		Length	Mass (Da)
	Q53GL7 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: AC9CCFCF9B83A989	FASTA	1,025	109,998
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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.

IPI

IPI00064457.
IPI00977906.

RefSeq

NP_116178.2. NM_032789.3.

UniGene

Hs.348609.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DHX	NMR	-	A	10-100	[»]
3HKV	X-ray	2.10	A/B	809-1017	[»]

ProteinModelPortal

Q53GL7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q53GL7. 1 interaction.

STRING

9606.ENSP00000325618.

PTM databases

PhosphoSite

Q53GL7.

Polymorphism databases

DMDM

116248563.

Proteomic databases

PaxDb

Q53GL7.

PRIDE

Q53GL7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313028; ENSP00000325618; ENSG00000178685.
ENST00000568154; ENSP00000456537; ENSG00000261660.

GeneID

84875.

KEGG

hsa:84875.

UCSC

uc003zal.4. human.

Organism-specific databases

CTD

84875.

GeneCards

GC08M145051.

H-InvDB

HIX0201285.

HGNC

HGNC:25895. PARP10.

HPA

HPA028122.

MIM

609564. gene.

neXtProt

NX_Q53GL7.

PharmGKB

PA134892853.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42948.

HOVERGEN

HBG068843.

InParanoid

Q53GL7.

KO

K15261.

OrthoDB

EOG4JWVD9.

PhylomeDB

Q53GL7.

Gene expression databases

ArrayExpress

Q53GL7.

Bgee

Q53GL7.

CleanEx

HS_PARP10.

Genevestigator

Q53GL7.

GermOnline

ENSG00000178685. Homo sapiens.

Family and domain databases

InterPro

IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR003903. Ubiquitin-int_motif.
[Graphical view]

Pfam

PF00644. PARP. 1 hit.
[Graphical view]

SMART

SM00726. UIM. 3 hits.
[Graphical view]

PROSITE

PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q53GL7.

GenomeRNAi

84875.

NextBio

75175.

SOURCE

Search...

Entry information

Entry name

PAR10_HUMAN

Accession

Primary (citable) accession number: Q53GL7
Secondary accession number(s): Q8N2I0 , Q8WV05, Q96CH7, Q96K72

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.