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P11103

- PARP1_MOUSE

UniProt

P11103 - PARP1_MOUSE

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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity). 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. 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 (By similarity).By similarity

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi2 – 372371Add
BLAST
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. NAD+ ADP-ribosyltransferase activity Source: MGI
  3. NAD binding Source: InterPro
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: MGI
  2. cellular response to superoxide Source: MGI
  3. DNA metabolic process Source: MGI
  4. DNA repair Source: MGI
  5. double-strand break repair Source: UniProtKB
  6. protein ADP-ribosylation Source: InterPro
  7. regulation of growth rate Source: MGI
  8. regulation of transcription, DNA-templated Source: UniProtKB-KW
  9. telomere maintenance Source: MGI
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 1 (EC:2.4.2.30)
Short name:
PARP-1
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
Short name:
msPARP
Gene namesi
Name:Parp1
Synonyms:Adprp, Adprt, Adprt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1340806. Parp1.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity
Note: Localizes at sites of DNA damage.By similarity

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nucleolus Source: MGI
  3. nucleoplasm Source: MGI
  4. nucleus Source: BHF-UCL
  5. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice show a complete lack of nuclear poly(ADP-ribosyl)ation. Mice are however viable and fertile. Moreover, repair of UV and MNNG induced DNA damage are not affected. However, about 30% of the mutant mice developed pathological skin aberrations on a mixed 129/Sv x C57B1/6 genetic background.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10131012Poly [ADP-ribose] polymerase 1PRO_0000023259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei97 – 971N6-acetyllysine1 Publication
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei179 – 1791PhosphoserineBy similarity
Modified residuei407 – 4071PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei413 – 4131PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei435 – 4351PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei437 – 4371PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei444 – 4441PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei445 – 4451PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei448 – 4481PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei456 – 4561PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei484 – 4841PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei488 – 4881PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei491 – 4911PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei512 – 5121PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei513 – 5131PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei519 – 5191PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei599 – 5991N6-acetyllysineBy similarity
Modified residuei620 – 6201N6-acetyllysineBy similarity
Modified residuei781 – 7811PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PRKDC and TXK.
Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity).By similarity
S-nitrosylated, leading to inhibit transcription regulation activity.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP11103.
PaxDbiP11103.
PRIDEiP11103.

PTM databases

PhosphoSiteiP11103.

Expressioni

Tissue specificityi

Widely expressed. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult. Expressed in B-cells that have been induced to switch to various Ig isotypes.1 Publication

Developmental stagei

At stage E12.5, expressed at high level in the developing liver and kidneys. Expressed at higher level in the genital ridge and the spinal ganglia. At E18.5, preferentially expressed in the thymus and in regions of the nervous system. Within the developing trunk, preferential expression persisted in the liver and became restricted to the cortical region of the kidney, spleen, adrenal gland, and to stomach and intestinal epithelia. From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus. Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate. Expressed at high level in the seminiferous tubules of the developing testis.1 Publication

Gene expression databases

CleanExiMM_PARP1.
GenevestigatoriP11103.

Interactioni

Subunit structurei

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 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 (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423. Interacts with RNF4. Interacts with EEF1A1 and TXK (By similarity). Interacts with RNF146 (By similarity). 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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P030872EBI-642213,EBI-1555770From a different organism.
ArntlQ9WTL87EBI-642213,EBI-644534
Casp3P706773EBI-642213,EBI-1790419
Casp7P978643EBI-642213,EBI-5307197
Pou5f1P202632EBI-642213,EBI-1606219

Protein-protein interaction databases

DIPiDIP-39371N.
IntActiP11103. 12 interactions.
MINTiMINT-237428.

Structurei

3D structure databases

ProteinModelPortaliP11103.
SMRiP11103. Positions 5-94, 108-359, 388-486, 519-1010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini385 – 47692BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini661 – 778118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini787 – 1013227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni373 – 523151Automodification domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2093Nuclear localization signal
Motifi221 – 2266Nuclear localization signal

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 2 PARP-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243963.
HOVERGENiHBG053513.
InParanoidiP11103.
PhylomeDBiP11103.

Family and domain databases

Gene3Di1.20.142.10. 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.
InterProiIPR001357. 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]
PfamiPF00533. 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]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P11103-1) [UniParc]FASTAAdd to Basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD
110 120 130 140 150
GSGGKAEKTL GDFAAEYAKS NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP
210 220 230 240 250
AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA QNELIWNIKD
260 270 280 290 300
ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK
410 420 430 440 450
LSQNKDEAKA VIEKLGGKLT GSANKASLCI SIKKEVEKMN KKMEEVKEAN
460 470 480 490 500
IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP WGAEVKAEPG EVVAPRGKSA
510 520 530 540 550
APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH SAHVLEKGGK
560 570 580 590 600
VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL
610 620 630 640 650
EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA
660 670 680 690 700
VKKLTVKPGT KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL
710 720 730 740 750
SRRQIQAAYS ILSEVQQPVS QGSSESQILD LSNRFYTLIP HDFGMKKPPL
760 770 780 790 800
LNNADSVQAK VEMLDNLLDI EVAYSLLRGG SDDSSKDPID VNYEKLKTDI
810 820 830 840 850
KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER EGESQRYKPF
860 870 880 890 900
RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
910 920 930 940 950
SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL
960 970 980 990 1000
GKTTPDPSAS ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY
1010
LLKLKFNFKT SLW
Length:1,013
Mass (Da):113,100
Last modified:January 23, 2007 - v3
Checksum:i5E54C3E5F60BB922
GO
Isoform 2 (identifier: P11103-2) [UniParc]FASTAAdd to Basket

Also known as: Short, sPARP-1

The sequence of this isoform differs from the canonical sequence as follows:
     2-521: Missing.

Note: No experimental confirmation available.

Show »
Length:493
Mass (Da):55,368
Checksum:iFBD0D37BA9E04DC7
GO

Sequence cautioni

The sequence AAF61293.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141A → L AA sequence (PubMed:9642267)Curated
Sequence conflicti591 – 5911L → V in AAF61293. (PubMed:10809783)Curated
Sequence conflicti608 – 6081E → D in AAF61293. (PubMed:10809783)Curated
Sequence conflicti612 – 6121Q → H in AAF61293. (PubMed:10809783)Curated
Sequence conflicti629 – 6291N → D in AAF61293. (PubMed:10809783)Curated
Sequence conflicti679 – 6791D → E in AAF61293. (PubMed:10809783)Curated
Sequence conflicti717 – 7171Q → E in AAF61293. (PubMed:10809783)Curated
Sequence conflicti758 – 7581Q → L in AAF61293. (PubMed:10809783)Curated
Sequence conflicti982 – 9821A → C in AAF61293. (PubMed:10809783)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 521520Missing in isoform 2. 1 PublicationVSP_018970Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14206 mRNA. Translation: CAA32421.1.
AF126717 mRNA. Translation: AAF61293.1. Different initiation.
PIRiS04200.
UniGeneiMm.277779.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14206 mRNA. Translation: CAA32421.1 .
AF126717 mRNA. Translation: AAF61293.1 . Different initiation.
PIRi S04200.
UniGenei Mm.277779.

3D structure databases

ProteinModelPortali P11103.
SMRi P11103. Positions 5-94, 108-359, 388-486, 519-1010.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-39371N.
IntActi P11103. 12 interactions.
MINTi MINT-237428.

Chemistry

BindingDBi P11103.
ChEMBLi CHEMBL3740.

PTM databases

PhosphoSitei P11103.

Proteomic databases

MaxQBi P11103.
PaxDbi P11103.
PRIDEi P11103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1340806. Parp1.

Phylogenomic databases

eggNOGi NOG243963.
HOVERGENi HBG053513.
InParanoidi P11103.
PhylomeDBi P11103.

Miscellaneous databases

PROi P11103.
SOURCEi Search...

Gene expression databases

CleanExi MM_PARP1.
Genevestigatori P11103.

Family and domain databases

Gene3Di 1.20.142.10. 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.
InterProi IPR001357. 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 ]
Pfami PF00533. 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 ]
PIRSFi PIRSF000489. NAD_ADPRT. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view ]
SUPFAMi SSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and organization of the mouse poly (ADP-ribose) polymerase gene."
    Huppi K., Bhatia K., Siwarski D., Klinman D., Cherney B., Smulson M.
    Nucleic Acids Res. 17:3387-3401(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BXSB.
  2. "Characterization of sPARP-1. An alternative product of PARP-1 gene with poly(ADP-ribose) polymerase activity independent of DNA strand breaks."
    Sallmann F.R., Vodenicharov M.D., Wang Z.-Q., Poirier G.G.
    J. Biol. Chem. 275:15504-15511(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
    Strain: C57BL/6 X 129/Sv.
    Tissue: Fibroblast.
  3. Cited for: PROTEIN SEQUENCE OF 109-119 AND 865-875, SUBUNIT, TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Spleen.
  4. "On the biological role of the nuclear polymerizing NAD+: protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse."
    Auer B., Flick K., Wang Z.Q., Haidacher D., Jaeger S., Berghammer H., Kofler B., Schweiger M., Wagner E.F.
    Biochimie 77:444-449(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1."
    Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M.
    J. Biol. Chem. 277:23028-23036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  6. "Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target genes."
    Ku M.-C., Stewart S., Hata A.
    Biochem. Biophys. Res. Commun. 311:702-707(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF423.
  7. "Nitric oxide-dependent negative feedback of PARP-1 trans-activation of the inducible nitric-oxide synthase gene."
    Yu Z., Kuncewicz T., Dubinsky W.P., Kone B.C.
    J. Biol. Chem. 281:9101-9109(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION.
  8. Cited for: INTERACTION WITH TIAM2.
  9. "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.
  10. "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.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPARP1_MOUSE
AccessioniPrimary (citable) accession number: P11103
Secondary accession number(s): Q9JLX4, Q9QVQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3