PAR10_HUMAN
ID PAR10_HUMAN Reviewed; 1025 AA.
AC Q53GL7; Q8N2I0; Q8WV05; Q96CH7; Q96K72;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP10 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 10 {ECO:0000303|PubMed:20106667};
DE Short=ARTD10 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 10 {ECO:0000303|PubMed:20106667};
DE Short=PARP-10 {ECO:0000303|PubMed:20106667};
GN Name=PARP10 {ECO:0000312|HGNC:HGNC:25895};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
RP 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) polymerase
RT activity, inhibits transformation.";
RL Oncogene 24:1982-1993(2005).
RN [5]
RP 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 FUNCTION, CATALYTIC ACTIVITY, ADP-RIBOSYLATION AT GLU-882, AND MUTAGENESIS
RP OF GLU-882; GLY-888; 980-ASP--ILE-982; PRO-985; ILE-987 AND THR-999.
RX PubMed=18851833; DOI=10.1016/j.molcel.2008.08.009;
RA Kleine H., Poreba E., Lesniewicz K., Hassa P.O., Hottiger M.O.,
RA Litchfield D.W., Shilton B.H., Luescher B.;
RT "Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-
RT ribosylation.";
RL Mol. Cell 32:57-69(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-916, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [8]
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-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-1011, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP FUNCTION.
RX PubMed=23332125; DOI=10.1186/1478-811x-11-5;
RA Feijs K.L., Kleine H., Braczynski A., Forst A.H., Herzog N., Verheugd P.,
RA Linzen U., Kremmer E., Luscher B.;
RT "ARTD10 substrate identification on protein microarrays: regulation of
RT GSK3beta by mono-ADP-ribosylation.";
RL Cell Commun. Signal. 11:5-5(2013).
RN [11]
RP FUNCTION.
RX PubMed=23474714; DOI=10.1038/nsmb.2521;
RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R.,
RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B.,
RA Hottiger M.O.;
RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
RL Nat. Struct. Mol. Biol. 20:502-507(2013).
RN [12]
RP INTERACTION WITH PARP14, AND MUTAGENESIS OF GLY-888.
RX PubMed=23473667; DOI=10.1016/j.str.2012.12.019;
RA Forst A.H., Karlberg T., Herzog N., Thorsell A.G., Gross A., Feijs K.L.,
RA Verheugd P., Kursula P., Nijmeijer B., Kremmer E., Kleine H.,
RA Ladurner A.G., Schuler H., Luscher B.;
RT "Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8
RT macrodomains.";
RL Structure 21:462-475(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-423; SER-431 AND
RP SER-663, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, INTERACTION WITH PCNA, AND MUTAGENESIS OF 650-LEU--GLN-690;
RP 831-GLN--TYR-838 AND GLY-888.
RX PubMed=24695737; DOI=10.1074/jbc.m114.556340;
RA Nicolae C.M., Aho E.R., Vlahos A.H., Choe K.N., De S., Karras G.I.,
RA Moldovan G.L.;
RT "The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell
RT nuclear antigen (PCNA) and is required for DNA damage tolerance.";
RL J. Biol. Chem. 289:13627-13637(2014).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT GLU-106; LYS-140 AND
RP LYS-916.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [16]
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 [17]
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 with
RT an inhibitor 3-aminobenzamide.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate and aspartate residues on target proteins (PubMed:18851833,
CC PubMed:23332125, PubMed:23474714, PubMed:25043379). In contrast to
CC PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation
CC (PubMed:18851833). Catalyzes mono-ADP-ribosylation of GSK3B, leading to
CC negatively regulate GSK3B kinase activity (PubMed:23332125). Involved
CC in translesion DNA synthesis in response to DNA damage via its
CC interaction with PCNA (PubMed:24695737). {ECO:0000269|PubMed:18851833,
CC ECO:0000269|PubMed:23332125, ECO:0000269|PubMed:23474714,
CC ECO:0000269|PubMed:24695737, ECO:0000269|PubMed:25043379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-
CC lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142515; Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000269|PubMed:18851833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000269|PubMed:18851833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379};
CC -!- SUBUNIT: Interacts with MYC (PubMed:15674325). Interacts with PARP14
CC (PubMed:23473667). Interacts (via-PIP box and ubiquitin-interacting
CC motifs) with PCNA (PubMed:24695737). {ECO:0000269|PubMed:15674325,
CC ECO:0000269|PubMed:23473667, ECO:0000269|PubMed:24695737}.
CC -!- INTERACTION:
CC Q53GL7; Q9Y530: OARD1; NbExp=3; IntAct=EBI-2857573, EBI-8502288;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15674325}.
CC Cytoplasm {ECO:0000269|PubMed:15674325}. Note=Shuttles between the
CC nuclear and cytoplasmic compartment (PubMed:15674325). A subpopulation
CC concentrates in the nucleolus during late G1/S phase (PubMed:15674325).
CC {ECO:0000269|PubMed:15674325}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus
CC (PubMed:15674325). Intermediate levels in liver, kidney, pancreas,
CC prostate, testis, ovary, intestine, and leukocytes (PubMed:15674325).
CC Low expression in heart, brain, placenta, lung, skeletal muscle, and
CC colon (PubMed:15674325). {ECO:0000269|PubMed:15674325}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA.
CC {ECO:0000269|PubMed:24695737}.
CC -!- PTM: Stimulated through its phosphorylation by CDK2 (PubMed:16455663).
CC Acquires CDK-dependent phosphorylation through late-G1 to S phase, and
CC from prometaphase to cytokinesis in the nucleolar organizing regions
CC (PubMed:16455663). Phosphorylation is suppressed in growth-arrested
CC cells (PubMed:16455663). {ECO:0000269|PubMed:16455663}.
CC -!- PTM: Auto-mono-ADP-ribosylated on glutamate and lysine residues.
CC {ECO:0000269|PubMed:18851833, ECO:0000269|PubMed:25043379}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11498.1; Type=Frameshift; Evidence={ECO:0000305};
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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 CCDS; CCDS34960.1; -.
DR RefSeq; NP_116178.2; NM_032789.4.
DR PDB; 2DHX; NMR; -; A=10-100.
DR PDB; 3HKV; X-ray; 2.10 A; A/B=809-1017.
DR PDB; 5LX6; X-ray; 1.25 A; A/B=819-1007.
DR PDB; 6FXI; X-ray; 2.60 A; A/B=819-1007.
DR PDBsum; 2DHX; -.
DR PDBsum; 3HKV; -.
DR PDBsum; 5LX6; -.
DR PDBsum; 6FXI; -.
DR AlphaFoldDB; Q53GL7; -.
DR SMR; Q53GL7; -.
DR BioGRID; 124320; 28.
DR IntAct; Q53GL7; 10.
DR MINT; Q53GL7; -.
DR STRING; 9606.ENSP00000325618; -.
DR BindingDB; Q53GL7; -.
DR ChEMBL; CHEMBL2429708; -.
DR DrugCentral; Q53GL7; -.
DR GlyGen; Q53GL7; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q53GL7; -.
DR PhosphoSitePlus; Q53GL7; -.
DR BioMuta; PARP10; -.
DR DMDM; 116248563; -.
DR EPD; Q53GL7; -.
DR jPOST; Q53GL7; -.
DR MassIVE; Q53GL7; -.
DR MaxQB; Q53GL7; -.
DR PaxDb; Q53GL7; -.
DR PeptideAtlas; Q53GL7; -.
DR PRIDE; Q53GL7; -.
DR ProteomicsDB; 62485; -.
DR Antibodypedia; 28206; 113 antibodies from 28 providers.
DR DNASU; 84875; -.
DR Ensembl; ENST00000313028.12; ENSP00000325618.7; ENSG00000178685.14.
DR GeneID; 84875; -.
DR KEGG; hsa:84875; -.
DR MANE-Select; ENST00000313028.12; ENSP00000325618.7; NM_032789.5; NP_116178.2.
DR UCSC; uc003zal.5; human.
DR CTD; 84875; -.
DR DisGeNET; 84875; -.
DR GeneCards; PARP10; -.
DR HGNC; HGNC:25895; PARP10.
DR HPA; ENSG00000178685; Low tissue specificity.
DR MIM; 609564; gene.
DR neXtProt; NX_Q53GL7; -.
DR OpenTargets; ENSG00000178685; -.
DR PharmGKB; PA134892853; -.
DR VEuPathDB; HostDB:ENSG00000178685; -.
DR eggNOG; ENOG502R572; Eukaryota.
DR GeneTree; ENSGT00940000162035; -.
DR InParanoid; Q53GL7; -.
DR OMA; QAFYNTL; -.
DR PhylomeDB; Q53GL7; -.
DR TreeFam; TF328965; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q53GL7; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SignaLink; Q53GL7; -.
DR BioGRID-ORCS; 84875; 25 hits in 1075 CRISPR screens.
DR ChiTaRS; PARP10; human.
DR EvolutionaryTrace; Q53GL7; -.
DR GeneWiki; PARP10; -.
DR GenomeRNAi; 84875; -.
DR Pharos; Q53GL7; Tchem.
DR PRO; PR:Q53GL7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q53GL7; protein.
DR Bgee; ENSG00000178685; Expressed in granulocyte and 168 other tissues.
DR ExpressionAtlas; Q53GL7; baseline and differential.
DR Genevisible; Q53GL7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IMP:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IMP:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; 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 GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR CDD; cd12547; RRM1_2_PAR10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034464; PAR10_RRM1_2.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR Pfam; PF00644; PARP; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Cytoplasm; DNA damage;
KW DNA repair; Glycosyltransferase; NAD; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1025
FT /note="Protein mono-ADP-ribosyltransferase PARP10"
FT /id="PRO_0000252435"
FT DOMAIN 806..1025
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..907
FT /note="Myc binding"
FT /evidence="ECO:0000269|PubMed:15674325"
FT REGION 1006..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 650..667
FT /note="Ubiquitin-interacting"
FT /evidence="ECO:0000305|PubMed:24695737"
FT MOTIF 673..690
FT /note="Ubiquitin-interacting"
FT /evidence="ECO:0000305|PubMed:24695737"
FT MOTIF 831..838
FT /note="PIP-box"
FT /evidence="ECO:0000269|PubMed:24695737"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16455663"
FT MOD_RES 106
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 140
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 882
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:18851833"
FT MOD_RES 916
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 916
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 249
FT /note="I -> V (in dbSNP:rs11136344)"
FT /id="VAR_027859"
FT VARIANT 395
FT /note="L -> P (in dbSNP:rs11136343)"
FT /id="VAR_027860"
FT VARIANT 630
FT /note="V -> A (in dbSNP:rs11544989)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_027861"
FT MUTAGEN 650..690
FT /note="Missing: Decreased interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:24695737"
FT MUTAGEN 831..838
FT /note="QEVVRAFY->AEVARAAA: Abolishes interaction with
FT PCNA."
FT /evidence="ECO:0000269|PubMed:24695737"
FT MUTAGEN 882
FT /note="E->A: Decreased auto-mono-ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:18851833"
FT MUTAGEN 888
FT /note="G->W: Abolishes catalytic activity; abolishes
FT interaction with PARP14."
FT /evidence="ECO:0000269|PubMed:18851833,
FT ECO:0000269|PubMed:23473667, ECO:0000269|PubMed:24695737"
FT MUTAGEN 980..982
FT /note="DCI->ACA: Strongly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:18851833"
FT MUTAGEN 985
FT /note="P->A: Strongly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:18851833"
FT MUTAGEN 987
FT /note="I->E: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:18851833"
FT MUTAGEN 999
FT /note="T->A: Does not affect catalytic activity."
FT /evidence="ECO:0000269|PubMed:18851833"
FT CONFLICT 313
FT /note="M -> I (in Ref. 1; BAB55067)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="P -> S (in Ref. 1; BAB55067)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="L -> P (in Ref. 3; AAH14229)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="R -> K (in Ref. 1; BAB55067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="D -> G (in Ref. 2; BAD96634)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2DHX"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:2DHX"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:2DHX"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2DHX"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2DHX"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2DHX"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2DHX"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2DHX"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:3HKV"
FT HELIX 828..839
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:5LX6"
FT TURN 845..847
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 848..856
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 859..875
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:6FXI"
FT STRAND 883..889
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 894..900
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 904..906
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 916..923
FT /evidence="ECO:0007829|PDB:5LX6"
FT HELIX 924..927
FT /evidence="ECO:0007829|PDB:5LX6"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 941..948
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 952..955
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:3HKV"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 982..984
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 987..990
FT /evidence="ECO:0007829|PDB:5LX6"
FT STRAND 995..1006
FT /evidence="ECO:0007829|PDB:5LX6"
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
