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Poly [ADP-ribose] polymerase 15 (PARP-15) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 7) (ARTD7) (B-aggressive lymphoma protein 3)

 PAR15_HUMAN             Reviewed;         678 AA.
Q460N3; J3KR47; Q8N1K3;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 2.
28-MAR-2018, entry version 115.
RecName: Full=Poly [ADP-ribose] polymerase 15;
Short=PARP-15;
EC=2.4.2.30 {ECO:0000269|PubMed:25635049};
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 7;
Short=ARTD7;
AltName: Full=B-aggressive lymphoma protein 3;
Name=PARP15; Synonyms=BAL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-678 (ISOFORM 1), AND FUNCTION.
PubMed=16061477; DOI=10.1074/jbc.M505408200;
Aguiar R.C.T., Takeyama K., He C., Kreinbrink K., Shipp M.A.;
"B-aggressive lymphoma family proteins have unique domains that
modulate transcription and exhibit poly(ADP-ribose) polymerase
activity.";
J. Biol. Chem. 280:33756-33765(2005).
[5]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[6]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 481-678.
PubMed=22823910; DOI=10.1021/jm300746d;
Andersson C.D., Karlberg T., Ekblad T., Lindgren A.E., Thorsell A.G.,
Spjut S., Uciechowska U., Niemiec M.S., Wittung-Stafshede P.,
Weigelt J., Elofsson M., Schuler H., Linusson A.;
"Discovery of ligands for ADP-ribosyltransferases via docking-based
virtual screening.";
J. Med. Chem. 55:7706-7718(2012).
[7]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 295-470 IN COMPLEX WITH
SUBSTRATE.
PubMed=23473667; DOI=10.1016/j.str.2012.12.019;
Forst A.H., Karlberg T., Herzog N., Thorsell A.G., Gross A.,
Feijs K.L., Verheugd P., Kursula P., Nijmeijer B., Kremmer E.,
Kleine H., Ladurner A.G., Schuler H., Luscher B.;
"Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8
macrodomains.";
Structure 21:462-475(2013).
[8]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 481-678, FUNCTION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF HIS-559; GLY-560 AND TYR-604.
PubMed=25635049; DOI=10.1074/jbc.M114.630160;
Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
Schuler H.;
"Structural basis for lack of ADP-ribosyltransferase activity in
poly(ADP-ribose) polymerase-13/zinc finger antiviral protein.";
J. Biol. Chem. 290:7336-7344(2015).
-!- FUNCTION: Possesses ADP-ribosyltransferase activity
(PubMed:16061477, PubMed:25635049). Transcriptional repressor
(PubMed:16061477). {ECO:0000269|PubMed:16061477,
ECO:0000269|PubMed:25635049}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397,
ECO:0000269|PubMed:25635049}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q460N3-1; Sequence=Displayed;
Name=2;
IsoId=Q460N3-2; Sequence=VSP_020971, VSP_020972;
-!- SEQUENCE CAUTION:
Sequence=AAY64451.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK097916; BAC05197.1; -; mRNA.
EMBL; BC101703; AAI01704.1; -; mRNA.
EMBL; BC101701; AAI01702.1; -; mRNA.
EMBL; AC092908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DQ063586; AAY64451.1; ALT_INIT; mRNA.
CCDS; CCDS3016.1; -. [Q460N3-2]
CCDS; CCDS46893.1; -. [Q460N3-1]
RefSeq; NP_001106995.1; NM_001113523.2. [Q460N3-1]
RefSeq; NP_001295249.1; NM_001308320.1.
RefSeq; NP_689828.1; NM_152615.2. [Q460N3-2]
UniGene; Hs.120250; -.
PDB; 3BLJ; X-ray; 2.20 A; A/B=481-678.
PDB; 3GEY; X-ray; 2.20 A; A/B/C/D=481-678.
PDB; 3V2B; X-ray; 2.20 A; A=295-470.
PDB; 4F0E; X-ray; 2.40 A; A/B/C/D=481-678.
PDBsum; 3BLJ; -.
PDBsum; 3GEY; -.
PDBsum; 3V2B; -.
PDBsum; 4F0E; -.
ProteinModelPortal; Q460N3; -.
SMR; Q460N3; -.
BioGrid; 127917; 1.
STRING; 9606.ENSP00000417214; -.
BindingDB; Q460N3; -.
ChEMBL; CHEMBL2176778; -.
iPTMnet; Q460N3; -.
PhosphoSitePlus; Q460N3; -.
BioMuta; PARP15; -.
DMDM; 116248564; -.
PaxDb; Q460N3; -.
PeptideAtlas; Q460N3; -.
PRIDE; Q460N3; -.
Ensembl; ENST00000310366; ENSP00000308436; ENSG00000173200. [Q460N3-2]
Ensembl; ENST00000464300; ENSP00000417214; ENSG00000173200. [Q460N3-1]
GeneID; 165631; -.
KEGG; hsa:165631; -.
UCSC; uc003efm.3; human. [Q460N3-1]
CTD; 165631; -.
DisGeNET; 165631; -.
EuPathDB; HostDB:ENSG00000173200.12; -.
GeneCards; PARP15; -.
H-InvDB; HIX0200519; -.
HGNC; HGNC:26876; PARP15.
HPA; HPA075786; -.
MIM; 612066; gene.
neXtProt; NX_Q460N3; -.
OpenTargets; ENSG00000173200; -.
PharmGKB; PA134905094; -.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
GeneTree; ENSGT00760000119084; -.
HOGENOM; HOG000026781; -.
HOVERGEN; HBG082106; -.
InParanoid; Q460N3; -.
KO; K15261; -.
OMA; FPMIGTG; -.
OrthoDB; EOG091G00EB; -.
PhylomeDB; Q460N3; -.
ChiTaRS; PARP15; human.
EvolutionaryTrace; Q460N3; -.
GenomeRNAi; 165631; -.
PRO; PR:Q460N3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000173200; -.
CleanEx; HS_PARP15; -.
ExpressionAtlas; Q460N3; baseline and differential.
Genevisible; Q460N3; HS.
GO; GO:0005634; C:nucleus; IC:UniProtKB.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IMP:UniProtKB.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR002589; Macro_dom.
InterPro; IPR034401; PARP15.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
PANTHER; PTHR14453:SF54; PTHR14453:SF54; 1.
Pfam; PF01661; Macro; 2.
Pfam; PF00644; PARP; 1.
SMART; SM00506; A1pp; 2.
PROSITE; PS51154; MACRO; 2.
PROSITE; PS51059; PARP_CATALYTIC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Glycosyltransferase; NAD; Nucleus; Polymorphism; Reference proteome;
Repeat; Transcription; Transcription regulation; Transferase.
CHAIN 1 678 Poly [ADP-ribose] polymerase 15.
/FTId=PRO_0000252436.
DOMAIN 78 267 Macro 1. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 293 464 Macro 2. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 482 678 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
REGION 312 313 Substrate binding. {ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
REGION 324 325 Substrate binding. {ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
REGION 409 413 Substrate binding. {ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
BINDING 331 331 Substrate. {ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
BINDING 335 335 Substrate; via amide nitrogen.
{ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
BINDING 449 449 Substrate. {ECO:0000244|PDB:3V2B,
ECO:0000269|PubMed:23473667}.
VAR_SEQ 1 234 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020971.
VAR_SEQ 235 256 RPITSPLQEVHFLVYTNDDEGC -> MLQRIGLIFLHNIVV
VSNCFYF (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020972.
VARIANT 337 337 R -> K (in dbSNP:rs6793271).
/FTId=VAR_027862.
VARIANT 521 521 A -> T (in dbSNP:rs34383355).
/FTId=VAR_056658.
VARIANT 628 628 G -> R (in dbSNP:rs12489170).
/FTId=VAR_027863.
MUTAGEN 559 559 H->Y: Abolishes catalytic activity.
{ECO:0000269|PubMed:25635049}.
MUTAGEN 560 560 G->A: Slightly reduces catalytic
activity. Abolishes activity; when
associated with Y-559 and C-604.
{ECO:0000269|PubMed:25635049}.
MUTAGEN 604 604 Y->C: Reduces catalytic activity 20-fold.
Abolishes activity; when associated with
Y-559 and A-560.
{ECO:0000269|PubMed:25635049}.
CONFLICT 42 42 V -> M (in Ref. 4; AAY64451).
{ECO:0000305}.
STRAND 296 301 {ECO:0000244|PDB:3V2B}.
STRAND 304 311 {ECO:0000244|PDB:3V2B}.
HELIX 313 315 {ECO:0000244|PDB:3V2B}.
STRAND 318 325 {ECO:0000244|PDB:3V2B}.
HELIX 335 343 {ECO:0000244|PDB:3V2B}.
HELIX 345 355 {ECO:0000244|PDB:3V2B}.
STRAND 361 366 {ECO:0000244|PDB:3V2B}.
STRAND 370 379 {ECO:0000244|PDB:3V2B}.
HELIX 384 397 {ECO:0000244|PDB:3V2B}.
STRAND 402 405 {ECO:0000244|PDB:3V2B}.
HELIX 417 434 {ECO:0000244|PDB:3V2B}.
STRAND 442 449 {ECO:0000244|PDB:3V2B}.
HELIX 451 461 {ECO:0000244|PDB:3V2B}.
STRAND 493 498 {ECO:0000244|PDB:3BLJ}.
HELIX 504 517 {ECO:0000244|PDB:3BLJ}.
STRAND 520 530 {ECO:0000244|PDB:3BLJ}.
HELIX 531 547 {ECO:0000244|PDB:3BLJ}.
STRAND 548 550 {ECO:0000244|PDB:3BLJ}.
STRAND 554 561 {ECO:0000244|PDB:3BLJ}.
HELIX 563 565 {ECO:0000244|PDB:3BLJ}.
HELIX 566 572 {ECO:0000244|PDB:3BLJ}.
TURN 576 578 {ECO:0000244|PDB:3BLJ}.
STRAND 588 595 {ECO:0000244|PDB:3BLJ}.
HELIX 596 600 {ECO:0000244|PDB:3BLJ}.
TURN 602 604 {ECO:0000244|PDB:3BLJ}.
STRAND 613 621 {ECO:0000244|PDB:3BLJ}.
STRAND 624 627 {ECO:0000244|PDB:3BLJ}.
STRAND 637 639 {ECO:0000244|PDB:3BLJ}.
STRAND 642 646 {ECO:0000244|PDB:3GEY}.
STRAND 648 652 {ECO:0000244|PDB:3BLJ}.
STRAND 654 656 {ECO:0000244|PDB:3BLJ}.
STRAND 658 662 {ECO:0000244|PDB:3BLJ}.
STRAND 667 677 {ECO:0000244|PDB:3BLJ}.
SEQUENCE 678 AA; 74576 MW; E299386DA4B2BF8C CRC64;
MAAPGPLPAA ALSPGAPTPR ELMHGVAGVT SRAGRDREAG SVLPAGNRGA RKASRRSSSR
SMSRDNKFSK KDCLSIRNVV ASIQTKEGLN LKLISGDVLY IWADVIVNSV PMNLQLGGGP
LSRAFLQKAG PMLQKELDDR RRETEEKVGN IFMTSGCNLD CKAVLHAVAP YWNNGAETSW
QIMANIIKKC LTTVEVLSFS SITFPMIGTG SLQFPKAVFA KLILSEVFEY SSSTRPITSP
LQEVHFLVYT NDDEGCQAFL DEFTNWSRIN PNKARIPMAG DTQGVVGTVS KPCFTAYEMK
IGAITFQVAT GDIATEQVDV IVNSTARTFN RKSGVSRAIL EGAGQAVESE CAVLAAQPHR
DFIITPGGCL KCKIIIHVPG GKDVRKTVTS VLEECEQRKY TSVSLPAIGT GNAGKNPITV
ADNIIDAIVD FSSQHSTPSL KTVKVVIFQP ELLNIFYDSM KKRDLSASLN FQSTFSMTTC
NLPEHWTDMN HQLFCMVQLE PGQSEYNTIK DKFTRTCSSY AIEKIERIQN AFLWQSYQVK
KRQMDIKNDH KNNERLLFHG TDADSVPYVN QHGFNRSCAG KNAVSYGKGT YFAVDASYSA
KDTYSKPDSN GRKHMYVVRV LTGVFTKGRA GLVTPPPKNP HNPTDLFDSV TNNTRSPKLF
VVFFDNQAYP EYLITFTA


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E0947c ELISA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947c ELISA kit ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947c CLIA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T


 

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