Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09874 (PARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 186. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 1

Short name=PARP-1
EC=2.4.2.30
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 1
Short name=ARTD1
NAD(+) ADP-ribosyltransferase 1
Short name=ADPRT 1
Poly[ADP-ribose] synthase 1
Gene names
Name:PARP1
Synonyms:ADPRT, PPOL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Ref.13 Ref.28 Ref.30 Ref.33 Ref.44

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.28

Subunit structure

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 By similarity. Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1, RNF4 and TXK. Interacts with RNF146. Interacts with ZNF423. Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated) with PARP9. Ref.13 Ref.22 Ref.24 Ref.25 Ref.26 Ref.31 Ref.33 Ref.38 Ref.39 Ref.41 Ref.44

Subcellular location

Nucleus. Nucleusnucleolus. Note: Localizes at sites of DNA damage. Ref.13 Ref.39 Ref.42 Ref.44

Post-translational modification

Phosphorylated by PRKDC and TXK. Ref.13 Ref.23

Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites. Ref.33

S-nitrosylated, leading to inhibit transcription regulation activity By similarity.

Miscellaneous

The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 PARP-type zinc fingers.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
ADP-ribosylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, detection of DNA damage

Inferred from electronic annotation. Source: Ensembl

DNA repair

Traceable author statement Ref.26. Source: UniProtKB

base-excision repair

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

double-strand break repair

Inferred from mutant phenotype Ref.44. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

macrophage differentiation

Traceable author statement PubMed 18309324. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

positive regulation of SMAD protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

protein ADP-ribosylation

Inferred from direct assay Ref.26. Source: UniProtKB

protein autoprocessing

Inferred from electronic annotation. Source: Ensembl

protein poly-ADP-ribosylation

Inferred from direct assay PubMed 15674325. Source: UniProtKB

regulation of growth rate

Inferred from electronic annotation. Source: Ensembl

signal transduction involved in regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 10944198. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentnuclear envelope

Inferred from direct assay Ref.22. Source: UniProtKB

nucleolus

Inferred from direct assay PubMed 16107709Ref.22. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from direct assay PubMed 19303849. Source: BHF-UCL

   Molecular_functionDNA binding

Traceable author statement Ref.4. Source: ProtInc

NAD binding

Inferred from electronic annotation. Source: Ensembl

NAD+ ADP-ribosyltransferase activity

Inferred from direct assay PubMed 16107709Ref.26. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 23382074. Source: UniProt

identical protein binding

Inferred from physical interaction PubMed 14734561PubMed 23481255. Source: IntAct

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 16107709. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11248244Ref.24Ref.26Ref.28Ref.33PubMed 21549307Ref.41Ref.44Ref.22. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 19303849. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 10141013Poly [ADP-ribose] polymerase 1
PRO_0000211320

Regions

Domain385 – 47692BRCT
Domain662 – 779118PARP alpha-helical
Domain788 – 1014227PARP catalytic
DNA binding2 – 372371
Zinc finger9 – 9385PARP-type 1
Zinc finger113 – 20391PARP-type 2
Region373 – 524152Automodification domain
Motif207 – 2093Nuclear localization signal Ref.20
Motif221 – 2266Nuclear localization signal Ref.20

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.43
Modified residue411Phosphoserine Ref.35
Modified residue971N6-acetyllysine Ref.34
Modified residue1051N6-acetyllysine Ref.34
Modified residue1311N6-acetyllysine Ref.34
Modified residue1791Phosphoserine Ref.27
Modified residue3681Phosphothreonine Ref.29
Modified residue4071PolyADP-ribosyl glutamic acid Potential
Modified residue4131PolyADP-ribosyl glutamic acid Potential
Modified residue4351PolyADP-ribosyl glutamic acid Potential
Modified residue4371PolyADP-ribosyl glutamic acid Potential
Modified residue4441PolyADP-ribosyl glutamic acid Potential
Modified residue4451PolyADP-ribosyl glutamic acid Potential
Modified residue4481PolyADP-ribosyl glutamic acid Potential
Modified residue4561PolyADP-ribosyl glutamic acid Potential
Modified residue4711PolyADP-ribosyl glutamic acid Potential
Modified residue4841PolyADP-ribosyl glutamic acid Potential
Modified residue4881PolyADP-ribosyl glutamic acid Potential
Modified residue4911PolyADP-ribosyl glutamic acid Potential
Modified residue5131PolyADP-ribosyl glutamic acid Potential
Modified residue5141PolyADP-ribosyl glutamic acid Potential
Modified residue5201PolyADP-ribosyl glutamic acid Potential
Modified residue6001N6-acetyllysine Ref.34
Modified residue6211N6-acetyllysine Ref.34
Modified residue7821Phosphoserine Ref.29 Ref.32 Ref.35 Ref.40

Natural variations

Natural variant541F → L.
Corresponds to variant rs3738708 [ dbSNP | Ensembl ].
VAR_050460
Natural variant1881A → T. Ref.5
Corresponds to variant rs1805409 [ dbSNP | Ensembl ].
VAR_014714
Natural variant3341V → I. Ref.5
Corresponds to variant rs3219057 [ dbSNP | Ensembl ].
VAR_019171
Natural variant3771P → S.
Corresponds to variant rs2230484 [ dbSNP | Ensembl ].
VAR_050461
Natural variant3831S → Y. Ref.5
Corresponds to variant rs3219062 [ dbSNP | Ensembl ].
VAR_019172
Natural variant4881E → V in a breast cancer sample; somatic mutation. Ref.46
VAR_035852
Natural variant7621V → A. Ref.5 Ref.8
Corresponds to variant rs1136410 [ dbSNP | Ensembl ].
VAR_014715
Natural variant9401K → R. Ref.3 Ref.5
Corresponds to variant rs3219145 [ dbSNP | Ensembl ].
VAR_019173

Experimental info

Mutagenesis7971L → P: 1.5% of wild-type activity. Ref.19 Ref.21
Mutagenesis8681N → S: 4% of wild-type activity. Ref.19 Ref.21
Mutagenesis8901M → V: <0.5% of wild-type activity. Ref.19 Ref.21
Mutagenesis8931K → I: Abolishes enzymatic activity. Ref.19 Ref.21
Mutagenesis8971F → S: 10% of wild-type activity. Ref.19 Ref.21
Mutagenesis8991D → N: 0.6% of wild-type activity. Ref.19 Ref.21
Mutagenesis9081C → R: <0.5% of wild-type activity. Ref.19 Ref.21
Mutagenesis9261L → F: 1.5% of wild-type activity. Ref.19 Ref.21
Mutagenesis9861Y → H: 14% of wild-type activity and increased branching 15-fold. Ref.19 Ref.21
Mutagenesis9881E → K: 1.25% of wild-type activity; only monomers are added. Ref.19 Ref.21
Mutagenesis10031L → P: 1.5% of wild-type activity. Ref.19 Ref.21
Sequence conflict171G → E in AAB59447. Ref.2
Sequence conflict701E → Q in AAA60137. Ref.1
Sequence conflict2121E → K in AAB59447. Ref.2
Sequence conflict6131H → Q in AAA60155. Ref.3
Sequence conflict8271N → S in AAA60155. Ref.3
Sequence conflict9081C → Y in AAA60155. Ref.3
Sequence conflict9801N → I in AAA60155. Ref.3

Secondary structure

................................................................................................................................................................................ 1014
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09874 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6A5FC01EB91C046B

FASTA1,014113,084
        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 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase."
Uchida K., Morita T., Sato T., Ogura T., Yamashita R., Noguchi S., Suzuki H., Nyunoya H., Miwa M., Sugimura T.
Biochem. Biophys. Res. Commun. 148:617-622(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence."
Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M., Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S., Shizuta Y.
J. Biol. Chem. 262:15990-15997(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[3]"cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase."
Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K., Hensley P., Smulson M.E.
Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-940.
[4]"Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene."
Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.
DNA 8:575-580(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]NIEHS SNPs program
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-188; ILE-334; TYR-383; ALA-762 AND ARG-940.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-762.
Tissue: Brain.
[9]"Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region."
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.
Eur. J. Biochem. 194:521-526(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
[10]"Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene."
Ogura T., Nyunoya H., Takahashi-Masutani M., Miwa M., Sugimura T., Esumi H.
Biochem. Biophys. Res. Commun. 167:701-710(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[11]"Human pADPRT is involved in the regulation of its own gene."
Herzog H., Schneider R., Hirsch-Kauffmann M., Schnitzer D., Schweiger M.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[12]Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[13]"Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells."
Maruyama T., Nara K., Yoshikawa H., Suzuki N.
Clin. Exp. Immunol. 147:164-175(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 166-177 AND 356-367, INTERACTION WITH EEF1A1 AND TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, FUNCTION AS A TRANSCRIPTION FACTOR.
[14]"Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase."
Schneider R., Auer B., Kuhne C., Herzog H., Klocker H., Burtscher H.J., Hirsch-Kauffmann M., Wintersberger U., Schweiger M.
Eur. J. Cell Biol. 44:302-307(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 381-420 AND 682-710.
[15]"Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation."
Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
Biochem. Biophys. Res. Commun. 146:403-409(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 441-1014.
[16]Erratum
Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
Biochem. Biophys. Res. Commun. 148:1549-1550(1987)
[17]"The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA."
Gradwohl G., Menissier-de Murcia J., Molinete M., Simonin F., Koken M.H.M., Hoeijmakers J.H.J., de Murcia G.M.
Proc. Natl. Acad. Sci. U.S.A. 87:2990-2994(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ANALYSIS OF ZINC-FINGERS.
[18]"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."
Ikelima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., Miwa M.
J. Biol. Chem. 265:21907-21913(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ANALYSIS OF ZINC-FINGERS.
[19]"Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity."
Simonin F., Menissier-de Murcia J., Poch O., Muller S., Gradwohl G., Molinete M., Penning C., Keith G., de Murcia G.M.
J. Biol. Chem. 265:19249-19256(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
[20]"The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity."
Schreiber V., Molinete M., Boeuf H., de Murcia G.M., Menissier-de Murcia J.
EMBO J. 11:3263-3269(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL.
[21]"Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching."
Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G.M.
Biochemistry 36:12147-12154(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
[22]"Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Menissier-de Murcia J.
Nucleic Acids Res. 26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLA1.
[23]"Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro."
Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T., Shimotohno K., Ueda K., Hatanaka M., Noda M.
Oncogene 18:4616-4625(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[24]"Aprataxin, a novel protein that protects against genotoxic stress."
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.
Hum. Mol. Genet. 13:1081-1093(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APTX.
[25]"The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions."
Li Y., Oh H.J., Lau Y.-F.C.
Mol. Cell. Endocrinol. 257:35-46(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRY.
[26]"A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APLF.
[27]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[28]"Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins."
Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C.
Nature 451:81-85(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[29]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[30]"Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes."
Reinemund J., Seidel K., Steckelings U.M., Zaade D., Klare S., Rompe F., Katerbaum M., Schacherl J., Li Y., Menk M., Schefe J.H., Goldin-Lang P., Szabo C., Olah G., Unger T., Funke-Kaiser H.
Biochem. Pharmacol. 77:1795-1805(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF4.
[32]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[33]"Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1."
Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.
Science 325:1240-1243(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, POLY-ADP-RIBOSYLATION, INTERACTION WITH CHD1L.
[34]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-105; LYS-131; LYS-600 AND LYS-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[37]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Poly(ADP-ribose)-dependent regulation of Snail1 protein stability."
Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J., de Herreros A.G., Oliver F.J.
Oncogene 30:4365-4372(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAI1.
[39]"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling."
Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S., Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S., Polakis P., Costa M.
PLoS ONE 6:E22595-E22595(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF146, SUBCELLULAR LOCATION.
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H. expand/collapse author list , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF423.
[42]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[43]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8."
Yan Q., Xu R., Zhu L., Cheng X., Wang Z., Manis J., Shipp M.A.
Mol. Cell. Biol. 33:845-857(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP9.
[45]"Solution structure of the first ZF-PARP domain, of the BRCT domain and of the WGR domain of human poly(ADP-ribose)polymerase-1."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-93 AND 385-643.
[46]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-488.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18112 mRNA. Translation: AAA60137.1.
J03473 mRNA. Translation: AAB59447.1.
M32721 mRNA. Translation: AAA60155.1.
M29786 expand/collapse EMBL AC list , M29545, M29766, M29767, M29768, M29769, M29770, M29771, M29772, M29773, M29774, M29775, M29776, M29777, M29778, M29779, M29780, M29781, M29783, M29784, M29785, M29544, M29782 Genomic DNA. Translation: AAA51663.1.
AF524947 Genomic DNA. Translation: AAM75364.1.
AL359704, AL359742 Genomic DNA. Translation: CAH70215.1.
AL359742, AL359704 Genomic DNA. Translation: CAI12102.1.
CH471098 Genomic DNA. Translation: EAW69783.1.
BC037545 mRNA. Translation: AAH37545.1.
X56140, X56141 Genomic DNA. Translation: CAA39606.1.
X16674 Genomic DNA. Translation: CAA34663.1.
M60436 Genomic DNA. Translation: AAA60000.1.
M17081 mRNA. Translation: AAA51599.1. Sequence problems.
CCDSCCDS1554.1.
PIRA29725.
RefSeqNP_001609.2. NM_001618.3.
UniGeneHs.177766.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UK0X-ray3.00A/B662-1011[»]
1UK1X-ray3.00A/B662-1011[»]
1WOKX-ray3.00A/B/C/D662-1011[»]
2COKNMR-A387-486[»]
2CR9NMR-A518-643[»]
2CS2NMR-A103-223[»]
2DMJNMR-A1-93[»]
2JVNNMR-A233-358[»]
2L30NMR-A1-108[»]
2L31NMR-A103-214[»]
2RCWX-ray2.80A662-1011[»]
2RD6X-ray2.30A662-1011[»]
2RIQX-ray1.70A216-366[»]
3GJWX-ray2.30A662-1011[»]
3GN7X-ray2.50A662-1011[»]
3L3LX-ray2.50A662-1011[»]
3L3MX-ray2.50A662-1011[»]
3OD8X-ray2.40A/B/C/D/E/F/G/H2-96[»]
3ODAX-ray2.64A/B/C/D/E/F/G/H2-96[»]
3ODCX-ray2.80A/B105-206[»]
3ODEX-ray2.95A/B105-206[»]
4AV1X-ray3.10A/B/C/D5-202[»]
4DQYX-ray3.25A/D1-96[»]
B/E216-366[»]
C/F518-1014[»]
4GV7X-ray2.89A/B/C/D662-1011[»]
4HHYX-ray2.36A/B/C/D660-1011[»]
4HHZX-ray2.72A/B/C/D660-1011[»]
4L6SX-ray2.20A/B662-1011[»]
ProteinModelPortalP09874.
SMRP09874. Positions 1-359, 381-489, 520-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106652. 192 interactions.
DIPDIP-38N.
IntActP09874. 64 interactions.
MINTMINT-104344.
STRING9606.ENSP00000355759.

Chemistry

BindingDBP09874.
ChEMBLCHEMBL3105.

PTM databases

PhosphoSiteP09874.

Polymorphism databases

DMDM130781.

2D gel databases

SWISS-2DPAGEP09874.

Proteomic databases

MaxQBP09874.
PaxDbP09874.
PeptideAtlasP09874.
PRIDEP09874.

Protocols and materials databases

DNASU142.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366794; ENSP00000355759; ENSG00000143799.
GeneID142.
KEGGhsa:142.
UCSCuc001hqd.4. human.

Organism-specific databases

CTD142.
GeneCardsGC01M226548.
H-InvDBHIX0023551.
HGNCHGNC:270. PARP1.
HPACAB000147.
CAB003839.
CAB003840.
HPA045168.
MIM173870. gene.
neXtProtNX_P09874.
PharmGKBPA32.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243963.
HOGENOMHOG000030402.
HOVERGENHBG053513.
InParanoidP09874.
KOK10798.
OMAITAWTKC.
OrthoDBEOG7KM5S0.
PhylomeDBP09874.
TreeFamTF316616.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkP09874.

Gene expression databases

ArrayExpressP09874.
BgeeP09874.
CleanExHS_PARP1.
GenevestigatorP09874.

Family and domain databases

Gene3D1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProIPR001357. BRCT_dom.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFPIRSF000489. NAD_ADPRT. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 2 hits.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARP1. human.
EvolutionaryTraceP09874.
GeneWikiPARP1.
GenomeRNAi142.
NextBio565.
PMAP-CutDBP09874.
PROP09874.
SOURCESearch...

Entry information

Entry namePARP1_HUMAN
AccessionPrimary (citable) accession number: P09874
Secondary accession number(s): B1ANJ4, Q8IUZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 186 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM