PAR11_HUMAN
ID PAR11_HUMAN Reviewed; 338 AA.
AC Q9NR21; B4DRQ0; F8WBZ7; Q68DS1; Q8N5Y9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP11 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 11 {ECO:0000303|PubMed:20106667};
DE Short=ARTD11 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 11 {ECO:0000303|PubMed:20106667};
DE Short=PARP-11 {ECO:0000303|PubMed:20106667};
GN Name=PARP11 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:1186};
GN Synonyms=C12orf6;
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 [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RA Lorenz B., Strom T.M.;
RT "Transcripts in human map region 12p13.3.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Bone marrow, and 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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT GLU-13; LYS-18;
RP CYS-56; CYS-72 AND ASP-87.
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 FUNCTION, SUBCELLULAR LOCATION, MONO-ADP-RIBOSYLATION, AND MUTAGENESIS OF
RP TYR-38; PHE-48; TYR-84; GLN-93; ARG-102 AND GLY-205.
RX PubMed=25673562; DOI=10.1095/biolreprod.114.123661;
RA Meyer-Ficca M.L., Ihara M., Bader J.J., Leu N.A., Beneke S., Meyer R.G.;
RT "Spermatid head elongation with normal nuclear shaping requires ADP-
RT ribosyltransferase PARP11 (ARTD11) in mice.";
RL Biol. Reprod. 92:80-80(2015).
RN [10]
RP STRUCTURE BY NMR OF 22-110.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of WWE domain in poly (ADP-ribose) polymerase family,
RT member 11 (PARP11).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins (PubMed:25043379, PubMed:25673562).
CC Plays a role in nuclear envelope stability and nuclear remodeling
CC during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:Q8CFF0,
CC ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:25673562}.
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-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 -!- 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 -!- 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 -!- INTERACTION:
CC Q9NR21-1; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-17644640, EBI-2340258;
CC Q9NR21-1; Q969Y2: GTPBP3; NbExp=7; IntAct=EBI-17644640, EBI-740290;
CC Q9NR21-1; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-17644640, EBI-10961706;
CC Q9NR21-1; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-17644640, EBI-12039345;
CC Q9NR21-1; Q969G2: LHX4; NbExp=3; IntAct=EBI-17644640, EBI-2865388;
CC Q9NR21-5; P07550: ADRB2; NbExp=3; IntAct=EBI-17159452, EBI-491169;
CC Q9NR21-5; P28329-3: CHAT; NbExp=3; IntAct=EBI-17159452, EBI-25837549;
CC Q9NR21-5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-17159452, EBI-10976677;
CC Q9NR21-5; P22607: FGFR3; NbExp=3; IntAct=EBI-17159452, EBI-348399;
CC Q9NR21-5; Q14957: GRIN2C; NbExp=3; IntAct=EBI-17159452, EBI-8285963;
CC Q9NR21-5; P28799: GRN; NbExp=3; IntAct=EBI-17159452, EBI-747754;
CC Q9NR21-5; P06396: GSN; NbExp=3; IntAct=EBI-17159452, EBI-351506;
CC Q9NR21-5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-17159452, EBI-1055254;
CC Q9NR21-5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-17159452, EBI-10975473;
CC Q9NR21-5; O60260-5: PRKN; NbExp=3; IntAct=EBI-17159452, EBI-21251460;
CC Q9NR21-5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17159452, EBI-396669;
CC Q9NR21-5; P37840: SNCA; NbExp=3; IntAct=EBI-17159452, EBI-985879;
CC Q9NR21-5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-17159452, EBI-5235340;
CC Q9NR21-5; Q13148: TARDBP; NbExp=3; IntAct=EBI-17159452, EBI-372899;
CC Q9NR21-5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-17159452, EBI-12806590;
CC Q9NR21-5; Q9Y649; NbExp=3; IntAct=EBI-17159452, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:25673562}. Note=Colocalizes with NUP153 at nuclear
CC pores. {ECO:0000269|PubMed:25673562}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NR21-4; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR21-2; Sequence=VSP_059435, VSP_059437;
CC Name=3;
CC IsoId=Q9NR21-1; Sequence=VSP_059436;
CC Name=4;
CC IsoId=Q9NR21-5; Sequence=VSP_059438, VSP_059439;
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:25043379,
CC ECO:0000269|PubMed:25673562}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17569.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH31073.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF263540; AAF91391.1; -; mRNA.
DR EMBL; AK299372; BAG61362.1; -; mRNA.
DR EMBL; CR749294; CAH18149.1; -; mRNA.
DR EMBL; AC005842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88853.1; -; Genomic_DNA.
DR EMBL; BC017569; AAH17569.1; ALT_INIT; mRNA.
DR EMBL; BC031073; AAH31073.1; ALT_INIT; mRNA.
DR CCDS; CCDS66281.1; -. [Q9NR21-2]
DR CCDS; CCDS8523.2; -. [Q9NR21-4]
DR RefSeq; NP_001273450.1; NM_001286521.1. [Q9NR21-2]
DR RefSeq; NP_001273451.1; NM_001286522.1. [Q9NR21-2]
DR RefSeq; NP_065100.2; NM_020367.5. [Q9NR21-4]
DR RefSeq; XP_005253768.1; XM_005253711.4.
DR RefSeq; XP_011519272.1; XM_011520970.1. [Q9NR21-1]
DR RefSeq; XP_011519273.1; XM_011520971.2.
DR RefSeq; XP_011519275.1; XM_011520973.2. [Q9NR21-1]
DR RefSeq; XP_016875159.1; XM_017019670.1.
DR RefSeq; XP_016875160.1; XM_017019671.1. [Q9NR21-2]
DR PDB; 2DK6; NMR; -; A=22-110.
DR PDBsum; 2DK6; -.
DR AlphaFoldDB; Q9NR21; -.
DR SMR; Q9NR21; -.
DR BioGRID; 121365; 17.
DR IntAct; Q9NR21; 28.
DR STRING; 9606.ENSP00000228820; -.
DR BindingDB; Q9NR21; -.
DR ChEMBL; CHEMBL2380189; -.
DR GlyGen; Q9NR21; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; Q9NR21; -.
DR BioMuta; PARP11; -.
DR DMDM; 74734315; -.
DR MassIVE; Q9NR21; -.
DR PaxDb; Q9NR21; -.
DR PeptideAtlas; Q9NR21; -.
DR PRIDE; Q9NR21; -.
DR ProteomicsDB; 30979; -.
DR ProteomicsDB; 82256; -. [Q9NR21-1]
DR ProteomicsDB; 82258; -. [Q9NR21-4]
DR Antibodypedia; 10533; 135 antibodies from 28 providers.
DR DNASU; 57097; -.
DR Ensembl; ENST00000228820.9; ENSP00000228820.4; ENSG00000111224.14. [Q9NR21-4]
DR Ensembl; ENST00000416739.5; ENSP00000392392.1; ENSG00000111224.14. [Q9NR21-5]
DR Ensembl; ENST00000427057.6; ENSP00000397058.2; ENSG00000111224.14. [Q9NR21-2]
DR Ensembl; ENST00000447133.7; ENSP00000405385.3; ENSG00000111224.14. [Q9NR21-2]
DR GeneID; 57097; -.
DR KEGG; hsa:57097; -.
DR MANE-Select; ENST00000228820.9; ENSP00000228820.4; NM_020367.6; NP_065100.2.
DR UCSC; uc001qml.4; human. [Q9NR21-4]
DR CTD; 57097; -.
DR DisGeNET; 57097; -.
DR GeneCards; PARP11; -.
DR HGNC; HGNC:1186; PARP11.
DR HPA; ENSG00000111224; Low tissue specificity.
DR MIM; 616706; gene.
DR neXtProt; NX_Q9NR21; -.
DR OpenTargets; ENSG00000111224; -.
DR PharmGKB; PA25507; -.
DR VEuPathDB; HostDB:ENSG00000111224; -.
DR eggNOG; ENOG502QT2S; Eukaryota.
DR GeneTree; ENSGT00940000156857; -.
DR HOGENOM; CLU_014825_1_0_1; -.
DR InParanoid; Q9NR21; -.
DR OMA; TWNPRIF; -.
DR OrthoDB; 782733at2759; -.
DR PhylomeDB; Q9NR21; -.
DR TreeFam; TF338389; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q9NR21; -.
DR SignaLink; Q9NR21; -.
DR BioGRID-ORCS; 57097; 33 hits in 1081 CRISPR screens.
DR ChiTaRS; PARP11; human.
DR EvolutionaryTrace; Q9NR21; -.
DR GenomeRNAi; 57097; -.
DR Pharos; Q9NR21; Tbio.
DR PRO; PR:Q9NR21; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NR21; protein.
DR Bgee; ENSG00000111224; Expressed in buccal mucosa cell and 159 other tissues.
DR ExpressionAtlas; Q9NR21; baseline and differential.
DR Genevisible; Q9NR21; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006998; P:nuclear envelope organization; IEA:Ensembl.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Differentiation;
KW Glycosyltransferase; mRNA transport; NAD; Nuclear pore complex;
KW Nucleotidyltransferase; Nucleus; Protein transport; Reference proteome;
KW Spermatogenesis; Transferase; Translocation; Transport.
FT CHAIN 1..338
FT /note="Protein mono-ADP-ribosyltransferase PARP11"
FT /id="PRO_0000273419"
FT DOMAIN 22..106
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 123..338
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT MOD_RES 13
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 18
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 56
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 72
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 87
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /id="VSP_059435"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 3)"
FT /id="VSP_059436"
FT VAR_SEQ 82..89
FT /note="FSYKIDFA -> MWEVAHVS (in isoform 2)"
FT /id="VSP_059437"
FT VAR_SEQ 234..239
FT /note="GTYFAR -> DNMWKL (in isoform 4)"
FT /id="VSP_059438"
FT VAR_SEQ 240..338
FT /note="Missing (in isoform 4)"
FT /id="VSP_059439"
FT MUTAGEN 38
FT /note="Y->A: No effect on subcellular location at the
FT nuclear envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT MUTAGEN 48
FT /note="F->A: No effect on subcellular location at the
FT nuclear envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT MUTAGEN 84
FT /note="Y->A: Loss of subcellular location at the nuclear
FT envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT MUTAGEN 93
FT /note="Q->A: Loss of subcellular location at the nuclear
FT envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT MUTAGEN 102
FT /note="R->A: Loss of subcellular location at the nuclear
FT envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT MUTAGEN 205
FT /note="G->W: No effect on subcellular location at the
FT nuclear envelope."
FT /evidence="ECO:0000269|PubMed:25673562"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2DK6"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2DK6"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2DK6"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2DK6"
SQ SEQUENCE 338 AA; 39597 MW; 2019EB49823BB08F CRC64;
MWEANPEMFH KAEELFSKTT NNEVDDMDTS DTQWGWFYLA ECGKWHMFQP DTNSQCSVSS
EDIEKSFKTN PCGSISFTTS KFSYKIDFAE MKQMNLTTGK QRLIKRAPFS ISAFSYICEN
EAIPMPPHWE NVNTQVPYQL IPLHNQTHEY NEVANLFGKT MDRNRIKRIQ RIQNLDLWEF
FCRKKAQLKK KRGVPQINEQ MLFHGTSSEF VEAICIHNFD WRINGIHGAV FGKGTYFARD
AAYSSRFCKD DIKHGNTFQI HGVSLQQRHL FRTYKSMFLA RVLIGDYING DSKYMRPPSK
DGSYVNLYDS CVDDTWNPKI FVVFDANQIY PEYLIDFH
