PARP8_HUMAN
ID PARP8_HUMAN Reviewed; 854 AA.
AC Q8N3A8; Q3KRB7; Q6DHZ1; Q9H754;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP8 {ECO:0000305};
DE EC=2.4.2.-;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 16 {ECO:0000303|PubMed:20106667};
DE Short=ARTD16 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 8 {ECO:0000303|PubMed:20106667};
DE Short=PARP-8 {ECO:0000303|PubMed:20106667};
GN Name=PARP8 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:26124};
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 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas, and Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-854 (ISOFORM 1).
RC TISSUE=Colon;
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT CYS-332; CYS-367;
RP CYS-376 AND CYS-395.
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-777.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000269|PubMed:25043379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-
CC D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:140607; Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56613;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N3A8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3A8-2; Sequence=VSP_020970;
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:25043379}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05790.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL834477; CAD39136.1; -; mRNA.
DR EMBL; BC075801; AAH75801.1; -; mRNA.
DR EMBL; BC105789; AAI05790.1; ALT_SEQ; mRNA.
DR EMBL; AK024961; BAB15044.1; -; mRNA.
DR CCDS; CCDS3954.1; -. [Q8N3A8-1]
DR CCDS; CCDS54849.1; -. [Q8N3A8-2]
DR RefSeq; NP_001171526.1; NM_001178055.1. [Q8N3A8-1]
DR RefSeq; NP_001171527.1; NM_001178056.1. [Q8N3A8-2]
DR RefSeq; NP_078891.2; NM_024615.3. [Q8N3A8-1]
DR RefSeq; XP_011541933.1; XM_011543631.2. [Q8N3A8-1]
DR RefSeq; XP_011541934.2; XM_011543632.2. [Q8N3A8-2]
DR AlphaFoldDB; Q8N3A8; -.
DR BioGRID; 122793; 14.
DR IntAct; Q8N3A8; 11.
DR MINT; Q8N3A8; -.
DR STRING; 9606.ENSP00000281631; -.
DR BindingDB; Q8N3A8; -.
DR ChEMBL; CHEMBL3091262; -.
DR iPTMnet; Q8N3A8; -.
DR PhosphoSitePlus; Q8N3A8; -.
DR BioMuta; PARP8; -.
DR DMDM; 74714811; -.
DR EPD; Q8N3A8; -.
DR jPOST; Q8N3A8; -.
DR MassIVE; Q8N3A8; -.
DR MaxQB; Q8N3A8; -.
DR PaxDb; Q8N3A8; -.
DR PeptideAtlas; Q8N3A8; -.
DR PRIDE; Q8N3A8; -.
DR ProteomicsDB; 71784; -. [Q8N3A8-1]
DR ProteomicsDB; 71785; -. [Q8N3A8-2]
DR Antibodypedia; 23287; 133 antibodies from 22 providers.
DR DNASU; 79668; -.
DR Ensembl; ENST00000281631.10; ENSP00000281631.4; ENSG00000151883.19. [Q8N3A8-1]
DR Ensembl; ENST00000505697.6; ENSP00000422217.2; ENSG00000151883.19. [Q8N3A8-1]
DR Ensembl; ENST00000514067.6; ENSP00000424814.2; ENSG00000151883.19. [Q8N3A8-2]
DR GeneID; 79668; -.
DR KEGG; hsa:79668; -.
DR MANE-Select; ENST00000281631.10; ENSP00000281631.4; NM_024615.4; NP_078891.2.
DR UCSC; uc003jon.5; human. [Q8N3A8-1]
DR CTD; 79668; -.
DR DisGeNET; 79668; -.
DR GeneCards; PARP8; -.
DR HGNC; HGNC:26124; PARP8.
DR HPA; ENSG00000151883; Tissue enhanced (bone).
DR neXtProt; NX_Q8N3A8; -.
DR OpenTargets; ENSG00000151883; -.
DR PharmGKB; PA134903201; -.
DR VEuPathDB; HostDB:ENSG00000151883; -.
DR eggNOG; ENOG502QPRC; Eukaryota.
DR GeneTree; ENSGT00950000183129; -.
DR HOGENOM; CLU_021399_0_0_1; -.
DR InParanoid; Q8N3A8; -.
DR OMA; AKCVPIR; -.
DR OrthoDB; 268345at2759; -.
DR PhylomeDB; Q8N3A8; -.
DR TreeFam; TF323413; -.
DR PathwayCommons; Q8N3A8; -.
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; Q8N3A8; -.
DR BioGRID-ORCS; 79668; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; PARP8; human.
DR GeneWiki; PARP8; -.
DR GenomeRNAi; 79668; -.
DR Pharos; Q8N3A8; Tdark.
DR PRO; PR:Q8N3A8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N3A8; protein.
DR Bgee; ENSG00000151883; Expressed in granulocyte and 172 other tissues.
DR ExpressionAtlas; Q8N3A8; baseline and differential.
DR Genevisible; Q8N3A8; HS.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
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 ADP-ribosylation; Alternative splicing; Glycosyltransferase; NAD;
KW Reference proteome; Transferase.
FT CHAIN 1..854
FT /note="Protein mono-ADP-ribosyltransferase PARP8"
FT /id="PRO_0000252433"
FT DOMAIN 617..844
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 113..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 367
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 376
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 395
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VAR_SEQ 557..598
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020970"
FT VARIANT 777
FT /note="S -> A (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035853"
FT CONFLICT 849
FT /note="N -> D (in Ref. 3; BAB15044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 95871 MW; D3287F5F46BA2B63 CRC64;
MGMCSRQERI QKDIDVVIQK SRAEKDCLFA DFRYSDSTFT FTYVGGPRSV SYSVHVSEDY
PDNTYVSSSE NDEDVLVTTE PIPVIFHRIA TELRKTNDIN CCLSIKSKLQ KENGEESRQN
STVEEDSEGD NDSEEFYYGG QVNYDGELHK HPQLEADLSA VREIYGPHAV SLREYGAIDD
VDIDLHIDVS FLDEEIAVAW EVIRTEPIIV RLHCSLTQYL NGPVPTVDVF QISTKERFGL
GHQLKKIMQT FVTQQWKQSK EKSNCLHNKK LSEKKVKSPL HLFSTLRRSP SYPPPGCGKS
KSKLKSEQDG ISKTHKLLRR TCSSTVKTDD VCVTKSHRTF GRSLSSDPRA EQAMTAIKSH
KLLNRPCPAA VKSEECLTLK SHRLLTRSCS GDPRCEHNTN LKPHKLLSRS YSSNLRMEEL
YGLKNHKLLS KSYSSAPKSS KTELFKEPNA EGRRLSLTSG LIGILTPSSS SSSQLAPNGA
KCIPVRDRGF LVQTIEFAEQ RIPVLNEYCV VCDEPHVFQN GPMLRPTVCE RELCVFAFQT
LGVMNEAADE IATGAQVVDL LVSMCRSALE SPRKVVIFEP YPSVVDPNDP QMLAFNPRKK
NYDRVMKALD SITSIREMTQ APYLEIKKQM DKQDPLAHPL LQWVISSNRS HIVKLPVNRQ
LKFMHTPHQF LLLSSPPAKE SNFRAAKKLF GSTFAFHGSH IENWHSILRN GLVVASNTRL
QLHGAMYGSG IYLSPMSSIS FGYSGMNKKQ KVSAKDEPAS SSKSSNTSQS QKKGQQSQFL
QSRNLKCIAL CEVITSSDLH KHGEIWVVPN TDHVCTRFFF VYEDGQVGDA NINTQEGGIH
KEILRVIGNQ TATG
