Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Single-strand selective monofunctional uracil-DNA glycosylase

Gene

Smug1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate; via amide nitrogenBy similarity
Binding sitei98 – 981Substrate; via amide nitrogenBy similarity
Binding sitei163 – 1631SubstrateBy similarity
Binding sitei239 – 2391SubstrateBy similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Source: RGD
  • single-strand selective uracil DNA N-glycosylase activity Source: HGNC
  • uracil DNA N-glycosylase activity Source: HGNC

GO - Biological processi

  • base-excision repair Source: HGNC
  • DNA repair Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BRENDAi3.2.2.27. 5301.
ReactomeiR-RNO-110329. Cleavage of the damaged pyrimidine.
R-RNO-110357. Displacement of DNA glycosylase by APEX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Single-strand selective monofunctional uracil-DNA glycosylase (EC:3.2.2.-)
Gene namesi
Name:Smug1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi631403. Smug1.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • nuclear lumen Source: GO_Central
  • nucleolus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278Single-strand selective monofunctional uracil-DNA glycosylasePRO_0000071994Add
BLAST

Proteomic databases

PaxDbiQ811Q1.
PRIDEiQ811Q1.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052164.

Structurei

3D structure databases

ProteinModelPortaliQ811Q1.
SMRiQ811Q1. Positions 26-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 18715DNA bindingBy similarityAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IFBA. Eukaryota.
ENOG410XQUR. LUCA.
GeneTreeiENSGT00390000004897.
HOGENOMiHOG000220288.
HOVERGENiHBG084399.
InParanoidiQ811Q1.
KOiK10800.
OMAiIMHPSPR.
OrthoDBiEOG7W41CR.
PhylomeDBiQ811Q1.
TreeFamiTF324356.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.

Sequencei

Sequence statusi: Complete.

Q811Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSQTFPPG PAHEPASALM EPCARSLAEG FLEEELRLNA ELSQLQFPEP
60 70 80 90 100
VGVIYNPVDY AWEPHRNYVT RYCQGPKEVL FLGMNPGPFG MAQTGVPFGE
110 120 130 140 150
VNVVRDWLGI GGSVLSPPQE HPKRPVLGLE CPQSEVSGAR FWGFFRTLCG
160 170 180 190 200
QPQVFFRHCF VHNLCPLLFL APSGRNLTPA DLPAKHREQL LSICDAALCR
210 220 230 240 250
QVQLLGVRLV VGVGRLAEQR ARRALAGLTP EVQVEGLLHP SPRSPQANKG
260 270
WETAARERLQ ELGLLPLLTD EGSVRPTP
Length:278
Mass (Da):30,562
Last modified:June 1, 2003 - v1
Checksum:iC1A047F60AB76F56
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191521 mRNA. Translation: AAO38671.1.
RefSeqiNP_808795.1. NM_177934.3.
XP_006242461.1. XM_006242399.2.
XP_008763971.1. XM_008765749.1.
UniGeneiRn.162974.

Genome annotation databases

EnsembliENSRNOT00000055290; ENSRNOP00000052164; ENSRNOG00000036842.
ENSRNOT00000082149; ENSRNOP00000069685; ENSRNOG00000036842.
GeneIDi315344.
KEGGirno:315344.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191521 mRNA. Translation: AAO38671.1.
RefSeqiNP_808795.1. NM_177934.3.
XP_006242461.1. XM_006242399.2.
XP_008763971.1. XM_008765749.1.
UniGeneiRn.162974.

3D structure databases

ProteinModelPortaliQ811Q1.
SMRiQ811Q1. Positions 26-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000052164.

Proteomic databases

PaxDbiQ811Q1.
PRIDEiQ811Q1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000055290; ENSRNOP00000052164; ENSRNOG00000036842.
ENSRNOT00000082149; ENSRNOP00000069685; ENSRNOG00000036842.
GeneIDi315344.
KEGGirno:315344.

Organism-specific databases

CTDi23583.
RGDi631403. Smug1.

Phylogenomic databases

eggNOGiENOG410IFBA. Eukaryota.
ENOG410XQUR. LUCA.
GeneTreeiENSGT00390000004897.
HOGENOMiHOG000220288.
HOVERGENiHBG084399.
InParanoidiQ811Q1.
KOiK10800.
OMAiIMHPSPR.
OrthoDBiEOG7W41CR.
PhylomeDBiQ811Q1.
TreeFamiTF324356.

Enzyme and pathway databases

BRENDAi3.2.2.27. 5301.
ReactomeiR-RNO-110329. Cleavage of the damaged pyrimidine.
R-RNO-110357. Displacement of DNA glycosylase by APEX1.

Miscellaneous databases

PROiQ811Q1.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions."
    Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H., Ohyama Y., Karino N., Matsuda A., Ide H.
    Biochemistry 42:5003-5012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: Wistar.
    Tissue: Kidney.

Entry informationi

Entry nameiSMUG1_RAT
AccessioniPrimary (citable) accession number: Q811Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.