Full text data of PARP10
PARP10
[Confidence: low (only semi-automatic identification from reviews)]
Poly [ADP-ribose] polymerase 10; PARP-10; 2.4.2.30 (ADP-ribosyltransferase diphtheria toxin-like 10; ARTD10)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Poly [ADP-ribose] polymerase 10; PARP-10; 2.4.2.30 (ADP-ribosyltransferase diphtheria toxin-like 10; ARTD10)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q53GL7
ID PAR10_HUMAN Reviewed; 1025 AA.
AC Q53GL7; Q8N2I0; Q8WV05; Q96CH7; Q96K72;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Poly [ADP-ribose] polymerase 10;
DE Short=PARP-10;
DE EC=2.4.2.30;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 10;
DE Short=ARTD10;
GN Name=PARP10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-630.
RC TISSUE=Mammary gland, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1025.
RC TISSUE=Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH MYC.
RX PubMed=15674325; DOI=10.1038/sj.onc.1208410;
RA Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E.,
RA Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y.,
RA Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.;
RT "PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
RT polymerase activity, inhibits transformation.";
RL Oncogene 24:1982-1993(2005).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION AT THR-101.
RX PubMed=16455663; DOI=10.1074/jbc.M506745200;
RA Chou H.Y., Chou H.T., Lee S.C.;
RT "CDK-dependent activation of poly(ADP-ribose) polymerase member 10
RT (PARP10).";
RL J. Biol. Chem. 281:15201-15207(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-916, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-
RT ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [8]
RP STRUCTURE BY NMR OF 7-101.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM domain in the human poly (ADP-ribose)
RT polymerase family, member 10 variant.";
RL Submitted (FEB-2007) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 809-1017.
RG Structural genomics consortium (SGC);
RT "Human poly(ADP-ribose) polymerase 10, catalytic fragment in complex
RT with an inhibitor 3-aminobenzamide.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: May play a role in cell proliferation. May be required
CC for the maintenance of cell cycle progression.
CC -!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
CC nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
CC -!- SUBUNIT: Interacts with MYC.
CC -!- INTERACTION:
CC Q9Y530:OARD1; NbExp=3; IntAct=EBI-2857573, EBI-8502288;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Shuttles
CC between the nuclear and cytoplasmic compartment. A subpopulation
CC concentrates in the nucleolus during late G1/S phase.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus.
CC Intermediate levels in liver, kidney, pancreas, prostate, testis,
CC ovary, intestine, and leukocytes. Low expression in heart, brain,
CC placenta, lung, skeletal muscle, and colon.
CC -!- PTM: Stimulated through its phosphorylation by CDK2. Acquires CDK-
CC dependent phosphorylation through late-G1 to S phase, and from
CC prometaphase to cytokinesis in the nucleolar organizing regions.
CC Phosphorylation is suppressed in growth-arrested cells.
CC -!- SIMILARITY: Contains 1 PARP catalytic domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11498.1; Type=Frameshift; Positions=965;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK027370; BAB55067.1; -; mRNA.
DR EMBL; AK075250; BAC11498.1; ALT_SEQ; mRNA.
DR EMBL; AK222914; BAD96634.1; -; mRNA.
DR EMBL; BC014229; AAH14229.2; -; mRNA.
DR EMBL; BC019030; AAH19030.2; -; mRNA.
DR RefSeq; NP_116178.2; NM_032789.3.
DR UniGene; Hs.348609; -.
DR PDB; 2DHX; NMR; -; A=10-100.
DR PDB; 3HKV; X-ray; 2.10 A; A/B=809-1017.
DR PDBsum; 2DHX; -.
DR PDBsum; 3HKV; -.
DR ProteinModelPortal; Q53GL7; -.
DR SMR; Q53GL7; 11-101, 817-1008.
DR IntAct; Q53GL7; 4.
DR MINT; MINT-8408778; -.
DR STRING; 9606.ENSP00000325618; -.
DR PhosphoSite; Q53GL7; -.
DR DMDM; 116248563; -.
DR PaxDb; Q53GL7; -.
DR PRIDE; Q53GL7; -.
DR Ensembl; ENST00000313028; ENSP00000325618; ENSG00000178685.
DR Ensembl; ENST00000568154; ENSP00000456537; ENSG00000261660.
DR GeneID; 84875; -.
DR KEGG; hsa:84875; -.
DR UCSC; uc003zal.4; human.
DR CTD; 84875; -.
DR GeneCards; GC08M145051; -.
DR H-InvDB; HIX0201285; -.
DR HGNC; HGNC:25895; PARP10.
DR HPA; HPA028122; -.
DR MIM; 609564; gene.
DR neXtProt; NX_Q53GL7; -.
DR PharmGKB; PA134892853; -.
DR eggNOG; NOG42948; -.
DR HOVERGEN; HBG068843; -.
DR InParanoid; Q53GL7; -.
DR KO; K15261; -.
DR PhylomeDB; Q53GL7; -.
DR EvolutionaryTrace; Q53GL7; -.
DR GeneWiki; PARP10; -.
DR GenomeRNAi; 84875; -.
DR NextBio; 75175; -.
DR PRO; PR:Q53GL7; -.
DR ArrayExpress; Q53GL7; -.
DR Bgee; Q53GL7; -.
DR CleanEx; HS_PARP10; -.
DR Genevestigator; Q53GL7; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IDA:UniProtKB.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR003903; Ubiquitin-int_motif.
DR Pfam; PF00644; PARP; 1.
DR SMART; SM00726; UIM; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 1025 Poly [ADP-ribose] polymerase 10.
FT /FTId=PRO_0000252435.
FT DOMAIN 806 1025 PARP catalytic.
FT REGION 700 907 Myc binding.
FT MOTIF 650 667 Ubiquitin-interacting.
FT MOTIF 673 690 Ubiquitin-interacting.
FT COMPBIAS 186 193 Poly-Leu.
FT COMPBIAS 588 697 Glu-rich.
FT MOD_RES 101 101 Phosphothreonine.
FT MOD_RES 916 916 N6-acetyllysine.
FT VARIANT 249 249 I -> V (in dbSNP:rs11136344).
FT /FTId=VAR_027859.
FT VARIANT 395 395 L -> P (in dbSNP:rs11136343).
FT /FTId=VAR_027860.
FT VARIANT 630 630 V -> A (in dbSNP:rs11544989).
FT /FTId=VAR_027861.
FT CONFLICT 313 313 M -> I (in Ref. 1; BAB55067).
FT CONFLICT 518 518 P -> S (in Ref. 1; BAB55067).
FT CONFLICT 813 813 L -> P (in Ref. 3; AAH14229).
FT CONFLICT 922 922 R -> K (in Ref. 1; BAB55067).
FT CONFLICT 1013 1013 D -> G (in Ref. 2; BAD96634).
FT STRAND 12 17
FT HELIX 24 32
FT TURN 34 37
FT STRAND 43 48
FT STRAND 51 55
FT HELIX 59 66
FT STRAND 72 77
FT STRAND 79 82
FT STRAND 820 822
FT STRAND 825 827
FT HELIX 828 839
FT HELIX 842 846
FT STRAND 848 856
FT HELIX 859 875
FT STRAND 881 889
FT HELIX 891 893
FT HELIX 894 900
FT TURN 904 906
FT STRAND 916 923
FT HELIX 924 927
FT TURN 930 932
FT STRAND 939 949
FT STRAND 952 955
FT STRAND 961 963
FT STRAND 971 974
FT STRAND 976 980
FT STRAND 982 984
FT STRAND 987 990
FT STRAND 995 1006
SQ SEQUENCE 1025 AA; 109998 MW; AC9CCFCF9B83A989 CRC64;
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC GGVLTFREPA
DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT TPQRLEQHVQ ALLRASGLPV
QPCCALASPR PDRALVQLPK PLSEADVRVL EEQAQNLGLE GTLVSLARVP QARAVRVVGD
GASVDLLLLE LYLENERRSG GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE
LSLVPHYDIL EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS SMPMGSLEHE
GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL VEIAMDSPEQ EGLVGPMEIT
MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM EPGAMRFLQL YHEDLLAGLG DVALLPLEGP
DMTGFRLCGA QASCQAAEEF LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF
QCVFGTERLA TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL EEEAALQLAL
HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD GGTDGKAQLV VHSAFEQDVE
ELDRALRAAL EVHVQEETVG PWRRTLPAEL RARLERCHGV SVALRGDCTI LRGFGAHPAR
AARHLVALLA GPWDQSLAFP LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT
LDAARSSIRV VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT GDYGQGRRGL
RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH LITCEHVPRA SPDDPSGLPG
RSPDT
//
ID PAR10_HUMAN Reviewed; 1025 AA.
AC Q53GL7; Q8N2I0; Q8WV05; Q96CH7; Q96K72;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 86.
DE RecName: Full=Poly [ADP-ribose] polymerase 10;
DE Short=PARP-10;
DE EC=2.4.2.30;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 10;
DE Short=ARTD10;
GN Name=PARP10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-630.
RC TISSUE=Mammary gland, and Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1025.
RC TISSUE=Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH MYC.
RX PubMed=15674325; DOI=10.1038/sj.onc.1208410;
RA Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E.,
RA Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y.,
RA Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.;
RT "PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
RT polymerase activity, inhibits transformation.";
RL Oncogene 24:1982-1993(2005).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION AT THR-101.
RX PubMed=16455663; DOI=10.1074/jbc.M506745200;
RA Chou H.Y., Chou H.T., Lee S.C.;
RT "CDK-dependent activation of poly(ADP-ribose) polymerase member 10
RT (PARP10).";
RL J. Biol. Chem. 281:15201-15207(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-916, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-
RT ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [8]
RP STRUCTURE BY NMR OF 7-101.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM domain in the human poly (ADP-ribose)
RT polymerase family, member 10 variant.";
RL Submitted (FEB-2007) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 809-1017.
RG Structural genomics consortium (SGC);
RT "Human poly(ADP-ribose) polymerase 10, catalytic fragment in complex
RT with an inhibitor 3-aminobenzamide.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: May play a role in cell proliferation. May be required
CC for the maintenance of cell cycle progression.
CC -!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
CC nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
CC -!- SUBUNIT: Interacts with MYC.
CC -!- INTERACTION:
CC Q9Y530:OARD1; NbExp=3; IntAct=EBI-2857573, EBI-8502288;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Note=Shuttles
CC between the nuclear and cytoplasmic compartment. A subpopulation
CC concentrates in the nucleolus during late G1/S phase.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus.
CC Intermediate levels in liver, kidney, pancreas, prostate, testis,
CC ovary, intestine, and leukocytes. Low expression in heart, brain,
CC placenta, lung, skeletal muscle, and colon.
CC -!- PTM: Stimulated through its phosphorylation by CDK2. Acquires CDK-
CC dependent phosphorylation through late-G1 to S phase, and from
CC prometaphase to cytokinesis in the nucleolar organizing regions.
CC Phosphorylation is suppressed in growth-arrested cells.
CC -!- SIMILARITY: Contains 1 PARP catalytic domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11498.1; Type=Frameshift; Positions=965;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK027370; BAB55067.1; -; mRNA.
DR EMBL; AK075250; BAC11498.1; ALT_SEQ; mRNA.
DR EMBL; AK222914; BAD96634.1; -; mRNA.
DR EMBL; BC014229; AAH14229.2; -; mRNA.
DR EMBL; BC019030; AAH19030.2; -; mRNA.
DR RefSeq; NP_116178.2; NM_032789.3.
DR UniGene; Hs.348609; -.
DR PDB; 2DHX; NMR; -; A=10-100.
DR PDB; 3HKV; X-ray; 2.10 A; A/B=809-1017.
DR PDBsum; 2DHX; -.
DR PDBsum; 3HKV; -.
DR ProteinModelPortal; Q53GL7; -.
DR SMR; Q53GL7; 11-101, 817-1008.
DR IntAct; Q53GL7; 4.
DR MINT; MINT-8408778; -.
DR STRING; 9606.ENSP00000325618; -.
DR PhosphoSite; Q53GL7; -.
DR DMDM; 116248563; -.
DR PaxDb; Q53GL7; -.
DR PRIDE; Q53GL7; -.
DR Ensembl; ENST00000313028; ENSP00000325618; ENSG00000178685.
DR Ensembl; ENST00000568154; ENSP00000456537; ENSG00000261660.
DR GeneID; 84875; -.
DR KEGG; hsa:84875; -.
DR UCSC; uc003zal.4; human.
DR CTD; 84875; -.
DR GeneCards; GC08M145051; -.
DR H-InvDB; HIX0201285; -.
DR HGNC; HGNC:25895; PARP10.
DR HPA; HPA028122; -.
DR MIM; 609564; gene.
DR neXtProt; NX_Q53GL7; -.
DR PharmGKB; PA134892853; -.
DR eggNOG; NOG42948; -.
DR HOVERGEN; HBG068843; -.
DR InParanoid; Q53GL7; -.
DR KO; K15261; -.
DR PhylomeDB; Q53GL7; -.
DR EvolutionaryTrace; Q53GL7; -.
DR GeneWiki; PARP10; -.
DR GenomeRNAi; 84875; -.
DR NextBio; 75175; -.
DR PRO; PR:Q53GL7; -.
DR ArrayExpress; Q53GL7; -.
DR Bgee; Q53GL7; -.
DR CleanEx; HS_PARP10; -.
DR Genevestigator; Q53GL7; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IDA:UniProtKB.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR003903; Ubiquitin-int_motif.
DR Pfam; PF00644; PARP; 1.
DR SMART; SM00726; UIM; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 1025 Poly [ADP-ribose] polymerase 10.
FT /FTId=PRO_0000252435.
FT DOMAIN 806 1025 PARP catalytic.
FT REGION 700 907 Myc binding.
FT MOTIF 650 667 Ubiquitin-interacting.
FT MOTIF 673 690 Ubiquitin-interacting.
FT COMPBIAS 186 193 Poly-Leu.
FT COMPBIAS 588 697 Glu-rich.
FT MOD_RES 101 101 Phosphothreonine.
FT MOD_RES 916 916 N6-acetyllysine.
FT VARIANT 249 249 I -> V (in dbSNP:rs11136344).
FT /FTId=VAR_027859.
FT VARIANT 395 395 L -> P (in dbSNP:rs11136343).
FT /FTId=VAR_027860.
FT VARIANT 630 630 V -> A (in dbSNP:rs11544989).
FT /FTId=VAR_027861.
FT CONFLICT 313 313 M -> I (in Ref. 1; BAB55067).
FT CONFLICT 518 518 P -> S (in Ref. 1; BAB55067).
FT CONFLICT 813 813 L -> P (in Ref. 3; AAH14229).
FT CONFLICT 922 922 R -> K (in Ref. 1; BAB55067).
FT CONFLICT 1013 1013 D -> G (in Ref. 2; BAD96634).
FT STRAND 12 17
FT HELIX 24 32
FT TURN 34 37
FT STRAND 43 48
FT STRAND 51 55
FT HELIX 59 66
FT STRAND 72 77
FT STRAND 79 82
FT STRAND 820 822
FT STRAND 825 827
FT HELIX 828 839
FT HELIX 842 846
FT STRAND 848 856
FT HELIX 859 875
FT STRAND 881 889
FT HELIX 891 893
FT HELIX 894 900
FT TURN 904 906
FT STRAND 916 923
FT HELIX 924 927
FT TURN 930 932
FT STRAND 939 949
FT STRAND 952 955
FT STRAND 961 963
FT STRAND 971 974
FT STRAND 976 980
FT STRAND 982 984
FT STRAND 987 990
FT STRAND 995 1006
SQ SEQUENCE 1025 AA; 109998 MW; AC9CCFCF9B83A989 CRC64;
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC GGVLTFREPA
DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT TPQRLEQHVQ ALLRASGLPV
QPCCALASPR PDRALVQLPK PLSEADVRVL EEQAQNLGLE GTLVSLARVP QARAVRVVGD
GASVDLLLLE LYLENERRSG GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE
LSLVPHYDIL EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS SMPMGSLEHE
GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL VEIAMDSPEQ EGLVGPMEIT
MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM EPGAMRFLQL YHEDLLAGLG DVALLPLEGP
DMTGFRLCGA QASCQAAEEF LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF
QCVFGTERLA TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL EEEAALQLAL
HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD GGTDGKAQLV VHSAFEQDVE
ELDRALRAAL EVHVQEETVG PWRRTLPAEL RARLERCHGV SVALRGDCTI LRGFGAHPAR
AARHLVALLA GPWDQSLAFP LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT
LDAARSSIRV VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT GDYGQGRRGL
RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH LITCEHVPRA SPDDPSGLPG
RSPDT
//
MIM
609564
*RECORD*
*FIELD* NO
609564
*FIELD* TI
*609564 POLY(ADP-RIBOSE) POLYMERASE 10; PARP10
*FIELD* TX
DESCRIPTION
Poly(ADP-ribose) polymerases (PARPs), such as PARP10, regulate gene
read moretranscription by altering chromatin organization by adding ADP-ribose to
histones. PARPs can also function as transcriptional cofactors (Yu et
al., 2005).
CLONING
Yu et al. (2005) identified PARP10 as a MYC (190080)-interacting protein
by immunopurifying MYC-containing complexes from human Jurkat T cells.
By searching an EST database using PARP10 peptide sequences, they
identified a PARP10 cDNA. The deduced 1,025-amino acid protein had an
apparent molecular mass of 150 kD by SDS-PAGE. PARP10 contains an
N-terminal RNA recognition motif, followed by a glycine-rich domain, a
glutamic acid-rich domain, and a PARP catalytic domain. The glutamic
acid-rich domain has a potential leucine-rich nuclear export signal
(NES) and 2 ubiquitin-interacting motifs. Northern blot analysis
detected a 3.8-kb PARP10 transcript in all tissues analyzed, with
highest expression in spleen and thymus. PARP10 localized predominantly
to the cytoplasm of transfected human osteosarcoma cells, but mutation
of the NES or use of a nuclear export inhibitor resulted in PARP10
accumulation in the nuclear compartment.
GENE FUNCTION
Yu et al. (2005) found that the C-terminal half of PARP10 showed PARP
activity. The PARP domain possessed auto-PARP activity and modified all
4 core histones (see 142711) tested, with preference for histone H2A,
but it did not modify MYC, MAX (154950), histone H1, or YY1 (600013).
The full-length protein also exhibited PARP activity. Point mutation of
his887 or gly888 inactivated the enzyme, and point mutation of lys916
strongly reduced the catalytic activity. By coimmunoprecipitations and
in vitro protein pull-down assays, Yu et al. (2005) confirmed a direct
interaction between PARP10 and MYC. Mutation analysis indicated that the
C-terminal half of PARP10 interacted with both N- and C-terminal regions
of MYC. PARP10 overexpression inhibited MYC/HRAS (190020)- and
adenovirus E1A/HRAS-mediated cotransformation of rat embryo fibroblasts,
and it inhibited entry into S phase in serum-stimulated mouse
fibroblasts. The effects of PARP10 on cell proliferation were
independent of the PARP domain.
Kleine et al. (2008) demonstrated that, unlike PARP1 (173870), which
catalyzed poly-ADP-ribosylation, PARP10 catalyzed only
mono-ADP-ribosylation. Core secondary structural elements and critical
residues involved in NAD+ binding are conserved in PARP1 and PARP10, but
PARP10 has an isoleucine (I987) in place of the catalytic glutamate
found in PARP1 (E988). PARP10 catalyzed auto-ADP-ribosylation,
predominantly on E882. Structural analysis revealed that E882 lies near
the catalytic center of the molecule, and Kleine et al. (2008) showed
that E882, via substrate-assisted catalysis, behaved as the catalytic
glutamate. They concluded that automodification of the catalytic
glutamate prevents PARP10 from functioning as a poly-ADP-ribose
polymerase.
GENE STRUCTURE
Lesniewicz et al. (2005) determined that the mouse Parp10 gene contains
at least 11 exons. All introns are small except intron 9, which spans
more than 6 kb. A potential TATA box is located upstream of the most
5-prime sequence. The 3-prime sequence of the Parp10 gene overlaps on
the same strand with the 5-prime sequence of the Plec1 gene (601282).
Exons 10 and 11 of the Parp10 gene, which encode the last 109 amino
acids and the 3-prime UTR of Parp10, are spliced at different sites to
form the untranslated exons -1 and 0a of a Plec1 splice variant.
Lesniewicz et al. (2005) identified mouse ESTs containing sequences from
both Parp10 and Plec1, but they did not find read-through transcripts.
MAPPING
By FISH, Yu et al. (2005) mapped the PARP10 gene to chromosome 8q24.
Lesniewicz et al. (2005) mapped the mouse Parp10 gene to chromosome 15,
immediately upstream of and in a head-to-tail orientation with the Plec1
gene.
*FIELD* RF
1. Kleine, H.; Poreba, E.; Lesniewicz, K.; Hassa, P. O.; Hottiger,
M. O.; Litchfield, D. W.; Shilton, B. H.; Luscher, B.: Substrate-assisted
catalysis by PARP10 limits its activity to mono-ADP-ribosylation. Molec.
Cell 32: 57-69, 2008.
2. Lesniewicz, K.; Luscher-Firzlaff, J.; Poreba, E.; Fuchs, P.; Walsemann,
G.; Wiche, G.; Luscher, B.: Overlap of the gene encoding the novel
poly(ADP-ribose) polymerase Parp10 with the plectin 1 gene and common
use of exon sequences. Genomics 86: 38-46, 2005.
3. Yu, M.; Schreek, S.; Cerni, C.; Schamberger, C.; Lesniewicz, K.;
Poreba, E.; Vervoorts, J.; Walsemann, G.; Grotzinger, J.; Kremmer,
E.; Mehraein, Y.; Mertsching, J.; Kraft, R.; Austen, M.; Luscher-Firzlaff,
J.; Luscher, B.: PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
polymerase activity, inhibits transformation. Oncogene 24: 1982-1993,
2005.
*FIELD* CN
Patricia A. Hartz - updated: 11/24/2008
*FIELD* CD
Patricia A. Hartz: 8/31/2005
*FIELD* ED
wwang: 05/04/2009
mgross: 12/2/2008
terry: 11/24/2008
mgross: 8/31/2005
*RECORD*
*FIELD* NO
609564
*FIELD* TI
*609564 POLY(ADP-RIBOSE) POLYMERASE 10; PARP10
*FIELD* TX
DESCRIPTION
Poly(ADP-ribose) polymerases (PARPs), such as PARP10, regulate gene
read moretranscription by altering chromatin organization by adding ADP-ribose to
histones. PARPs can also function as transcriptional cofactors (Yu et
al., 2005).
CLONING
Yu et al. (2005) identified PARP10 as a MYC (190080)-interacting protein
by immunopurifying MYC-containing complexes from human Jurkat T cells.
By searching an EST database using PARP10 peptide sequences, they
identified a PARP10 cDNA. The deduced 1,025-amino acid protein had an
apparent molecular mass of 150 kD by SDS-PAGE. PARP10 contains an
N-terminal RNA recognition motif, followed by a glycine-rich domain, a
glutamic acid-rich domain, and a PARP catalytic domain. The glutamic
acid-rich domain has a potential leucine-rich nuclear export signal
(NES) and 2 ubiquitin-interacting motifs. Northern blot analysis
detected a 3.8-kb PARP10 transcript in all tissues analyzed, with
highest expression in spleen and thymus. PARP10 localized predominantly
to the cytoplasm of transfected human osteosarcoma cells, but mutation
of the NES or use of a nuclear export inhibitor resulted in PARP10
accumulation in the nuclear compartment.
GENE FUNCTION
Yu et al. (2005) found that the C-terminal half of PARP10 showed PARP
activity. The PARP domain possessed auto-PARP activity and modified all
4 core histones (see 142711) tested, with preference for histone H2A,
but it did not modify MYC, MAX (154950), histone H1, or YY1 (600013).
The full-length protein also exhibited PARP activity. Point mutation of
his887 or gly888 inactivated the enzyme, and point mutation of lys916
strongly reduced the catalytic activity. By coimmunoprecipitations and
in vitro protein pull-down assays, Yu et al. (2005) confirmed a direct
interaction between PARP10 and MYC. Mutation analysis indicated that the
C-terminal half of PARP10 interacted with both N- and C-terminal regions
of MYC. PARP10 overexpression inhibited MYC/HRAS (190020)- and
adenovirus E1A/HRAS-mediated cotransformation of rat embryo fibroblasts,
and it inhibited entry into S phase in serum-stimulated mouse
fibroblasts. The effects of PARP10 on cell proliferation were
independent of the PARP domain.
Kleine et al. (2008) demonstrated that, unlike PARP1 (173870), which
catalyzed poly-ADP-ribosylation, PARP10 catalyzed only
mono-ADP-ribosylation. Core secondary structural elements and critical
residues involved in NAD+ binding are conserved in PARP1 and PARP10, but
PARP10 has an isoleucine (I987) in place of the catalytic glutamate
found in PARP1 (E988). PARP10 catalyzed auto-ADP-ribosylation,
predominantly on E882. Structural analysis revealed that E882 lies near
the catalytic center of the molecule, and Kleine et al. (2008) showed
that E882, via substrate-assisted catalysis, behaved as the catalytic
glutamate. They concluded that automodification of the catalytic
glutamate prevents PARP10 from functioning as a poly-ADP-ribose
polymerase.
GENE STRUCTURE
Lesniewicz et al. (2005) determined that the mouse Parp10 gene contains
at least 11 exons. All introns are small except intron 9, which spans
more than 6 kb. A potential TATA box is located upstream of the most
5-prime sequence. The 3-prime sequence of the Parp10 gene overlaps on
the same strand with the 5-prime sequence of the Plec1 gene (601282).
Exons 10 and 11 of the Parp10 gene, which encode the last 109 amino
acids and the 3-prime UTR of Parp10, are spliced at different sites to
form the untranslated exons -1 and 0a of a Plec1 splice variant.
Lesniewicz et al. (2005) identified mouse ESTs containing sequences from
both Parp10 and Plec1, but they did not find read-through transcripts.
MAPPING
By FISH, Yu et al. (2005) mapped the PARP10 gene to chromosome 8q24.
Lesniewicz et al. (2005) mapped the mouse Parp10 gene to chromosome 15,
immediately upstream of and in a head-to-tail orientation with the Plec1
gene.
*FIELD* RF
1. Kleine, H.; Poreba, E.; Lesniewicz, K.; Hassa, P. O.; Hottiger,
M. O.; Litchfield, D. W.; Shilton, B. H.; Luscher, B.: Substrate-assisted
catalysis by PARP10 limits its activity to mono-ADP-ribosylation. Molec.
Cell 32: 57-69, 2008.
2. Lesniewicz, K.; Luscher-Firzlaff, J.; Poreba, E.; Fuchs, P.; Walsemann,
G.; Wiche, G.; Luscher, B.: Overlap of the gene encoding the novel
poly(ADP-ribose) polymerase Parp10 with the plectin 1 gene and common
use of exon sequences. Genomics 86: 38-46, 2005.
3. Yu, M.; Schreek, S.; Cerni, C.; Schamberger, C.; Lesniewicz, K.;
Poreba, E.; Vervoorts, J.; Walsemann, G.; Grotzinger, J.; Kremmer,
E.; Mehraein, Y.; Mertsching, J.; Kraft, R.; Austen, M.; Luscher-Firzlaff,
J.; Luscher, B.: PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
polymerase activity, inhibits transformation. Oncogene 24: 1982-1993,
2005.
*FIELD* CN
Patricia A. Hartz - updated: 11/24/2008
*FIELD* CD
Patricia A. Hartz: 8/31/2005
*FIELD* ED
wwang: 05/04/2009
mgross: 12/2/2008
terry: 11/24/2008
mgross: 8/31/2005