PARP6_HUMAN
ID PARP6_HUMAN Reviewed; 630 AA.
AC Q2NL67; Q9H7C5; Q9H9X6; Q9HAF3; Q9NPS6; Q9UFG4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP6 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 17;
DE Short=ARTD17;
DE AltName: Full=Poly [ADP-ribose] polymerase 6;
DE Short=PARP-6;
GN Name=PARP6 {ECO:0000312|HGNC:HGNC:26921};
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] (ISOFORMS 2 AND 3).
RC TISSUE=Coronary artery, Embryo, and Teratocarcinoma;
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] (ISOFORM 1).
RC TISSUE=PNS;
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 64-630 (ISOFORM 1).
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-630 (ISOFORM 2).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT CYS-237 AND ASP-600.
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).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2NL67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2NL67-2; Sequence=VSP_020965, VSP_020966;
CC Name=3;
CC IsoId=Q2NL67-3; Sequence=VSP_020963, VSP_020964;
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=BAB14969.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB59261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK021790; BAB13896.1; -; mRNA.
DR EMBL; AK022547; BAB14092.1; -; mRNA.
DR EMBL; AK024703; BAB14969.1; ALT_INIT; mRNA.
DR EMBL; BC110902; AAI10903.1; -; mRNA.
DR EMBL; AL122091; CAB59261.1; ALT_INIT; mRNA.
DR EMBL; AL390093; CAB98250.1; -; mRNA.
DR CCDS; CCDS10241.2; -. [Q2NL67-1]
DR PIR; T34522; T34522.
DR RefSeq; NP_001310451.1; NM_001323522.1. [Q2NL67-1]
DR RefSeq; NP_001310461.1; NM_001323532.1. [Q2NL67-1]
DR RefSeq; NP_064599.2; NM_020214.3. [Q2NL67-1]
DR AlphaFoldDB; Q2NL67; -.
DR SMR; Q2NL67; -.
DR BioGRID; 121286; 12.
DR STRING; 9606.ENSP00000456348; -.
DR BindingDB; Q2NL67; -.
DR ChEMBL; CHEMBL2380187; -.
DR iPTMnet; Q2NL67; -.
DR PhosphoSitePlus; Q2NL67; -.
DR BioMuta; PARP6; -.
DR DMDM; 116248567; -.
DR MassIVE; Q2NL67; -.
DR PaxDb; Q2NL67; -.
DR PeptideAtlas; Q2NL67; -.
DR PRIDE; Q2NL67; -.
DR ProteomicsDB; 61417; -. [Q2NL67-1]
DR ProteomicsDB; 61418; -. [Q2NL67-2]
DR ProteomicsDB; 61419; -. [Q2NL67-3]
DR Antibodypedia; 14201; 169 antibodies from 26 providers.
DR DNASU; 56965; -.
DR Ensembl; ENST00000260376.11; ENSP00000260376.7; ENSG00000137817.17. [Q2NL67-2]
DR Ensembl; ENST00000287196.13; ENSP00000287196.9; ENSG00000137817.17. [Q2NL67-1]
DR Ensembl; ENST00000569795.6; ENSP00000456348.1; ENSG00000137817.17. [Q2NL67-1]
DR GeneID; 56965; -.
DR KEGG; hsa:56965; -.
DR MANE-Select; ENST00000569795.6; ENSP00000456348.1; NM_001323532.2; NP_001310461.1.
DR UCSC; uc002auc.4; human. [Q2NL67-1]
DR CTD; 56965; -.
DR DisGeNET; 56965; -.
DR GeneCards; PARP6; -.
DR HGNC; HGNC:26921; PARP6.
DR HPA; ENSG00000137817; Low tissue specificity.
DR MIM; 619439; gene.
DR neXtProt; NX_Q2NL67; -.
DR OpenTargets; ENSG00000137817; -.
DR PharmGKB; PA134900863; -.
DR VEuPathDB; HostDB:ENSG00000137817; -.
DR eggNOG; ENOG502QPRC; Eukaryota.
DR GeneTree; ENSGT00950000183129; -.
DR InParanoid; Q2NL67; -.
DR OMA; QDIKGQY; -.
DR OrthoDB; 268345at2759; -.
DR PhylomeDB; Q2NL67; -.
DR TreeFam; TF323413; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q2NL67; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR BioGRID-ORCS; 56965; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; PARP6; human.
DR GenomeRNAi; 56965; -.
DR Pharos; Q2NL67; Tchem.
DR PRO; PR:Q2NL67; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q2NL67; protein.
DR Bgee; ENSG00000137817; Expressed in cortical plate and 202 other tissues.
DR ExpressionAtlas; Q2NL67; baseline and differential.
DR Genevisible; Q2NL67; 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:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
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 Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..630
FT /note="Protein mono-ADP-ribosyltransferase PARP6"
FT /id="PRO_0000252430"
FT DOMAIN 394..620
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT MOD_RES 237
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 600
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VAR_SEQ 373..388
FT /note="NPKKKNYERLQKALDS -> MVELDPRTTPHSDGPD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020963"
FT VAR_SEQ 389..630
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020964"
FT VAR_SEQ 498..518
FT /note="LHGAAYGKGIYLSPISSISFG -> EWEKDSTGCPPRMSWSRDTTG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_020965"
FT VAR_SEQ 519..630
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_020966"
FT CONFLICT 29
FT /note="S -> N (in Ref. 1; BAB14092)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="E -> G (in Ref. 1; BAB13896)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="S -> N (in Ref. 1; BAB14969)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="R -> RQ (in Ref. 1; BAB14092 and 4; CAB98250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 71115 MW; 5762F55F59AA9873 CRC64;
MDIKGQFWND DDSEGDNESE EFLYGVQGSC AADLYRHPQL DADIEAVKEI YSENSVSIRE
YGTIDDVDID LHINISFLDE EVSTAWKVLR TEPIVLRLRF SLSQYLDGPE PSIEVFQPSN
KEGFGLGLQL KKILGMFTSQ QWKHLSNDFL KTQQEKRHSW FKASGTIKKF RAGLSIFSPI
PKSPSFPIIQ DSMLKGKLGV PELRVGRLMN RSISCTMKNP KVEVFGYPPS PQAGLLCPQH
VGLPPPARTS PLVSGHCKNI PTLEYGFLVQ IMKYAEQRIP TLNEYCVVCD EQHVFQNGSM
LKPAVCTREL CVFSFYTLGV MSGAAEEVAT GAEVVDLLVA MCRAALESPR KSIIFEPYPS
VVDPTDPKTL AFNPKKKNYE RLQKALDSVM SIREMTQGSY LEIKKQMDKL DPLAHPLLQW
IISSNRSHIV KLPLSRLKFM HTSHQFLLLS SPPAKEARFR TAKKLYGSTF AFHGSHIENW
HSILRNGLVN ASYTKLQLHG AAYGKGIYLS PISSISFGYS GMGKGQHRMP SKDELVQRYN
RMNTIPQTRS IQSRFLQSRN LNCIALCEVI TSKDLQKHGN IWVCPVSDHV CTRFFFVYED
GQVGDANINT QDPKIQKEIM RVIGTQVYTN
