PARPT_HUMAN
ID PARPT_HUMAN Reviewed; 657 AA.
AC Q7Z3E1; D3DNK6; Q68CY9; Q86VP4; Q9Y4P7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein mono-ADP-ribosyltransferase TIPARP {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:30373764};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 14 {ECO:0000303|PubMed:20106667};
DE Short=ARTD14 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 7 {ECO:0000303|PubMed:20106667};
DE Short=PARP-7 {ECO:0000303|PubMed:20106667};
DE AltName: Full=TCDD-inducible poly [ADP-ribose] polymerase {ECO:0000303|PubMed:12851707};
GN Name=TIPARP {ECO:0000303|PubMed:12851707, ECO:0000312|HGNC:HGNC:23696};
GN Synonyms=PARP7 {ECO:0000303|PubMed:20106667};
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].
RC TISSUE=Endometrial tumor, and Testis;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-406.
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 [4]
RP IDENTIFICATION.
RX PubMed=12851707;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human TIPARP gene within the CCNL
RT amplicon at human chromosome 3q25.31.";
RL Int. J. Oncol. 23:541-547(2003).
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, INTERACTION WITH AHR, AND MUTAGENESIS OF
RP CYS-243; HIS-532; TYR-564 AND ILE-631.
RX PubMed=23275542; DOI=10.1093/nar/gks1337;
RA MacPherson L., Tamblyn L., Rajendra S., Bralha F., McPherson J.P.,
RA Matthews J.;
RT "2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP,
RT ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon
RT receptor transactivation.";
RL Nucleic Acids Res. 41:1604-1621(2013).
RN [7]
RP FUNCTION.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP ADP-RIBOSYLATION AT CYS-39, AND MUTAGENESIS OF CYS-39; LYS-41; CYS-243 AND
RP HIS-532.
RX PubMed=30373764; DOI=10.1042/bcj20180347;
RA Gomez A., Bindesboell C., Somisetty V.S., Grimaldi G., Hutin D.,
RA MacPherson L., Ahmed S., Tamblyn L., Cho T., Nebb H.I., Moen A.,
RA Anonsen J.H., Grant D.M., Matthews J.;
RT "Characterization of TCDD-Inducible Poly-ADP-Ribose Polymerase
RT (TIPARP/ARTD14) Catalytic Activity.";
RL Biochem. J. 475:3827-3846(2018).
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate, aspartate and cysteine residues on target proteins
CC (PubMed:23275542, PubMed:25043379, PubMed:30373764). Acts as a negative
CC regulator of AHR by mediating mono-ADP-ribosylation of AHR, leading to
CC inhibit transcription activator activity of AHR (PubMed:23275542,
CC PubMed:30373764). {ECO:0000269|PubMed:23275542,
CC ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:30373764}.
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:30373764};
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:30373764};
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:30373764};
CC -!- ACTIVITY REGULATION: ADP-ribosyltransferase activity is inhibited by
CC PJ34; inhibition is however not specific to TIPARP and other PARP-
CC domain containing proteins are also inhibited by PJ34
CC (PubMed:30373764). Partially inhibited by KU0058948 (PubMed:30373764).
CC {ECO:0000269|PubMed:30373764}.
CC -!- SUBUNIT: Interacts with AHR. {ECO:0000269|PubMed:23275542}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23275542,
CC ECO:0000269|PubMed:30373764}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:30373764}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AL080156; CAB45747.2; -; mRNA.
DR EMBL; BX537965; CAD97929.1; -; mRNA.
DR EMBL; CR749647; CAH18441.1; -; mRNA.
DR EMBL; CH471052; EAW78725.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78728.1; -; Genomic_DNA.
DR EMBL; BC050350; AAH50350.2; -; mRNA.
DR CCDS; CCDS3177.1; -.
DR PIR; T12540; T12540.
DR RefSeq; NP_001171646.1; NM_001184717.1.
DR RefSeq; NP_001171647.1; NM_001184718.1.
DR RefSeq; NP_056323.2; NM_015508.4.
DR AlphaFoldDB; Q7Z3E1; -.
DR SMR; Q7Z3E1; -.
DR BioGRID; 117460; 16.
DR IntAct; Q7Z3E1; 3.
DR MINT; Q7Z3E1; -.
DR STRING; 9606.ENSP00000420612; -.
DR BindingDB; Q7Z3E1; -.
DR ChEMBL; CHEMBL2380188; -.
DR iPTMnet; Q7Z3E1; -.
DR PhosphoSitePlus; Q7Z3E1; -.
DR BioMuta; TIPARP; -.
DR DMDM; 74723283; -.
DR EPD; Q7Z3E1; -.
DR MassIVE; Q7Z3E1; -.
DR PaxDb; Q7Z3E1; -.
DR PeptideAtlas; Q7Z3E1; -.
DR PRIDE; Q7Z3E1; -.
DR ProteomicsDB; 69039; -.
DR Antibodypedia; 33637; 91 antibodies from 24 providers.
DR DNASU; 25976; -.
DR Ensembl; ENST00000295924.12; ENSP00000295924.7; ENSG00000163659.13.
DR Ensembl; ENST00000461166.5; ENSP00000420612.1; ENSG00000163659.13.
DR Ensembl; ENST00000486483.5; ENSP00000418757.1; ENSG00000163659.13.
DR Ensembl; ENST00000542783.5; ENSP00000438345.1; ENSG00000163659.13.
DR GeneID; 25976; -.
DR KEGG; hsa:25976; -.
DR MANE-Select; ENST00000295924.12; ENSP00000295924.7; NM_015508.5; NP_056323.2.
DR UCSC; uc003fav.4; human.
DR CTD; 25976; -.
DR DisGeNET; 25976; -.
DR GeneCards; TIPARP; -.
DR HGNC; HGNC:23696; TIPARP.
DR HPA; ENSG00000163659; Low tissue specificity.
DR MIM; 612480; gene.
DR neXtProt; NX_Q7Z3E1; -.
DR OpenTargets; ENSG00000163659; -.
DR PharmGKB; PA134885396; -.
DR VEuPathDB; HostDB:ENSG00000163659; -.
DR eggNOG; ENOG502QQXA; Eukaryota.
DR GeneTree; ENSGT00940000155368; -.
DR InParanoid; Q7Z3E1; -.
DR OMA; SKKMTGL; -.
DR OrthoDB; 782733at2759; -.
DR PhylomeDB; Q7Z3E1; -.
DR TreeFam; TF328965; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q7Z3E1; -.
DR SignaLink; Q7Z3E1; -.
DR BioGRID-ORCS; 25976; 186 hits in 1079 CRISPR screens.
DR ChiTaRS; TIPARP; human.
DR GeneWiki; TIPARP; -.
DR GenomeRNAi; 25976; -.
DR Pharos; Q7Z3E1; Tbio.
DR PRO; PR:Q7Z3E1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q7Z3E1; protein.
DR Bgee; ENSG00000163659; Expressed in secondary oocyte and 192 other tissues.
DR ExpressionAtlas; Q7Z3E1; baseline and differential.
DR Genevisible; Q7Z3E1; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0008209; P:androgen metabolic process; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA: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:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00644; PARP; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..657
FT /note="Protein mono-ADP-ribosyltransferase TIPARP"
FT /id="PRO_0000247835"
FT DOMAIN 332..410
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 449..657
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 237..264
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:30373764"
FT MOD_RES 39
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:30373764"
FT VARIANT 406
FT /note="R -> S (in dbSNP:rs17854621)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027155"
FT MUTAGEN 39
FT /note="C->A: Slight reduction of auto-mono-ADP-
FT ribosylation."
FT /evidence="ECO:0000269|PubMed:23275542,
FT ECO:0000269|PubMed:30373764"
FT MUTAGEN 41
FT /note="K->A: Partial relocalization to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:30373764"
FT MUTAGEN 243
FT /note="C->A: Relocalization to the cytosol."
FT /evidence="ECO:0000269|PubMed:23275542,
FT ECO:0000269|PubMed:30373764"
FT MUTAGEN 532
FT /note="H->A: Abolishes ADP-ribosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23275542,
FT ECO:0000269|PubMed:30373764"
FT MUTAGEN 564
FT /note="Y->A: Abolishes ADP-ribosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23275542"
FT MUTAGEN 631
FT /note="I->A: Does not affect ADP-ribosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23275542"
FT CONFLICT 43
FT /note="K -> E (in Ref. 1; CAH18441)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="G -> R (in Ref. 1; CAH18441)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="V -> A (in Ref. 1; CAH18441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 76227 MW; 1E63E311F1B36CEB CRC64;
MEMETTEPEP DCVVQPPSPP DDFSCQMRLS EKITPLKTCF KKKDQKRLGT GTLRSLRPIL
NTLLESGSLD GVFRSRNQST DENSLHEPMM KKAMEINSSC PPAENNMSVL IPDRTNVGDQ
IPEAHPSTEA PERVVPIQDH SFPSETLSGT VADSTPAHFQ TDLLHPVSSD VPTSPDCLDK
VIDYVPGIFQ ENSFTIQYIL DTSDKLSTEL FQDKSEEASL DLVFELVNQL QYHTHQENGI
EICMDFLQGT CIYGRDCLKH HTVLPYHWQI KRTTTQKWQS VFNDSQEHLE RFYCNPENDR
MRMKYGGQEF WADLNAMNVY ETTEFDQLRR LSTPPSSNVN SIYHTVWKFF CRDHFGWREY
PESVIRLIEE ANSRGLKEVR FMMWNNHYIL HNSFFRREIK RRPLFRSCFI LLPYLQTLGG
VPTQAPPPLE ATSSSQIICP DGVTSANFYP ETWVYMHPSQ DFIQVPVSAE DKSYRIIYNL
FHKTVPEFKY RILQILRVQN QFLWEKYKRK KEYMNRKMFG RDRIINERHL FHGTSQDVVD
GICKHNFDPR VCGKHATMFG QGSYFAKKAS YSHNFSKKSS KGVHFMFLAK VLTGRYTMGS
HGMRRPPPVN PGSVTSDLYD SCVDNFFEPQ IFVIFNDDQS YPYFVIQYEE VSNTVSI
