PAR16_HUMAN
ID PAR16_HUMAN Reviewed; 322 AA.
AC Q8N5Y8; A0A024R5Y7; Q6PK64; Q9NX03;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP16 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 15 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 16 {ECO:0000303|PubMed:20106667};
DE Short=PARP-16 {ECO:0000303|PubMed:20106667};
GN Name=PARP16 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:26040};
GN Synonyms=ARTD15 {ECO:0000303|PubMed:20106667},
GN C15orf30 {ECO:0000312|HGNC:HGNC:26040};
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] (ISOFORM 2).
RC TISSUE=Carcinoma;
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-280.
RC TISSUE=Brain;
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-152 AND TYR-182.
RX PubMed=23103912; DOI=10.1038/ncb2593;
RA Jwa M., Chang P.;
RT "PARP16 is a tail-anchored endoplasmic reticulum protein required for the
RT PERK-and IRE1alpha-mediated unfolded protein response.";
RL Nat. Cell Biol. 14:1223-1230(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH KPNB1, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF HIS-152 AND TYR-254, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND AUTO-ADP-RIBOSYLATION.
RX PubMed=22701565; DOI=10.1371/journal.pone.0037352;
RA Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M.;
RT "PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-
RT ribosyltransferase that interacts with, and modifies karyopherin-beta1.";
RL PLoS ONE 7:E37352-E37352(2012).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT ASP-37; GLU-70;
RP LYS-110 AND LYS-137.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 5-279 IN COMPLEX WITH NAD ANALOG,
RP AUTO-ADP-RIBOSYLATION, DOMAIN PARP ALPHA-HELICAL, AND NAD-BINDING SITES.
RX PubMed=22661712; DOI=10.1074/jbc.m112.379289;
RA Karlberg T., Thorsell A.G., Kallas A., Schuler H.;
RT "Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a
RT novel putative regulatory domain.";
RL J. Biol. Chem. 287:24077-24081(2012).
CC -!- FUNCTION: Intracellular mono-ADP-ribosyltransferase that may play a
CC role in different processes through the mono-ADP-ribosylation of
CC proteins involved in those processes (PubMed:23103912, PubMed:22701565,
CC PubMed:25043379). May play a role in the unfolded protein response
CC (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two
CC important UPR effectors (PubMed:23103912). May also mediate mono-ADP-
CC ribosylation of karyopherin KPNB1 a nuclear import factor
CC (PubMed:22701565). May not modify proteins on arginine or cysteine
CC residues compared to other mono-ADP-ribosyltransferases
CC (PubMed:22701565). {ECO:0000269|PubMed:22701565,
CC ECO:0000269|PubMed:23103912, 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:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={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-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:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 uM for NAD (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:22701565};
CC Vmax=0.7 pmol/h/ug enzyme (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:22701565};
CC -!- SUBUNIT: Interacts with KPNB1. {ECO:0000269|PubMed:22661712,
CC ECO:0000269|PubMed:22701565}.
CC -!- INTERACTION:
CC Q8N5Y8; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-10266912, EBI-10172181;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23103912}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:22701565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N5Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5Y8-2; Sequence=VSP_020973;
CC Name=3;
CC IsoId=Q8N5Y8-3; Sequence=VSP_020974;
CC -!- DOMAIN: The N-terminal PARP alpha-helical domain is regulatory, it
CC packs against the catalytic domain, and may relay effector-binding
CC event to the NAD-binding site. {ECO:0000269|PubMed:22661712}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:22661712,
CC ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:25043379}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AK000516; BAA91222.1; -; mRNA.
DR EMBL; AC068213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77718.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77720.1; -; Genomic_DNA.
DR EMBL; BC006389; AAH06389.1; -; mRNA.
DR EMBL; BC031074; AAH31074.1; -; mRNA.
DR CCDS; CCDS10204.1; -. [Q8N5Y8-3]
DR CCDS; CCDS81897.1; -. [Q8N5Y8-2]
DR RefSeq; NP_001303872.1; NM_001316943.1. [Q8N5Y8-1]
DR RefSeq; NP_001303873.1; NM_001316944.1. [Q8N5Y8-2]
DR RefSeq; NP_060321.3; NM_017851.5. [Q8N5Y8-3]
DR PDB; 4F0D; X-ray; 2.70 A; A/B=5-279.
DR PDB; 6HXR; X-ray; 2.90 A; A/B/C=5-279.
DR PDB; 6HXS; X-ray; 2.05 A; A/B/C=5-279.
DR PDB; 6W65; X-ray; 2.13 A; A/B/C=5-279.
DR PDBsum; 4F0D; -.
DR PDBsum; 6HXR; -.
DR PDBsum; 6HXS; -.
DR PDBsum; 6W65; -.
DR AlphaFoldDB; Q8N5Y8; -.
DR SMR; Q8N5Y8; -.
DR BioGRID; 120294; 54.
DR IntAct; Q8N5Y8; 25.
DR MINT; Q8N5Y8; -.
DR STRING; 9606.ENSP00000261888; -.
DR BindingDB; Q8N5Y8; -.
DR ChEMBL; CHEMBL4105981; -.
DR iPTMnet; Q8N5Y8; -.
DR PhosphoSitePlus; Q8N5Y8; -.
DR SwissPalm; Q8N5Y8; -.
DR BioMuta; PARP16; -.
DR DMDM; 116248565; -.
DR EPD; Q8N5Y8; -.
DR jPOST; Q8N5Y8; -.
DR MassIVE; Q8N5Y8; -.
DR MaxQB; Q8N5Y8; -.
DR PaxDb; Q8N5Y8; -.
DR PeptideAtlas; Q8N5Y8; -.
DR PRIDE; Q8N5Y8; -.
DR ProteomicsDB; 72111; -. [Q8N5Y8-1]
DR ProteomicsDB; 72112; -. [Q8N5Y8-2]
DR ProteomicsDB; 72113; -. [Q8N5Y8-3]
DR Antibodypedia; 25928; 170 antibodies from 25 providers.
DR DNASU; 54956; -.
DR Ensembl; ENST00000261888.10; ENSP00000261888.6; ENSG00000138617.16. [Q8N5Y8-3]
DR Ensembl; ENST00000444347.2; ENSP00000396118.2; ENSG00000138617.16. [Q8N5Y8-2]
DR Ensembl; ENST00000649807.2; ENSP00000496935.1; ENSG00000138617.16. [Q8N5Y8-1]
DR GeneID; 54956; -.
DR KEGG; hsa:54956; -.
DR MANE-Select; ENST00000649807.2; ENSP00000496935.1; NM_001316943.2; NP_001303872.1.
DR UCSC; uc002aop.4; human. [Q8N5Y8-1]
DR CTD; 54956; -.
DR DisGeNET; 54956; -.
DR GeneCards; PARP16; -.
DR HGNC; HGNC:26040; PARP16.
DR HPA; ENSG00000138617; Low tissue specificity.
DR neXtProt; NX_Q8N5Y8; -.
DR OpenTargets; ENSG00000138617; -.
DR PharmGKB; PA134984504; -.
DR VEuPathDB; HostDB:ENSG00000138617; -.
DR eggNOG; ENOG502QPKE; Eukaryota.
DR GeneTree; ENSGT00950000183129; -.
DR HOGENOM; CLU_053263_1_0_1; -.
DR InParanoid; Q8N5Y8; -.
DR OMA; NSPAFLY; -.
DR OrthoDB; 1618442at2759; -.
DR PhylomeDB; Q8N5Y8; -.
DR TreeFam; TF323413; -.
DR BRENDA; 2.4.2.30; 2681.
DR BRENDA; 2.4.2.31; 2681.
DR PathwayCommons; Q8N5Y8; -.
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; Q8N5Y8; -.
DR BioGRID-ORCS; 54956; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; PARP16; human.
DR GenomeRNAi; 54956; -.
DR Pharos; Q8N5Y8; Tchem.
DR PRO; PR:Q8N5Y8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8N5Y8; protein.
DR Bgee; ENSG00000138617; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q8N5Y8; baseline and differential.
DR Genevisible; Q8N5Y8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI: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:0043539; F:protein serine/threonine kinase activator activity; IMP:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IMP:UniProtKB.
DR GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; 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:0019082; P:viral protein processing; TAS:Reactome.
DR InterPro; IPR041400; PARP16_N.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR Pfam; PF18084; ARTD15_N; 1.
DR Pfam; PF00644; PARP; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; NAD;
KW Nucleotidyltransferase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Unfolded protein response.
FT CHAIN 1..322
FT /note="Protein mono-ADP-ribosyltransferase PARP16"
FT /id="PRO_0000252437"
FT TOPO_DOM 1..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..322
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 5..91
FT /note="PARP alpha-helical"
FT DOMAIN 94..279
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22661712"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22661712"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22661712"
FT SITE 193
FT /note="Nicotinamide-stacking aromate"
FT /evidence="ECO:0000269|PubMed:22661712"
FT MOD_RES 37
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 70
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 110
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 137
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VAR_SEQ 59..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020973"
FT VAR_SEQ 277
FT /note="K -> KS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020974"
FT VARIANT 280
FT /note="S -> P (in dbSNP:rs17852901)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027864"
FT MUTAGEN 152
FT /note="H->A: Loss of ADP-ribosyltransferase activity; when
FT associated with A-254."
FT /evidence="ECO:0000269|PubMed:22701565"
FT MUTAGEN 152
FT /note="H->Q: ADP-ribosyltransferase activity is only 6% of
FT wild-type; when associated with A-182."
FT /evidence="ECO:0000269|PubMed:23103912"
FT MUTAGEN 182
FT /note="Y->A: ADP-ribosyltransferase activity is only 6% of
FT wild-type; when associated with Q-152."
FT /evidence="ECO:0000269|PubMed:23103912"
FT MUTAGEN 254
FT /note="Y->A: Loss of ADP-ribosyltransferase activity; when
FT associated with H-152."
FT /evidence="ECO:0000269|PubMed:22701565"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4F0D"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:6HXS"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6HXS"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:6HXS"
SQ SEQUENCE 322 AA; 36383 MW; DA1C99E8A1305982 CRC64;
MQPSGWAAAR EAAGRDMLAA DLRCSLFASA LQSYKRDSVL RPFPASYARG DCKDFEALLA
DASKLPNLKE LLQSSGDNHK RAWDLVSWIL SSKVLTIHSA GKAEFEKIQK LTGAPHTPVP
APDFLFEIEY FDPANAKFYE TKGERDLIYA FHGSRLENFH SIIHNGLHCH LNKTSLFGEG
TYLTSDLSLA LIYSPHGHGW QHSLLGPILS CVAVCEVIDH PDVKCQTKKK DSKEIDRRRA
RIKHSEGGDI PPKYFVVTNN QLLRVKYLLV YSQKPPKRAS SQLSWFSSHW FTVMISLYLL
LLLIVSVINS SAFQHFWNRA KR
