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Poly [ADP-ribose] polymerase 14 (PARP-14) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 8) (ARTD8) (B aggressive lymphoma protein 2)

 PAR14_HUMAN             Reviewed;        1801 AA.
Q460N5; B4E2H0; Q460N4; Q8J027; Q9H9X9; Q9NV60; Q9ULF2;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 3.
18-JUL-2018, entry version 123.
RecName: Full=Poly [ADP-ribose] polymerase 14;
Short=PARP-14;
EC=2.4.2.30 {ECO:0000255|PROSITE-ProRule:PRU00397, ECO:0000269|PubMed:16061477, ECO:0000269|PubMed:27796300};
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 8;
Short=ARTD8;
AltName: Full=B aggressive lymphoma protein 2;
Name=PARP14; Synonyms=BAL2, KIAA1268;
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 3).
TISSUE=Ovary;
Guo J.H., Yu L.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[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] OF 1-1560 (ISOFORMS 1 AND 5),
AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1380-1801 (ISOFORMS
1/3/6).
TISSUE=Ovarian carcinoma, Teratocarcinoma, and Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-266 (ISOFORM 1).
TISSUE=Trachea;
PubMed=16344560; DOI=10.1101/gr.4039406;
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
"Diversification of transcriptional modulation: large-scale
identification and characterization of putative alternative promoters
of human genes.";
Genome Res. 16:55-65(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 160-1801 (ISOFORM 4), NUCLEOTIDE
SEQUENCE [MRNA] OF 160-1801 (ISOFORM 1), ALTERNATIVE SPLICING,
FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 658-1801 (ISOFORM 4).
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[7]
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-1411, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1403, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARP9, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INDUCTION, AND ADP-RIBOSYLATION.
PubMed=27796300; DOI=10.1038/ncomms12849;
Iwata H., Goettsch C., Sharma A., Ricchiuto P., Goh W.W., Halu A.,
Yamada I., Yoshida H., Hara T., Wei M., Inoue N., Fukuda D.,
Mojcher A., Mattson P.C., Barabasi A.L., Boothby M., Aikawa E.,
Singh S.A., Aikawa M.;
"PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-
ribosylation.";
Nat. Commun. 7:12849-12849(2016).
[12]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1611-1801.
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).
[13]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1611-1801.
PubMed=22343925; DOI=10.1038/nbt.2121;
Wahlberg E., Karlberg T., Kouznetsova E., Markova N., Macchiarulo A.,
Thorsell A.G., Pol E., Frostell A., Ekblad T., Oncu D., Kull B.,
Robertson G.M., Pellicciari R., Schuler H., Weigelt J.;
"Family-wide chemical profiling and structural analysis of PARP and
tankyrase inhibitors.";
Nat. Biotechnol. 30:283-288(2012).
[14]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 784-1196 AND 1208-1388 IN
COMPLEX WITH SUBSTRATE, INTERACTION WITH PARP10, AND MUTAGENESIS OF
GLY-1055.
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).
-!- FUNCTION: ADP-ribosyltransferase (PubMed:16061477,
PubMed:27796300). By mono-ADP-ribosylating STAT1 at 'Glu-657' and
'Glu-705' and thus decreasing STAT1 phosphorylation, negatively
regulates pro-inflammatory cytokines production in macrophages in
response to IFNG stimulation (PubMed:27796300). Mono-ADP-
ribosylates STAT6 (By similarity). Enhances STAT6-dependent
transcription (By similarity). In macrophages, positively
regulates MRC1 expression in response to IL4 stimulation by
promoting STAT6 phosphorylation (PubMed:27796300). Mono-ADP-
ribosylates PARP9 (PubMed:27796300).
{ECO:0000250|UniProtKB:Q2EMV9, ECO:0000269|PubMed:16061477,
ECO:0000269|PubMed:27796300}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397,
ECO:0000269|PubMed:16061477, ECO:0000269|PubMed:27796300}.
-!- SUBUNIT: Interacts with STAT6 (By similarity). Interacts with
PARP10 (PubMed:23473667). Interacts with PARP9 in IFNG-stimulated
macrophages; the interaction prevents PARP14-mediated STAT1 and
STAT6 ADP-riboslylation (PubMed:27796300).
{ECO:0000250|UniProtKB:Q2EMV9, ECO:0000269|PubMed:23473667,
ECO:0000269|PubMed:27796300}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q2EMV9}.
Cytoplasm {ECO:0000269|PubMed:27796300}. Note=In steady state
splenocytes the protein is mostly nuclear (By similarity). A minor
proportion is detected in the cytoplasm (By similarity). In
macrophages, mainly localizes to the cytoplasm (PubMed:27796300).
{ECO:0000250|UniProtKB:Q2EMV9, ECO:0000269|PubMed:27796300}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=6;
IsoId=Q460N5-6; Sequence=Displayed;
Name=1; Synonyms=BAL2B;
IsoId=Q460N5-1; Sequence=VSP_040876;
Name=3; Synonyms=BAL2A;
IsoId=Q460N5-3; Sequence=VSP_020014;
Name=4;
IsoId=Q460N5-4; Sequence=VSP_020018, VSP_020019;
Name=5;
IsoId=Q460N5-5; Sequence=VSP_020013, VSP_020017;
-!- TISSUE SPECIFICITY: Expressed in macrophages.
{ECO:0000269|PubMed:27796300}.
-!- INDUCTION: Up-regulated by IFNG in macrophages. Down-regulated by
IL4 in macrophages. {ECO:0000269|PubMed:27796300}.
-!- PTM: Auto-ADP-ribosylated. {ECO:0000269|PubMed:16061477,
ECO:0000269|PubMed:27796300}.
-!- SEQUENCE CAUTION:
Sequence=AAY64449.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAY64450.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14089.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=DB237115; Type=Frameshift; Positions=48; Evidence={ECO:0000305};
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EMBL; AY134858; AAN08627.1; -; mRNA.
EMBL; AC048348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK001770; BAA91897.1; -; mRNA.
EMBL; AK022542; BAB14089.1; ALT_INIT; mRNA.
EMBL; AK304269; BAG65132.1; -; mRNA.
EMBL; DB237115; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; DQ063584; AAY64449.1; ALT_INIT; mRNA.
EMBL; DQ063585; AAY64450.1; ALT_INIT; mRNA.
EMBL; AB033094; BAA86582.1; -; mRNA.
CCDS; CCDS46894.1; -. [Q460N5-6]
RefSeq; NP_060024.2; NM_017554.2. [Q460N5-6]
UniGene; Hs.518203; -.
PDB; 3GOY; X-ray; 2.80 A; A/B/C/D=1611-1801.
PDB; 3Q6Z; X-ray; 2.23 A; A=789-979.
PDB; 3Q71; X-ray; 2.20 A; A=999-1196.
PDB; 3SE2; X-ray; 2.30 A; A/B/C/D=1611-1801.
PDB; 3SMI; X-ray; 2.40 A; A/B=1611-1801.
PDB; 3SMJ; X-ray; 1.50 A; A/B=1611-1801.
PDB; 3VFQ; X-ray; 2.80 A; A=784-1196.
PDB; 4ABK; X-ray; 1.60 A; A=1208-1388.
PDB; 4ABL; X-ray; 1.15 A; A=1208-1388.
PDB; 4D86; X-ray; 2.00 A; A=784-1196.
PDB; 4F1L; X-ray; 1.90 A; A/B/C/D=1611-1801.
PDB; 4F1Q; X-ray; 2.80 A; A/B=1611-1801.
PDB; 4PY4; X-ray; 2.76 A; A/B=1613-1801.
PDB; 5LXP; X-ray; 2.07 A; A/B=1611-1801.
PDB; 5LYH; X-ray; 2.17 A; A/B=1611-1801.
PDB; 5NQE; X-ray; 2.71 A; A/B=1611-1801.
PDB; 5O2D; X-ray; 1.60 A; A=994-1191.
PDB; 5V7T; X-ray; 2.30 A; A=1610-1801.
PDB; 5V7W; X-ray; 2.65 A; A/B=1610-1801.
PDB; 6G0W; X-ray; 2.34 A; A/B=1611-1801.
PDBsum; 3GOY; -.
PDBsum; 3Q6Z; -.
PDBsum; 3Q71; -.
PDBsum; 3SE2; -.
PDBsum; 3SMI; -.
PDBsum; 3SMJ; -.
PDBsum; 3VFQ; -.
PDBsum; 4ABK; -.
PDBsum; 4ABL; -.
PDBsum; 4D86; -.
PDBsum; 4F1L; -.
PDBsum; 4F1Q; -.
PDBsum; 4PY4; -.
PDBsum; 5LXP; -.
PDBsum; 5LYH; -.
PDBsum; 5NQE; -.
PDBsum; 5O2D; -.
PDBsum; 5V7T; -.
PDBsum; 5V7W; -.
PDBsum; 6G0W; -.
ProteinModelPortal; Q460N5; -.
SMR; Q460N5; -.
BioGrid; 120082; 14.
DIP; DIP-61130N; -.
IntAct; Q460N5; 1.
STRING; 9606.ENSP00000418194; -.
BindingDB; Q460N5; -.
ChEMBL; CHEMBL2176777; -.
iPTMnet; Q460N5; -.
PhosphoSitePlus; Q460N5; -.
BioMuta; PARP14; -.
DMDM; 327478567; -.
EPD; Q460N5; -.
MaxQB; Q460N5; -.
PaxDb; Q460N5; -.
PeptideAtlas; Q460N5; -.
PRIDE; Q460N5; -.
ProteomicsDB; 61930; -.
ProteomicsDB; 61931; -. [Q460N5-1]
ProteomicsDB; 61932; -. [Q460N5-3]
ProteomicsDB; 61933; -. [Q460N5-4]
ProteomicsDB; 61934; -. [Q460N5-5]
Ensembl; ENST00000474629; ENSP00000418194; ENSG00000173193. [Q460N5-6]
GeneID; 54625; -.
KEGG; hsa:54625; -.
UCSC; uc003efq.5; human. [Q460N5-6]
CTD; 54625; -.
DisGeNET; 54625; -.
EuPathDB; HostDB:ENSG00000173193.13; -.
GeneCards; PARP14; -.
H-InvDB; HIX0019605; -.
HGNC; HGNC:29232; PARP14.
HPA; HPA008846; -.
HPA; HPA012063; -.
MIM; 610028; gene.
neXtProt; NX_Q460N5; -.
OpenTargets; ENSG00000173193; -.
PharmGKB; PA134861585; -.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
GeneTree; ENSGT00760000119084; -.
HOVERGEN; HBG082105; -.
InParanoid; Q460N5; -.
KO; K15261; -.
OMA; HHVIHAV; -.
OrthoDB; EOG091G00EB; -.
PhylomeDB; Q460N5; -.
TreeFam; TF328965; -.
BRENDA; 2.4.2.30; 2681.
Reactome; R-HSA-197264; Nicotinamide salvaging.
ChiTaRS; PARP14; human.
EvolutionaryTrace; Q460N5; -.
GenomeRNAi; 54625; -.
PRO; PR:Q460N5; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000173193; -.
CleanEx; HS_PARP14; -.
ExpressionAtlas; Q460N5; baseline and differential.
Genevisible; Q460N5; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12543; RRM2_PAR14; 1.
Gene3D; 3.30.70.330; -; 2.
Gene3D; 3.30.720.50; -; 1.
InterPro; IPR002589; Macro_dom.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034517; PAR14_RRM2.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004170; WWE-dom.
InterPro; IPR037197; WWE_dom_sf.
Pfam; PF01661; Macro; 3.
Pfam; PF00644; PARP; 1.
SMART; SM00506; A1pp; 3.
SUPFAM; SSF117839; SSF117839; 1.
PROSITE; PS51154; MACRO; 3.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50918; WWE; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing;
Complete proteome; Cytoplasm; Glycosyltransferase; Immunity;
Innate immunity; NAD; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Transcription; Transcription regulation; Transferase.
CHAIN 1 1801 Poly [ADP-ribose] polymerase 14.
/FTId=PRO_0000247589.
DOMAIN 791 978 Macro 1. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1003 1190 Macro 2. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1216 1387 Macro 3. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1523 1601 WWE. {ECO:0000255|PROSITE-
ProRule:PRU00248}.
DOMAIN 1605 1801 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
REGION 922 926 Substrate 1 binding.
{ECO:0000244|PDB:3Q6Z,
ECO:0000269|PubMed:23473667}.
REGION 1023 1024 Substrate 2 binding.
{ECO:0000244|PDB:3Q71,
ECO:0000244|PDB:3VFQ,
ECO:0000269|PubMed:23473667}.
REGION 1046 1049 Substrate 2 binding.
{ECO:0000244|PDB:3Q71,
ECO:0000244|PDB:3VFQ,
ECO:0000269|PubMed:23473667}.
REGION 1133 1137 Substrate 2 binding.
{ECO:0000244|PDB:3Q71,
ECO:0000244|PDB:3VFQ,
ECO:0000269|PubMed:23473667}.
REGION 1175 1178 Substrate 2 binding.
{ECO:0000244|PDB:3Q71,
ECO:0000244|PDB:3VFQ,
ECO:0000269|PubMed:23473667}.
REGION 1235 1236 Substrate 3 binding.
{ECO:0000244|PDB:4ABK,
ECO:0000269|PubMed:23473667}.
REGION 1332 1336 Substrate 3 binding.
{ECO:0000244|PDB:3Q71,
ECO:0000244|PDB:3VFQ,
ECO:0000269|PubMed:23473667}.
BINDING 824 824 Substrate 1. {ECO:0000244|PDB:3Q6Z,
ECO:0000269|PubMed:23473667}.
BINDING 833 833 Substrate 1; via amide nitrogen.
{ECO:0000244|PDB:3Q6Z,
ECO:0000269|PubMed:23473667}.
BINDING 961 961 Substrate 1. {ECO:0000244|PDB:3Q6Z,
ECO:0000269|PubMed:23473667}.
BINDING 1034 1034 Substrate 2. {ECO:0000244|PDB:4ABK,
ECO:0000269|PubMed:23473667}.
BINDING 1247 1247 Substrate 3. {ECO:0000244|PDB:4ABK,
ECO:0000269|PubMed:23473667}.
BINDING 1258 1258 Substrate 3; via amide nitrogen.
{ECO:0000244|PDB:4ABK,
ECO:0000269|PubMed:23473667}.
BINDING 1371 1371 Substrate 3. {ECO:0000244|PDB:4ABK,
ECO:0000269|PubMed:23473667}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1403 1403 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1411 1411 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1004 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_020013.
VAR_SEQ 1 283 Missing (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_020014.
VAR_SEQ 119 199 Missing (in isoform 1).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16061477,
ECO:0000303|PubMed:16344560}.
/FTId=VSP_040876.
VAR_SEQ 1005 1013 KGSLVSPGG -> MYLRRLLRP (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_020017.
VAR_SEQ 1648 1680 IERIQNPDLWNSYQAKKKTMDAKNGQTMNEKQL -> VSLL
LECSFWMVEISSVMVLYKIHFHSLPITFF (in isoform
4). {ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:16061477}.
/FTId=VSP_020018.
VAR_SEQ 1681 1801 Missing (in isoform 4).
{ECO:0000303|PubMed:10574462,
ECO:0000303|PubMed:16061477}.
/FTId=VSP_020019.
MUTAGEN 1055 1055 G->E: Abolishes interaction with PARP10.
{ECO:0000269|PubMed:23473667}.
CONFLICT 59 59 Y -> C (in Ref. 4; DB237115).
{ECO:0000305}.
CONFLICT 597 597 N -> D (in Ref. 3; BAG65132).
{ECO:0000305}.
CONFLICT 1239 1239 E -> G (in Ref. 3; BAA91897).
{ECO:0000305}.
CONFLICT 1499 1499 G -> A (in Ref. 1; AAN08627).
{ECO:0000305}.
CONFLICT 1521 1521 A -> G (in Ref. 1; AAN08627).
{ECO:0000305}.
STRAND 792 799 {ECO:0000244|PDB:4D86}.
STRAND 802 808 {ECO:0000244|PDB:4D86}.
STRAND 815 823 {ECO:0000244|PDB:4D86}.
HELIX 832 841 {ECO:0000244|PDB:4D86}.
HELIX 844 856 {ECO:0000244|PDB:4D86}.
STRAND 861 868 {ECO:0000244|PDB:4D86}.
STRAND 872 881 {ECO:0000244|PDB:4D86}.
HELIX 887 889 {ECO:0000244|PDB:4D86}.
HELIX 890 910 {ECO:0000244|PDB:4D86}.
STRAND 914 918 {ECO:0000244|PDB:4D86}.
TURN 921 926 {ECO:0000244|PDB:3VFQ}.
HELIX 930 947 {ECO:0000244|PDB:4D86}.
STRAND 956 963 {ECO:0000244|PDB:4D86}.
HELIX 964 977 {ECO:0000244|PDB:4D86}.
STRAND 1006 1009 {ECO:0000244|PDB:5O2D}.
STRAND 1015 1019 {ECO:0000244|PDB:5O2D}.
HELIX 1023 1025 {ECO:0000244|PDB:4D86}.
STRAND 1028 1034 {ECO:0000244|PDB:5O2D}.
STRAND 1041 1044 {ECO:0000244|PDB:4D86}.
HELIX 1045 1054 {ECO:0000244|PDB:5O2D}.
HELIX 1057 1066 {ECO:0000244|PDB:5O2D}.
STRAND 1076 1080 {ECO:0000244|PDB:5O2D}.
STRAND 1084 1092 {ECO:0000244|PDB:5O2D}.
HELIX 1097 1099 {ECO:0000244|PDB:5O2D}.
HELIX 1101 1121 {ECO:0000244|PDB:5O2D}.
STRAND 1126 1130 {ECO:0000244|PDB:5O2D}.
HELIX 1141 1158 {ECO:0000244|PDB:5O2D}.
STRAND 1166 1170 {ECO:0000244|PDB:5O2D}.
HELIX 1176 1189 {ECO:0000244|PDB:5O2D}.
STRAND 1213 1216 {ECO:0000244|PDB:4ABK}.
STRAND 1220 1224 {ECO:0000244|PDB:4ABL}.
STRAND 1227 1234 {ECO:0000244|PDB:4ABL}.
HELIX 1236 1238 {ECO:0000244|PDB:4ABL}.
STRAND 1242 1248 {ECO:0000244|PDB:4ABL}.
HELIX 1258 1266 {ECO:0000244|PDB:4ABL}.
HELIX 1268 1280 {ECO:0000244|PDB:4ABL}.
STRAND 1284 1289 {ECO:0000244|PDB:4ABL}.
STRAND 1293 1302 {ECO:0000244|PDB:4ABL}.
HELIX 1307 1320 {ECO:0000244|PDB:4ABL}.
STRAND 1325 1328 {ECO:0000244|PDB:4ABL}.
HELIX 1340 1356 {ECO:0000244|PDB:4ABL}.
STRAND 1365 1371 {ECO:0000244|PDB:4ABL}.
HELIX 1373 1386 {ECO:0000244|PDB:4ABL}.
STRAND 1617 1621 {ECO:0000244|PDB:3SMJ}.
HELIX 1629 1640 {ECO:0000244|PDB:3SMJ}.
STRAND 1643 1652 {ECO:0000244|PDB:3SMJ}.
HELIX 1654 1670 {ECO:0000244|PDB:3SMJ}.
TURN 1671 1673 {ECO:0000244|PDB:3SE2}.
STRAND 1677 1684 {ECO:0000244|PDB:3SMJ}.
HELIX 1686 1688 {ECO:0000244|PDB:3SMJ}.
HELIX 1689 1695 {ECO:0000244|PDB:3SMJ}.
TURN 1699 1701 {ECO:0000244|PDB:3SMI}.
HELIX 1704 1706 {ECO:0000244|PDB:3SMJ}.
STRAND 1707 1709 {ECO:0000244|PDB:3SMJ}.
STRAND 1713 1718 {ECO:0000244|PDB:3SMJ}.
HELIX 1719 1722 {ECO:0000244|PDB:3SMJ}.
TURN 1725 1727 {ECO:0000244|PDB:3SMJ}.
STRAND 1736 1744 {ECO:0000244|PDB:3SMJ}.
STRAND 1747 1750 {ECO:0000244|PDB:3SMJ}.
STRAND 1760 1762 {ECO:0000244|PDB:5V7W}.
STRAND 1763 1765 {ECO:0000244|PDB:5LYH}.
STRAND 1771 1775 {ECO:0000244|PDB:3SMJ}.
STRAND 1777 1779 {ECO:0000244|PDB:3SMJ}.
STRAND 1781 1785 {ECO:0000244|PDB:3SMJ}.
STRAND 1791 1800 {ECO:0000244|PDB:3SMJ}.
SEQUENCE 1801 AA; 202800 MW; 27B027DFC7E773BD CRC64;
MAVPGSFPLL VEGSWGPDPP KNLNTKLQMY FQSPKRSGGG ECEVRQDPRS PSRFLVFFYP
EDVRQKVLER KNHELVWQGK GTFKLTVQLP ATPDEIDHVF EEELLTKESK TKEDVKEPDV
SEELDTKLPL DGGLDKMEDI PEECENISSL VAFENLKANV TDIMLILLVE NISGLSNDDF
QVEIIRDFDV AVVTFQKHID TIRFVDDCTK HHSIKQLQLS PRLLEVTNTI RVENLPPGAD
DYSLKLFFEN PYNGGGRVAN VEYFPEESSA LIEFFDRKVL DTIMATKLDF NKMPLSVFPY
YASLGTALYG KEKPLIKLPA PFEESLDLPL WKFLQKKNHL IEEINDEMRR CHCELTWSQL
SGKVTIRPAA TLVNEGRPRI KTWQADTSTT LSSIRSKYKV NPIKVDPTMW DTIKNDVKDD
RILIEFDTLK EMVILAGKSE DVQSIEVQVR ELIESTTQKI KREEQSLKEK MIISPGRYFL
LCHSSLLDHL LTECPEIEIC YDRVTQHLCL KGPSADVYKA KCEIQEKVYT MAQKNIQVSP
EIFQFLQQVN WKEFSKCLFI AQKILALYEL EGTTVLLTSC SSEALLEAEK QMLSALNYKR
IEVENKEVLH GKKWKGLTHN LLKKQNSSPN TVIINELTSE TTAEVIITGC VKEVNETYKL
LFNFVEQNMK IERLVEVKPS LVIDYLKTEK KLFWPKIKKV NVQVSFNPEN KQKGILLTGS
KTEVLKAVDI VKQVWDSVCV KSVHTDKPGA KQFFQDKARF YQSEIKRLFG CYIELQENEV
MKEGGSPAGQ KCFSRTVLAP GVVLIVQQGD LARLPVDVVV NASNEDLKHY GGLAAALSKA
AGPELQADCD QIVKREGRLL PGNATISKAG KLPYHHVIHA VGPRWSGYEA PRCVYLLRRA
VQLSLCLAEK YKYRSIAIPA ISSGVFGFPL GRCVETIVSA IKENFQFKKD GHCLKEIYLV
DVSEKTVEAF AEAVKTVFKA TLPDTAAPPG LPPAAAGPGK TSWEKGSLVS PGGLQMLLVK
EGVQNAKTDV VVNSVPLDLV LSRGPLSKSL LEKAGPELQE ELDTVGQGVA VSMGTVLKTS
SWNLDCRYVL HVVAPEWRNG STSSLKIMED IIRECMEITE SLSLKSIAFP AIGTGNLGFP
KNIFAELIIS EVFKFSSKNQ LKTLQEVHFL LHPSDHENIQ AFSDEFARRA NGNLVSDKIP
KAKDTQGFYG TVSSPDSGVY EMKIGSIIFQ VASGDITKEE ADVIVNSTSN SFNLKAGVSK
AILECAGQNV ERECSQQAQQ RKNDYIITGG GFLRCKNIIH VIGGNDVKSS VSSVLQECEK
KNYSSICLPA IGTGNAKQHP DKVAEAIIDA IEDFVQKGSA QSVKKVKVVI FLPQVLDVFY
ANMKKREGTQ LSSQQSVMSK LASFLGFSKQ SPQKKNHLVL EKKTESATFR VCGENVTCVE
YAISWLQDLI EKEQCPYTSE DECIKDFDEK EYQELNELQK KLNINISLDH KRPLIKVLGI
SRDVMQARDE IEAMIKRVRL AKEQESRADC ISEFIEWQYN DNNTSHCFNK MTNLKLEDAR
REKKKTVDVK INHRHYTVNL NTYTATDTKG HSLSVQRLTK SKVDIPAHWS DMKQQNFCVV
ELLPSDPEYN TVASKFNQTC SHFRIEKIER IQNPDLWNSY QAKKKTMDAK NGQTMNEKQL
FHGTDAGSVP HVNRNGFNRS YAGKNAVAYG KGTYFAVNAN YSANDTYSRP DANGRKHVYY
VRVLTGIYTH GNHSLIVPPS KNPQNPTDLY DTVTDNVHHP SLFVAFYDYQ AYPEYLITFR
K


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