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UniProtKB/Swiss-Prot entry P09874


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PARP1_HUMAN
Primary accession number P09874
Secondary accession number Q8IUZ9
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 127)
Name and origin of the protein
Protein name Poly [ADP-ribose] polymerase 1
Synonyms PARP-1
EC 2.4.2.30
ADPRT
NAD(+) ADP-ribosyltransferase 1
Poly[ADP-ribose] synthetase 1
Gene name
Name: PARP1
Synonyms: ADPRT, PPOL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
DOI=10.1016/0006-291X(87)90921-1; PubMed=3120710 [NCBI, ExPASy, EBI, Israel, Japan]
Uchida K., Morita T., Sato T., Ogura T., Yamashita R., Noguchi S., Suzuki H., Nyunoya H., Miwa M., Sugimura T.;
"Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase.";
Biochem. Biophys. Res. Commun. 148:617-622(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=2824474 [NCBI, ExPASy, EBI, Israel, Japan]
Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M., Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S., Shizuta Y.;
"Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.";
J. Biol. Chem. 262:15990-15997(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-940.
DOI=10.1073/pnas.84.23.8370; PubMed=2891139 [NCBI, ExPASy, EBI, Israel, Japan]
Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K., Hensley P., Smulson M.E.;
"cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.";
Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2513174 [NCBI, ExPASy, EBI, Israel, Japan]
Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.;
"Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene.";
DNA 8:575-580(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-188; ILE-334; TYR-383; ALA-762 AND ARG-940.
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-762.
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
DOI=10.1111/j.1432-1033.1990.tb15647.x; PubMed=2125269 [NCBI, ExPASy, EBI, Israel, Japan]
Yokoyama Y., Kawamoto T., Mitsuuchi Y., Kurosaki T., Toda K., Ushiro H., Terashima M., Sumimoto H., Kuribayashi I., Yamamoto Y., Maeda T., Ikeda H., Sagara Y., Shizuta Y.;
"Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region.";
Eur. J. Biochem. 194:521-526(1990).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
DOI=10.1016/0006-291X(90)92082-B; PubMed=2108670 [NCBI, ExPASy, EBI, Israel, Japan]
Ogura T., Nyunoya H., Takahashi-Masutani M., Miwa M., Sugimura T., Esumi H.;
"Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene.";
Biochem. Biophys. Res. Commun. 167:701-710(1990).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
Herzog H., Schneider R., Hirsch-Kauffmann M., Schnitzer D., Schweiger M.;
"Human pADPRT is involved in the regulation of its own gene.";
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 2-10; 35-47; 66-78; 109-119; 183-197; 209-221; 263-282; 453-467; 487-496; 529-548; 552-564; 572-582; 637-654; 668-695; 748-761; 780-796; 803-816 AND 859-903, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 381-420 AND 682-710.
PubMed=3121332 [NCBI, ExPASy, EBI, Israel, Japan]
Schneider R., Auer B., Kuhne C., Herzog H., Klocker H., Burtscher H.J., Hirsch-Kauffmann M., Wintersberger U., Schweiger M.;
"Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase.";
Eur. J. Cell Biol. 44:302-307(1987).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 441-1014.
DOI=10.1016/0006-291X(87)90543-2; PubMed=3113420 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.;
"Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation.";
Biochem. Biophys. Res. Commun. 146:403-409(1987).
[13]
ERRATUM.
Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.;
Biochem. Biophys. Res. Commun. 148:1549-1550(1987).
[14]
ANALYSIS OF ZINC FINGERS.
DOI=10.1073/pnas.87.8.2990; PubMed=2109322 [NCBI, ExPASy, EBI, Israel, Japan]
Gradwohl G., Menissier-de Murcia J., Molinete M., Simonin F., Koken M.H.M., Hoeijmakers J.H.J., de Murcia G.M.;
"The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.";
Proc. Natl. Acad. Sci. U.S.A. 87:2990-2994(1990).
[15]
ANALYSIS OF ZINC FINGERS.
PubMed=2123876 [NCBI, ExPASy, EBI, Israel, Japan]
Ikelima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., Miwa M.;
"The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.";
J. Biol. Chem. 265:21907-21913(1990).
[16]
MUTAGENESIS OF CATALYTIC DOMAIN.
PubMed=2121735 [NCBI, ExPASy, EBI, Israel, Japan]
Simonin F., Menissier-de Murcia J., Poch O., Muller S., Gradwohl G., Molinete M., Penning C., Keith G., de Murcia G.M.;
"Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity.";
J. Biol. Chem. 265:19249-19256(1990).
[17]
NUCLEAR LOCALIZATION SIGNAL.
PubMed=1505517 [NCBI, ExPASy, EBI, Israel, Japan]
Schreiber V., Molinete M., Boeuf H., de Murcia G.M., Menissier-de Murcia J.;
"The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.";
EMBO J. 11:3263-3269(1992).
[18]
MUTAGENESIS OF CATALYTIC DOMAIN.
DOI=10.1021/bi971055p; PubMed=9315851 [NCBI, ExPASy, EBI, Israel, Japan]
Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G.M.;
"Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.";
Biochemistry 36:12147-12154(1997).
[19]
PHOSPHORYLATION.
DOI=10.1038/sj.onc.1202823; PubMed=10467406 [NCBI, ExPASy, EBI, Israel, Japan]
Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T., Shimotohno K., Ueda K., Hatanaka M., Noda M.;
"Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro.";
Oncogene 18:4616-4625(1999).
[20]
INTERACTION WITH APTX.
DOI=10.1093/hmg/ddh122; PubMed=15044383 [NCBI, ExPASy, EBI, Israel, Japan]
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.;
"Aprataxin, a novel protein that protects against genotoxic stress.";
Hum. Mol. Genet. 13:1081-1093(2004).
[21]
INTERACTION WITH SRY.
DOI=10.1016/j.mce.2006.06.008; PubMed=16904257 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y., Oh H.J., Lau Y.-F.C.;
"The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions.";
Mol. Cell. Endocrinol. 257:35-46(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; THR-368 AND SER-782, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[25]
STRUCTURE BY NMR OF 1-93 AND 385-643.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first ZF-PARP domain, of the BRCT domain and of the WGR domain of human poly(adp-ribose)polymerase-1.";
Submitted (APR-2007) to the PDB data bank.
[26]
VARIANT [LARGE SCALE ANALYSIS] VAL-488.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M18112; AAA60137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03473; AAB59447.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M32721; AAA60155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29786; AAA51663.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29545; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29766; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29767; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29768; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29769; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29770; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29771; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29772; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29773; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29774; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29775; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29776; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29777; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29778; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29779; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29780; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29781; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29783; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29784; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29785; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29544; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29782; AAA51663.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF524947; AAM75364.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037545; AAH37545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56140; CAA39606.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56141; CAA39606.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16674; CAA34663.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60436; AAA60000.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17081; AAA51599.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00449049; -.
PIR A29725; A29725.
RefSeq NP_001609.2; -.
UniGene Hs.177766
3D structure databases
PDB
1UK0; X-ray; 3.00 A; A/B=662-1010.[ExPASy / RCSB / EBI]
1UK1; X-ray; 3.00 A; A/B=662-1010.[ExPASy / RCSB / EBI]
1WOK; X-ray; 3.00 A; A/B/C/D=662-1010.[ExPASy / RCSB / EBI]
2COK; NMR; -; A=387-486.[ExPASy / RCSB / EBI]
2CR9; NMR; -; A=518-643.[ExPASy / RCSB / EBI]
2CS2; NMR; -; A=103-224.[ExPASy / RCSB / EBI]
2DMJ; NMR; -; A=1-93.[ExPASy / RCSB / EBI]
2JVN; NMR; -; A=233-358.[ExPASy / RCSB / EBI]
2RCW; X-ray; 2.80 A; A=662-1011.[ExPASy / RCSB / EBI]
2RD6; X-ray; 2.30 A; A=662-1011.[ExPASy / RCSB / EBI]
2RIQ; X-ray; 1.70 A; A=216-366.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1UK0; -.
1UK1; -.
1WOK; -.
2COK; -.
2CR9; -.
2CS2; -.
2DMJ; -.
2JVN; -.
2RCW; -.
2RD6; -.
2RIQ; -.
ModBase P09874.
Protein-protein interaction databases
DIP DIP:38N; -.
IntAct P09874; 21.
PTM databases
PhosphoSite P09874; -.
Enzyme and pathway databases
BRENDA 2.4.2.30; 247.
Pathway_Interaction_DB caspase_pathway; Caspase cascade in apoptosis.
faspathway; FAS signaling pathway (CD95).
2D gel databases
SWISS-2DPAGE P09874; -.
Aarhus/Ghent-2DPAGE 1620; NEPHGE.
Organism-specific databases
GeneCards GC01M224615; -.
HGNC HGNC:270; PARP1.
GenAtlas PARP1.
HPA CAB000147; -.
CAB003839; -.
CAB003840; -.
MIM 173870; gene. [NCBI / EBI]
PharmGKB PA32; -.
Gene expression databases
ArrayExpress P09874; -.
Bgee P09874; -.
CleanEx HS_PARP1; -.
GermOnline ENSG00000143799; Homo sapiens.
Ontologies
GO
GO:0005635; Cellular component: nuclear envelope (inferred from direct assay from UniProtKB).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0051287; Molecular function: NAD or NADH binding (inferred from electronic annotation from InterPro).
GO:0003950; Molecular function: NAD+ ADP-ribosyltransferase activity (inferred from direct assay from UniProtKB).
GO:0047485; Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0006471; Biological process: protein amino acid ADP-ribosylation (traceable author statement from ProtInc).
GO:0006366; Biological process: transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001357; BRCT.
IPR008288; NAD_ADPRT.
IPR012982; PADR1.
IPR012317; PARP_catalytic.
IPR004102; PARP_reg.
IPR008893; WGR.
IPR001510; Znf_PARP.
Graphical view of domain structure.
Gene3D G3DSA:1.20.142.10; PARP_reg; 1.
G3DSA:3.30.1740.10; Znf_PARP; 2.
Pfam PF00533; BRCT; 1.
PF08063; PADR1; 1.
PF00644; PARP; 1.
PF02877; PARP_reg; 1.
PF05406; WGR; 1.
PF00645; zf-PARP; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF000489; NAD_ADPRT; 1.
ProDom PD004675; Znf_PolyADPpol; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00292; BRCT; 1.
SM00773; WGR; 1.
SMART graphical view of domain structure.
PROSITE PS50172; BRCT; 1.
PS51060; PARP_ALPHA_HD; 1.
PS51059; PARP_CATALYTIC; 1.
PS00347; PARP_ZN_FINGER_1; 2.
PS50064; PARP_ZN_FINGER_2; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P09874; -.
PRIDE P09874; -.
Genome annotation databases
Ensembl ENSG00000143799; Homo sapiens. [Contig view]
GeneID 142; -.
KEGG hsa:142; -.
Phylogenomic databases
HOGENOM P09874; -.
HOVERGEN P09874; -.
OMA P09874; VDIVKGT.
Other
NextBio 565; -.
PMAP-CutDB P09874; -.
SOURCE PARP1; Homo sapiens.
ProtoNet P09874.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; ADP-ribosylation; Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Glycosyltransferase; Metal-binding; NAD; Nucleus; Phosphoprotein; Polymorphism; Repeat; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   1014  1013     Poly [ADP-ribose] polymerase 1. PRO_0000211320
DOMAIN   385    476  92     BRCT. 
DOMAIN   662    779  118     PARP alpha-helical. 
DOMAIN   788   1014  227     PARP catalytic. 
DNA_BIND   2    372  371      
ZN_FING   9     93  85     PARP-type 1. 
ZN_FING   113    203  91     PARP-type 2. 
REGION   373    524  152     Automodification domain. 
MOTIF   207    209  3     Nuclear localization signal. 
MOTIF   221    226  6     Nuclear localization signal. 
MOD_RES   2      2        N-acetylalanine. 
MOD_RES   41     41        Phosphoserine. 
MOD_RES   179    179        Phosphoserine. 
MOD_RES   368    368        Phosphothreonine. 
MOD_RES   407    407        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   413    413        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   435    435        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   437    437        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   444    444        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   445    445        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   448    448        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   456    456        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   471    471        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   484    484        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   488    488        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   491    491        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   513    513        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   514    514        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   520    520        PolyADP-ribosyl glutamic acid (Potential). 
MOD_RES   782    782        Phosphoserine. 
VARIANT   54     54  1     F -> L (in dbSNP:rs3738708 [NCBI]). VAR_050460 
VARIANT   188    188  1     A -> T (in dbSNP:rs1805409 [NCBI]). VAR_014714 
VARIANT   334    334  1     V -> I (in dbSNP:rs3219057 [NCBI]). VAR_019171 
VARIANT   377    377  1     P -> S (in dbSNP:rs2230484 [NCBI]). VAR_050461 
VARIANT   383    383  1     S -> Y (in dbSNP:rs3219062 [NCBI]). VAR_019172 
VARIANT   488    488  1     E -> V (in a breast cancer sample; somatic mutation). VAR_035852 
VARIANT   762    762  1     V -> A (in dbSNP:rs1136410 [NCBI]). VAR_014715 [3D]
VARIANT   940    940  1     K -> R (in dbSNP:rs3219145 [NCBI]). VAR_019173 [3D]
MUTAGEN   797    797        L->P: 1.5% of wild-type activity. 
MUTAGEN   868    868        N->S: 4% of wild-type activity. 
MUTAGEN   890    890        M->V: <0.5% of wild-type activity. 
MUTAGEN   893    893        K->I: Abolishes enzymatic activity. 
MUTAGEN   897    897        F->S: 10% of wild-type activity. 
MUTAGEN   899    899        D->N: 0.6% of wild-type activity. 
MUTAGEN   908    908        C->R: <0.5% of wild-type activity. 
MUTAGEN   926    926        L->F: 1.5% of wild-type activity. 
MUTAGEN   986    986        Y->H: 14% of wild-type activity and increased branching 15-fold. 
MUTAGEN   988    988        E->K: 1.25% of wild-type activity; only monomers are added. 
MUTAGEN   1003   1003        L->P: 1.5% of wild-type activity. 
CONFLICT   17     17        G -> E (in Ref. 2; AAB59447). 
CONFLICT   70     70        E -> Q (in Ref. 1; AAA60137). 
CONFLICT   212    212        E -> K (in Ref. 2; AAB59447). 
CONFLICT   613    613        H -> Q (in Ref. 3; AAA60155). 
CONFLICT   827    827        N -> S (in Ref. 3; AAA60155). 
CONFLICT   908    908        C -> Y (in Ref. 3; AAA60155). 
CONFLICT   980    980        N -> I (in Ref. 3; AAA60155). 
STRAND   110    117  8      
STRAND   119    121  3      
STRAND   126    128  3      
STRAND   136    144  9      
TURN   149    151  3      
STRAND   153    158  6      
HELIX   160    165  6      
TURN   166    171  6      
HELIX   178    180  3      
TURN   183    186  4      
HELIX   189    196  8      
HELIX   226    255  30      
HELIX   258    267  10      
HELIX   276    289  14      
TURN   296    298  3      
STRAND   302    305  4      
STRAND   308    311  4      
STRAND   314    316  3      
STRAND   324    327  4      
HELIX   337    340  4      
HELIX   342    347  6      
STRAND   389    392  4      
STRAND   394    397  4      
HELIX   405    414  10      
STRAND   418    421  4      
STRAND   427    430  4      
HELIX   433    438  6      
HELIX   441    448  8      
HELIX   457    463  7      
HELIX   469    475  7      
TURN   535    538  4      
TURN   540    542  3      
STRAND   543    545  3      
STRAND   554    560  7      
STRAND   562    564  3      
STRAND   567    577  11      
TURN   578    581  4      
STRAND   582    589  8      
STRAND   591    595  5      
STRAND   598    606  9      
HELIX   607    621  15      
STRAND   622    624  3      
STRAND   639    642  4      
HELIX   667    676  10      
HELIX   679    688  10      
TURN   693    695  3      
HELIX   703    721  19      
HELIX   726    739  14      
STRAND   752    754  3      
HELIX   755    779  25      
HELIX   793    796  4      
STRAND   799    803  5      
HELIX   809    820  12      
HELIX   824    826  3      
STRAND   828    834  7      
STRAND   837    841  5      
HELIX   844    848  5      
HELIX   850    853  4      
STRAND   855    863  9      
TURN   866    868  3      
HELIX   869    875  7      
HELIX   886    888  3      
STRAND   893    896  4      
STRAND   898    900  3      
HELIX   901    906  6      
STRAND   912    914  3      
STRAND   916    925  10      
STRAND   928    934  7      
STRAND   947    950  4      
STRAND   953    956  4      
HELIX   958    960  3      
HELIX   964    966  3      
STRAND   974    976  3      
STRAND   981    983  3      
STRAND   988    993  6      
HELIX   994    996  3      
STRAND   997   1008  12      
Sequence information
Length: 1014 AA [This is the length of the unprocessed precursor] Molecular weight: 113084 Da [This is the MW of the unprocessed precursor] CRC64: 6A5FC01EB91C046B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 

        70         80         90        100        110        120 
GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD GIGSKAEKTL GDFAAEYAKS 

       130        140        150        160        170        180 
NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ LGMIDRWYHP GCFVKNREEL GFRPEYSASQ 

       190        200        210        220        230        240 
LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA 

       250        260        270        280        290        300 
QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG 

       310        320        330        340        350        360 
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE 

       370        380        390        400        410        420 
TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK LSRNKDEVKA MIEKLGGKLT 

       430        440        450        460        470        480 
GTANKASLCI STKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP 

       490        500        510        520        530        540 
WGAEVKAEPV EVVAPRGKSG AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE 

       550        560        570        580        590        600 
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK 

       610        620        630        640        650        660 
LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVNPG 

       670        680        690        700        710        720 
TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV 

       730        740        750        760        770        780 
SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG 

       790        800        810        820        830        840 
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE 

       850        860        870        880        890        900 
REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 

       910        920        930        940        950        960 
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA 

       970        980        990       1000       1010 
NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW 

P09874 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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