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 27-MAR-2024, entry version 154. DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP16 {ECO:0000305}; DE EC=2.4.2.- {ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:34314702}; 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, GN ECO:0000312|HGNC:HGNC:26040}; GN Synonyms=ARTD15 {ECO:0000303|PubMed:20106667}, C15orf30 GN {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 FUNCTION, CATALYTIC ACTIVITY, AND AUTO-ADP-RIBOSYLATION. RX PubMed=34314702; DOI=10.1016/j.cell.2021.07.005; RA Challa S., Khulpateea B.R., Nandu T., Camacho C.V., Ryu K.W., Chen H., RA Peng Y., Lea J.S., Kraus W.L.; RT "Ribosome ADP-ribosylation inhibits translation and maintains proteostasis RT in cancers."; RL Cell 184:4531-4546(2021). RN [11] 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 plays a role CC in different processes, such as protein translation and unfolded CC protein response (UPR), through the mono-ADP-ribosylation of proteins CC involved in those processes (PubMed:22701565, PubMed:23103912, CC PubMed:25043379, PubMed:34314702). Acts as an inhibitor of protein CC translation by catalyzing mono-ADP-ribosylation of ribosomal subunits, CC such as RPL14 and RPS6, thereby inhibiting polysome assembly and mRNA CC loading (PubMed:34314702). Mono-ADP-ribosylation of ribosomal subunits CC is promoted by NMNAT2 (PubMed:34314702). Involved in the unfolded CC protein response (UPR) by ADP-ribosylating and activating EIF2AK3 and CC ERN1, two important UPR effectors (PubMed:23103912). May also mediate CC mono-ADP-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 ECO:0000269|PubMed:34314702}. 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, ECO:0000269|PubMed:34314702}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; CC Evidence={ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:34314702}; 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, ECO:0000269|PubMed:34314702}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; CC Evidence={ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:34314702}; 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 -!- ACTIVITY REGULATION: In absence of activation signal, PARP16 is CC autoinhibited by the PARP alpha-helical domain (also named HD region), CC which prevents effective NAD(+)-binding (By similarity). Activity is CC highly stimulated by signals, which unfold the PARP alpha-helical CC domain, relieving autoinhibition (By similarity). CC {ECO:0000250|UniProtKB:Q9UGN5}. 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 PARP alpha-helical domain (also named HD region) is CC regulatory, it packs against the catalytic domain. CC {ECO:0000269|PubMed:22661712}. CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:22661712, CC ECO:0000269|PubMed:22701565, ECO:0000269|PubMed:25043379, CC ECO:0000269|PubMed:34314702}. CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS92018.1; -. [Q8N5Y8-1] 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; 58. DR IntAct; Q8N5Y8; 27. 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; 9606-ENSP00000261888; -. DR PeptideAtlas; Q8N5Y8; -. DR ProteomicsDB; 72111; -. [Q8N5Y8-1] DR ProteomicsDB; 72112; -. [Q8N5Y8-2] DR ProteomicsDB; 72113; -. [Q8N5Y8-3] DR Pumba; Q8N5Y8; -. DR Antibodypedia; 25928; 185 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 AGR; HGNC:26040; -. DR CTD; 54956; -. DR DisGeNET; 54956; -. DR GeneCards; PARP16; -. DR HGNC; HGNC:26040; PARP16. DR HPA; ENSG00000138617; Low tissue specificity. DR MIM; 620391; gene. 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; AFLYYWN; -. DR OrthoDB; 5473461at2759; -. 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 1152 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 131 other cell types or tissues. DR ExpressionAtlas; Q8N5Y8; baseline and differential. 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: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:0140806; F:NAD+- protein-aspartate ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:0140804; F:NAD+- protein-lysine ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProt. DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB. DR GO; GO:0019082; P:viral protein processing; TAS:Reactome. DR Gene3D; 3.90.228.10; -; 1. DR InterPro; IPR041400; PARP16_N. DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom. DR PANTHER; PTHR21328; POLY ADP-RIBOSE POLYMERASE FAMILY, MEMBER PARP; 1. DR PANTHER; PTHR21328:SF2; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP16; 1. DR Pfam; PF18084; ARTD15_N; 1. DR Pfam; PF00644; PARP; 1. DR SUPFAM; SSF56399; ADP-ribosylation; 1. DR PROSITE; PS51059; PARP_CATALYTIC; 1. DR Genevisible; Q8N5Y8; HS. 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 //