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Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP)

 PARP4_HUMAN             Reviewed;        1724 AA.
Q9UKK3; O75903; Q14682; Q5QNZ9; Q9H1M6;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
13-FEB-2019, entry version 183.
RecName: Full=Protein mono-ADP-ribosyltransferase PARP4 {ECO:0000305};
EC=2.4.2.- {ECO:0000269|PubMed:25043379};
AltName: Full=193 kDa vault protein {ECO:0000303|PubMed:10477748};
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 4 {ECO:0000303|PubMed:20106667};
Short=ARTD4 {ECO:0000303|PubMed:20106667};
AltName: Full=PARP-related/IalphaI-related H5/proline-rich {ECO:0000303|PubMed:10100603};
Short=PH5P {ECO:0000303|PubMed:10100603};
AltName: Full=Poly [ADP-ribose] polymerase 4 {ECO:0000303|PubMed:20106667};
Short=PARP-4 {ECO:0000303|PubMed:20106667};
AltName: Full=Vault poly(ADP-ribose) polymerase {ECO:0000303|PubMed:10477748};
Short=VPARP {ECO:0000303|PubMed:10477748};
Name=PARP4 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:271};
Synonyms=ADPRTL1 {ECO:0000303|PubMed:10644454},
KIAA0177 {ECO:0000303|PubMed:8724849}, PARPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 306-319, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANT THR-899.
PubMed=10477748; DOI=10.1083/jcb.146.5.917;
Kickhoefer V.A., Siva A.C., Kedersha N.L., Inman E.M., Ruland C.,
Streuli M., Rome L.H.;
"The 193 kDa vault protein, VPARP, is a novel poly(ADP-ribose)
polymerase.";
J. Cell Biol. 146:917-928(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-873; ALA-1265 AND
ARG-1280.
TISSUE=Thymus;
PubMed=10644454; DOI=10.1006/geno.1999.6024;
Still I.H., Vince P., Cowell J.K.;
"Identification of a novel gene (ADPRTL1) encoding a potential
poly(ADP-ribosyl)transferase protein.";
Genomics 62:533-536(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-873; ALA-1265
AND ARG-1280.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
DISCUSSION OF SEQUENCE.
PubMed=10100603; DOI=10.1016/S0014-5793(99)00173-8;
Jean L., Risler J.-L., Nagase T., Coulouarn C., Nomura N.,
Salier J.-P.;
"The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a
missing link between poly(ADP-ribose)polymerase and the inter-alpha-
inhibitor family and a novel actor of DNA repair?";
FEBS Lett. 446:6-8(1999).
[7]
ASSOCIATION WITH TEP1.
PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O.,
Rome L.H.;
"Vaults and telomerase share a common subunit, TEP1.";
J. Biol. Chem. 274:32712-32717(1999).
[8]
INTERACTION WITH TEP1.
PubMed=15169895; DOI=10.1128/MCB.24.12.5314-5323.2004;
Liu Y., Snow B.E., Kickhoefer V.A., Erdmann N., Zhou W., Wakeham A.,
Gomez M., Rome L.H., Harrington L.;
"Vault poly(ADP-ribose) polymerase is associated with mammalian
telomerase and is dispensable for telomerase function and vault
structure in vivo.";
Mol. Cell. Biol. 24:5314-5323(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-1236; SER-1335
AND SER-1504, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1335, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-1236 AND
SER-1335, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101, 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).
[15]
FUNCTION.
PubMed=25043379; DOI=10.1038/ncomms5426;
Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
Chang P.;
"Family-wide analysis of poly(ADP-ribose) polymerase activity.";
Nat. Commun. 5:4426-4426(2014).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1476, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
ribosylation of target proteins. {ECO:0000269|PubMed:25043379}.
-!- CATALYTIC ACTIVITY:
Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424,
Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
Evidence={ECO:0000305};
-!- CATALYTIC ACTIVITY:
Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224,
Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
Evidence={ECO:0000305};
-!- SUBUNIT: Component of the vault ribonucleoprotein particle, at
least composed of MVP, PARP4 and one or more vault RNAs (vRNAs)
(PubMed:10477748). Interacts with TEP1 (PubMed:10551828,
PubMed:15169895). {ECO:0000269|PubMed:10477748,
ECO:0000269|PubMed:10551828, ECO:0000269|PubMed:15169895}.
-!- INTERACTION:
Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-2623021, EBI-6248094;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10477748}.
Nucleus {ECO:0000269|PubMed:10477748}. Cytoplasm, cytoskeleton,
spindle {ECO:0000269|PubMed:10477748}. Note=Also found in the
nucleus, associated with mitotic spindles.
{ECO:0000269|PubMed:10477748}.
-!- TISSUE SPECIFICITY: Widely expressed; the highest levels are in
the kidney; also detected in heart, placenta, lung, liver,
skeletal muscle, spleen, leukocytes and pancreas.
{ECO:0000269|PubMed:10477748}.
-!- CAUTION: Was initially thought to mediate to mediate poly-ADP-
ribosylation of proteins (PubMed:10477748). However, it was later
shown to act as a mono-ADP-ribosyltransferase (PubMed:25043379).
{ECO:0000269|PubMed:10477748, ECO:0000269|PubMed:25043379}.
-!- SEQUENCE CAUTION:
Sequence=BAA11494.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF158255; AAD47250.1; -; mRNA.
EMBL; AF057160; AAC62491.1; -; mRNA.
EMBL; D79999; BAA11494.2; ALT_INIT; mRNA.
EMBL; AL359763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS9307.1; -.
RefSeq; NP_006428.2; NM_006437.3.
RefSeq; XP_011533234.1; XM_011534932.2.
UniGene; Hs.744855; -.
ProteinModelPortal; Q9UKK3; -.
BioGrid; 106653; 13.
IntAct; Q9UKK3; 18.
MINT; Q9UKK3; -.
STRING; 9606.ENSP00000371419; -.
BindingDB; Q9UKK3; -.
ChEMBL; CHEMBL6142; -.
CarbonylDB; Q9UKK3; -.
iPTMnet; Q9UKK3; -.
PhosphoSitePlus; Q9UKK3; -.
BioMuta; PARP4; -.
DMDM; 308153574; -.
EPD; Q9UKK3; -.
jPOST; Q9UKK3; -.
MaxQB; Q9UKK3; -.
PaxDb; Q9UKK3; -.
PeptideAtlas; Q9UKK3; -.
PRIDE; Q9UKK3; -.
ProteomicsDB; 84811; -.
DNASU; 143; -.
Ensembl; ENST00000381989; ENSP00000371419; ENSG00000102699.
GeneID; 143; -.
KEGG; hsa:143; -.
UCSC; uc001upl.4; human.
CTD; 143; -.
DisGeNET; 143; -.
EuPathDB; HostDB:ENSG00000102699.5; -.
GeneCards; PARP4; -.
H-InvDB; HIX0019099; -.
HGNC; HGNC:271; PARP4.
HPA; HPA011739; -.
MIM; 607519; gene.
neXtProt; NX_Q9UKK3; -.
OpenTargets; ENSG00000102699; -.
PharmGKB; PA24591; -.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00940000160555; -.
HOGENOM; HOG000139369; -.
HOVERGEN; HBG053515; -.
InParanoid; Q9UKK3; -.
KO; K10798; -.
OMA; PYMSWQE; -.
OrthoDB; 955432at2759; -.
PhylomeDB; Q9UKK3; -.
TreeFam; TF329720; -.
BRENDA; 2.4.2.30; 2681.
Reactome; R-HSA-197264; Nicotinamide salvaging.
SignaLink; Q9UKK3; -.
ChiTaRS; PARP4; human.
GeneWiki; PARP4; -.
GenomeRNAi; 143; -.
PRO; PR:Q9UKK3; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102699; Expressed in 96 organ(s), highest expression level in intestine.
Genevisible; Q9UKK3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; NAS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IDA:MGI.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:1990404; F:protein ADP-ribosylase activity; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0051972; P:regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; NAS:UniProtKB.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR031273; PARP4.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR013694; VIT.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10338:SF127; PTHR10338:SF127; 1.
Pfam; PF00533; BRCT; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF08487; VIT; 1.
Pfam; PF00092; VWA; 1.
SMART; SM00292; BRCT; 1.
SMART; SM00609; VIT; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS51468; VIT; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Glycosyltransferase; Methylation; NAD; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ribonucleoprotein; Transferase.
CHAIN 1 1724 Protein mono-ADP-ribosyltransferase
PARP4.
/FTId=PRO_0000211330.
DOMAIN 1 94 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 242 370 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 369 573 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DOMAIN 607 735 VIT. {ECO:0000255|PROSITE-
ProRule:PRU00801}.
DOMAIN 876 1046 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 1562 1724 Interaction with the major vault protein.
{ECO:0000269|PubMed:10477748}.
MOTIF 19 25 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1237 1249 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1236 1236 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1335 1335 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1476 1476 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1504 1504 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 81 81 I -> V (in dbSNP:rs35200240).
/FTId=VAR_056645.
VARIANT 122 122 S -> N (in dbSNP:rs9578751).
/FTId=VAR_056646.
VARIANT 215 215 F -> Y (in dbSNP:rs9318600).
/FTId=VAR_056647.
VARIANT 792 792 P -> L (in dbSNP:rs4986818).
/FTId=VAR_056648.
VARIANT 873 873 S -> N (in dbSNP:rs7140044).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_056649.
VARIANT 899 899 A -> T (in dbSNP:rs2275660).
{ECO:0000269|PubMed:10477748}.
/FTId=VAR_056650.
VARIANT 991 991 K -> R (in dbSNP:rs34689435).
/FTId=VAR_056651.
VARIANT 1012 1012 V -> I (in dbSNP:rs9581043).
/FTId=VAR_056652.
VARIANT 1253 1253 S -> T (in dbSNP:rs4986822).
/FTId=VAR_056653.
VARIANT 1265 1265 G -> A (in dbSNP:rs1050110).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_016090.
VARIANT 1280 1280 G -> R (in dbSNP:rs13428).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_016091.
CONFLICT 519 519 S -> P (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 897 897 Q -> E (in Ref. 2; AAC62491 and 3;
BAA11494). {ECO:0000305}.
CONFLICT 936 936 M -> A (in Ref. 2; AAC62491 and 3;
BAA11494). {ECO:0000305}.
CONFLICT 936 936 M -> T (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 1065 1065 V -> A (in Ref. 1; AAD47250 and 2;
AAC62491). {ECO:0000305}.
CONFLICT 1080 1080 L -> R (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1108 1108 R -> C (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1328 1328 P -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1331 1331 A -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1394 1394 S -> A (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1459 1459 S -> Y (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1550 1550 L -> P (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1555 1555 V -> L (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 1564 1564 I -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1656 1656 A -> P (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
SEQUENCE 1724 AA; 192595 MW; DCA1DD4C001EA22F CRC64;
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ
LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP
DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR
DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL
ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC
ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV
NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD
SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT
TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP
LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN
LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK
QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL
PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL
SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG
AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL
NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI
LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED
FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA
PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS
ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS
LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE
IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR
ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE
GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1644: DNA replication
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1497: Hedgehog-related genes
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1559: TFs Regulate miRNAs related to cardiac hypertrophy
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism

Related Genes :
[PARP4 ADPRTL1 KIAA0177 PARPL] Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP)
[Parp4 Kiaa0177] Protein mono-ADP-ribosyltransferase PARP4 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (Poly [ADP-ribose] polymerase 4) (PARP-4) (Vault poly(ADP-ribose) polymerase) (VPARP) (mVparp)
[PARP3 ADPRT3 ADPRTL3] Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (IRT1) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (hPARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3)
[Parp3 Adprt3] Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3)
[PARP9 BAL BAL1] Protein mono-ADP-ribosyltransferase PARP9 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein) (Poly [ADP-ribose] polymerase 9) (PARP-9)
[PARP16 ARTD15 C15orf30] Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16)
[Parp9 Bal] Protein mono-ADP-ribosyltransferase PARP9 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein homolog) (Poly [ADP-ribose] polymerase 9) (PARP-9)
[Parp CG40411] Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.30) (NAD(+) ADP-ribosyltransferase) (ADPRT) (Poly[ADP-ribose] synthase) (Protein ADP-ribosyltransferase Parp) (EC 2.4.2.-)
[Parp16 Artd15] Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16)
[ZC3HAV1 ZC3HDC2 PRO1677] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger CCCH domain-containing protein 2) (Zinc finger antiviral protein) (ZAP)
[Parp16 Artd15] Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16)
[Zc3hav1] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13)
[Zc3hav1 Zap] Zinc finger CCCH-type antiviral protein 1 (ADP-ribosyltransferase diphtheria toxin-like 13) (ARTD13) (Inactive Poly [ADP-ribose] polymerase 13) (PARP13) (Zinc finger antiviral protein) (ZAP) (rZAP)
[ADPRHL2 ARH3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[Adprhl2 Arh3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[] Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.30) (NAD(+) ADP-ribosyltransferase) (ADPRT) (Poly[ADP-ribose] synthase) (Protein ADP-ribosyltransferase) (EC 2.4.2.-)
[ART3 TMART] Ecto-ADP-ribosyltransferase 3 (EC 2.4.2.31) (ADP-ribosyltransferase C2 and C3 toxin-like 3) (ARTC3) (Mono(ADP-ribosyl)transferase 3) (NAD(P)(+)--arginine ADP-ribosyltransferase 3)
[adprhl2 arh3] ADP-ribose glycohydrolase ARH3 (LchARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[adprhl2 arh3 zgc:92867] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[ADPRHL2 ARH3] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[ADPRHL2 ARH3 RCJMB04_30e5] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[adprhl2 arh3 TGas084j22.1] ADP-ribose glycohydrolase ARH3 (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-)
[sdeA lpg2157] Ubiquitinating/deubiquitinating enzyme SdeA (Effector protein SdeA) [Includes: Deubiquitinase (DUB) (EC 3.4.22.-) (Deneddylase) (Deubiquitinating enzyme); Ubiquitin transferase (EC 2.3.2.-); Mono-ADP-ribosyltransferase (mART) (EC 2.4.2.31)]
[] ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) (2'-phospho-ADP-ribosyl cyclase) (2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase) (EC 2.4.99.20) (2'-phospho-cyclic-ADP-ribose transferase) (ADP-ribosyl cyclase) (ADPRC) (ADRC) (NAD glycohydrolase) (NAD(+) nucleosidase) (NADase)
[MACROD1 LRP16] ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.5.1.-) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[MVP LRP] Major vault protein (MVP) (Lung resistance-related protein)
[modB mod] NAD--protein ADP-ribosyltransferase modB (EC 2.4.2.31)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

Bibliography :