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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

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

Functioni

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. Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.By similarity

Catalytic activityi

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi2 – 372Add BLAST371
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

GO - Molecular functioni

GO - Biological processi

  • ATP generation from poly-ADP-D-ribose Source: UniProtKB
  • base-excision repair Source: MGI
  • behavioral response to cocaine Source: MGI
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to insulin stimulus Source: MGI
  • cellular response to oxidative stress Source: MGI
  • cellular response to superoxide Source: MGI
  • DNA ligation involved in DNA repair Source: GO_Central
  • DNA metabolic process Source: MGI
  • DNA repair Source: MGI
  • double-strand break repair Source: UniProtKB
  • lagging strand elongation Source: GO_Central
  • mitochondrial DNA metabolic process Source: MGI
  • mitochondrial DNA repair Source: MGI
  • mitochondrion organization Source: MGI
  • negative regulation of ATP biosynthetic process Source: MGI
  • negative regulation of interleukin-17 secretion Source: MGI
  • negative regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • protein ADP-ribosylation Source: MGI
  • protein modification process Source: MGI
  • protein poly-ADP-ribosylation Source: MGI
  • regulation of cellular protein localization Source: MGI
  • regulation of growth rate Source: MGI
  • regulation of single strand break repair Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • telomere maintenance Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1340806. Parp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • nuclear chromosome, telomeric region Source: MGI
  • nuclear envelope Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: BHF-UCL
  • protein complex Source: MGI
  • transcription factor 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

Chemistry databases

ChEMBLiCHEMBL3740.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000232592 – 1013Poly [ADP-ribose] polymerase 1Add BLAST1012

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei97N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Modified residuei185PhosphoserineBy similarity1
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei274PhosphoserineBy similarity1
Modified residuei277PhosphoserineBy similarity1
Modified residuei407PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei413PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei435PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei437PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei444PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei448PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei456PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei484PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei488PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei491PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei512PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei519PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei599N6-acetyllysineBy similarity1
Modified residuei620N6-acetyllysineBy similarity1
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei781PhosphoserineBy similarity1
Modified residuei785PhosphoserineBy similarity1

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, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP11103.
MaxQBiP11103.
PaxDbiP11103.
PeptideAtlasiP11103.
PRIDEiP11103.

PTM databases

iPTMnetiP11103.
PhosphoSitePlusiP11103.

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.

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 (PubMed:17320046). Interacts with ZNF423 (PubMed:14623329). Interacts with RNF4 (PubMed:19779455). 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 (PubMed:21577210). Interacts (when poly-ADP-ribosylated) with PARP9 (By similarity). Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (By similarity). Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress. Interacts (via the PARP catalytic domain) with HPF1 (By similarity).By similarity4 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-39371N.
IntActiP11103. 13 interactors.
MINTiMINT-237428.
STRINGi10090.ENSMUSP00000027777.

Chemistry databases

BindingDBiP11103.

Structurei

3D structure databases

ProteinModelPortaliP11103.
SMRiP11103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini385 – 476BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini661 – 778PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini787 – 1013PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 523Automodification domainAdd BLAST151

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi207 – 209Nuclear localization signal3
Motifi221 – 226Nuclear localization signal6

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)DescriptionActionsGraphical viewLength
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOVERGENiHBG053513.
InParanoidiP11103.
PhylomeDBiP11103.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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.
IPR012982. PADR1.
IPR008288. PARP.
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.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[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. AlignAdd to basket

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: Short1 Publication, sPARP-11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-521: Missing.

Note: No experimental confirmation available.
Show »
Length:492
Mass (Da):55,237
Checksum:i6F429A5F21D15246
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti114A → L AA sequence (PubMed:9642267).Curated1
Sequence conflicti591L → V in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti608E → D in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti612Q → H in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti629N → D in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti679D → E in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti717Q → E in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti758Q → L in AAF61293 (PubMed:10809783).Curated1
Sequence conflicti982A → C in AAF61293 (PubMed:10809783).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189701 – 521Missing in isoform 2. 1 PublicationAdd BLAST521

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X14206 mRNA. Translation: CAA32421.1.
AF126717 mRNA. Translation: AAF61293.1. Different initiation.
PIRiS04200.
UniGeneiMm.277779.

3D structure databases

ProteinModelPortaliP11103.
SMRiP11103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39371N.
IntActiP11103. 13 interactors.
MINTiMINT-237428.
STRINGi10090.ENSMUSP00000027777.

Chemistry databases

BindingDBiP11103.
ChEMBLiCHEMBL3740.

PTM databases

iPTMnetiP11103.
PhosphoSitePlusiP11103.

Proteomic databases

EPDiP11103.
MaxQBiP11103.
PaxDbiP11103.
PeptideAtlasiP11103.
PRIDEiP11103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1340806. Parp1.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOVERGENiHBG053513.
InParanoidiP11103.
PhylomeDBiP11103.

Miscellaneous databases

PROiP11103.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PARP1.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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.
IPR012982. PADR1.
IPR008288. PARP.
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.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.