PAR10_MOUSE
ID PAR10_MOUSE Reviewed; 960 AA.
AC Q8CIE4; F6Z9X8; Q3TLV7; Q3U6C0; Q8BSZ1; Q8C8L6; Q8R133; Q8R1U9;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP10 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q53GL7};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 10 {ECO:0000250|UniProtKB:Q53GL7};
DE Short=ARTD10 {ECO:0000250|UniProtKB:Q53GL7};
DE AltName: Full=Poly [ADP-ribose] polymerase 10 {ECO:0000250|UniProtKB:Q53GL7};
DE Short=PARP-10 {ECO:0000250|UniProtKB:Q53GL7};
GN Name=Parp10 {ECO:0000312|MGI:MGI:3712326};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-960.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Mammary gland, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-960.
RC STRAIN=FVB/N; TISSUE=Eye {ECO:0000312|EMBL:AAH23056.1}, and Liver;
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).
CC -!- FUNCTION: ADP-ribosyltransferase that mediates mono-ADP-ribosylation of
CC glutamate and aspartate residues on target proteins. In contrast to
CC PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation.
CC Catalyzes mono-ADP-ribosylation of GSK3B, leading to negatively
CC regulate GSK3B kinase activity. Involved in translesion DNA synthesis
CC in response to DNA damage via its interaction with PCNA.
CC {ECO:0000250|UniProtKB:Q53GL7}.
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:0000250|UniProtKB:Q53GL7};
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:0000250|UniProtKB:Q53GL7};
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:0000250|UniProtKB:Q53GL7};
CC -!- SUBUNIT: Interacts with MYC. Interacts with PARP14. Interacts (via-PIP
CC box and ubiquitin-interacting motifs) with PCNA.
CC {ECO:0000250|UniProtKB:Q53GL7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at
CC steady state, but shuttles between nucleus and cytoplasm in a XPO1-
CC dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA.
CC {ECO:0000250|UniProtKB:Q53GL7}.
CC -!- PTM: Stimulated through its phosphorylation by CDK2. Acquires CDK-
CC dependent phosphorylation through late-G1 to S phase, and from
CC prometaphase to cytokinesis in the nucleolar organizing regions.
CC Phosphorylation is suppressed in growth-arrested cells.
CC {ECO:0000250|UniProtKB:Q53GL7}.
CC -!- PTM: Auto-mono-ADP-ribosylated on glutamate and lysine residues.
CC {ECO:0000250|UniProtKB:Q53GL7}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25608.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32856.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028373; BAC25913.1; -; mRNA.
DR EMBL; AK046755; BAC32856.1; ALT_FRAME; mRNA.
DR EMBL; AK153205; BAE31805.1; -; mRNA.
DR EMBL; AK166291; BAE38685.1; -; mRNA.
DR EMBL; AC110211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023056; AAH23056.1; -; mRNA.
DR EMBL; BC024074; AAH24074.1; -; mRNA.
DR EMBL; BC025608; AAH25608.1; ALT_INIT; mRNA.
DR CCDS; CCDS49650.1; -.
DR RefSeq; NP_001157047.1; NM_001163575.1.
DR RefSeq; NP_001157048.1; NM_001163576.1.
DR AlphaFoldDB; Q8CIE4; -.
DR SMR; Q8CIE4; -.
DR STRING; 10090.ENSMUSP00000129765; -.
DR iPTMnet; Q8CIE4; -.
DR PhosphoSitePlus; Q8CIE4; -.
DR EPD; Q8CIE4; -.
DR MaxQB; Q8CIE4; -.
DR PaxDb; Q8CIE4; -.
DR PRIDE; Q8CIE4; -.
DR ProteomicsDB; 334670; -.
DR ProteomicsDB; 357507; -.
DR Antibodypedia; 28206; 113 antibodies from 28 providers.
DR Ensembl; ENSMUST00000075689; ENSMUSP00000075110; ENSMUSG00000063268.
DR Ensembl; ENSMUST00000165738; ENSMUSP00000129765; ENSMUSG00000063268.
DR GeneID; 671535; -.
DR KEGG; mmu:671535; -.
DR UCSC; uc007wjj.2; mouse.
DR CTD; 84875; -.
DR MGI; MGI:3712326; Parp10.
DR VEuPathDB; HostDB:ENSMUSG00000063268; -.
DR eggNOG; ENOG502R572; Eukaryota.
DR GeneTree; ENSGT00940000162035; -.
DR HOGENOM; CLU_014825_3_2_1; -.
DR InParanoid; Q8CIE4; -.
DR OMA; QAFYNTL; -.
DR OrthoDB; 681829at2759; -.
DR PhylomeDB; Q8CIE4; -.
DR TreeFam; TF328965; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 671535; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Parp10; mouse.
DR PRO; PR:Q8CIE4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8CIE4; protein.
DR Bgee; ENSMUSG00000063268; Expressed in granulocyte and 118 other tissues.
DR ExpressionAtlas; Q8CIE4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISO:MGI.
DR GO; GO:0010847; P:regulation of chromatin assembly; ISO:MGI.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR CDD; cd12547; RRM1_2_PAR10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034464; PAR10_RRM1_2.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR Pfam; PF00644; PARP; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Cytoplasm; DNA damage; DNA repair; Glycosyltransferase;
KW NAD; Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..960
FT /note="Protein mono-ADP-ribosyltransferase PARP10"
FT /id="PRO_0000446172"
FT DOMAIN 755..960
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 325..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..856
FT /note="Myc binding"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOTIF 604..621
FT /note="Ubiquitin-interacting"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOTIF 780..787
FT /note="PIP-box"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT COMPBIAS 553..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT MOD_RES 831
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:Q53GL7"
FT CONFLICT 255
FT /note="G -> S (in Ref. 1; BAC25913)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="A -> T (in Ref. 1; BAE38685)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="V -> I (in Ref. 1; BAE38685)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="H -> Y (in Ref. 1; BAE38685)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="A -> S (in Ref. 1; BAE38685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 960 AA; 103679 MW; F3106C499027AE9F CRC64;
MAEVEAGAAL ELRGLPPEIP DELITLYFEN HRRSGGGLLL SWQRLGCGGV LIFQDPADAK
RVLAQAEHRL HGVRLSLRPA PPRAPERVLL QHLPPGTSPL SLEQHVQALL GAAGHPVQTC
HALASPRQDC ALVQLSTPLS EAEVSALAEQ ARNLPLNGAT VSLAWVPQTR AVRVVDSASP
VDLLLLELYL ENERRSGGGP LEGLRSLPGQ LGTVISFQQW QVAERVLKQK HWLQGIELSL
VPHYDVLEPE ALAEGVSGRD HSATQESGVI GHAPTGTGGL AGALTMAVGS GEAPQQLGTL
LRAGPVGAPG QALPVDSGSI RIQGSMGSTS PVDPVESSTE LPEQVGPMAS DSVGVQEQEG
LGEVATGQEG LMGLVGTAME SVETGLESPG YGEMQKQEGL VEMVMSVEPG AVRYLQLYYE
DLLASLEDVA LFPLEGTDVT GFRLCGARAP CQAAQELLQS LLGSISCHTL NMKHPGSARF
LLGVEGQHLL HRLEAQFQCV FGTEHLASAT LDIDPERTDP TEALQVLHGH ITGIDQESLR
LEDVRELLAT LESPHGGEDR VPLEMEKEKP GGPGETVVEQ QEEIPTLEAE EEPVALSTGA
RGQLEEEATL QLAIHRSLES QSQVADQQEA NALRRAMALS LLEAEEALDE DTGGEAQLVV
HTSFEQDVDE LNQALSNALE AHLREETVSL QGRMLPPELG ARLERCHDVS ATLRGDRVVL
RGFGVQPARA ARHLAALLVD PWDQNLTFPL EASKPNLSEQ GLKEPLGRLE ALEENSQEFQ
DVVRAFYSTL DAVHGRIRIV RVERVSHPLL QQQYQLHRER LMQSCQQRPV EQVLYHGTSE
SAVLDICAHG FNRSFCGRNG TLYGQGVYFA KRASLSVLDR YSPPNAEGYK AVFVAQVLTG
DYGQGSRGLK APPLRVSGQV LRYDSAVDCL QQPRIFVIFH DTQALPTHLI TCKNILPGTP
