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Protein

Uracil-DNA glycosylase

Gene

UNG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.

Catalytic activityi

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei154Proton acceptorUniRule annotation1

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • uracil DNA N-glycosylase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS01204-MONOMER.
BRENDAi3.2.2.27. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.
SABIO-RKP13051.

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylaseUniRule annotation (EC:3.2.2.27UniRule annotation)
Short name:
UDGUniRule annotation
Gene namesi
Name:UNGUniRule annotation
Synonyms:DGU, UNG1UniRule annotation, UNG15UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12572. UNG.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency with hyper-IgM 5 (HIGM5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.
See also OMIM:608106
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017094251F → S in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus. 2 PublicationsCorresponds to variant rs104894380dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi154D → E or N: Loss of activity. 1 Publication1
Mutagenesisi156Y → A, C or S: Thymine-DNA glycosylase activity. 1 Publication1
Mutagenesisi213N → D: Cytosine-DNA glycosylase activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi7374.
MalaCardsiUNG.
MIMi608106. phenotype.
OpenTargetsiENSG00000076248.
Orphaneti101092. Hyper-IgM syndrome type 5.
PharmGKBiPA364.

Chemistry databases

ChEMBLiCHEMBL3277.

Polymorphism and mutation databases

BioMutaiUNG.
DMDMi37999897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001761731 – 313Uracil-DNA glycosylaseAdd BLAST313

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphoserineCombined sources1
Modified residuei14PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei60PhosphothreonineCombined sources1
Modified residuei64PhosphoserineCombined sources1
Modified residuei295N6-acetyllysineCombined sources1

Post-translational modificationi

Isoform 1 is processed by cleavage of a transit peptide.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP13051.
MaxQBiP13051.
PaxDbiP13051.
PeptideAtlasiP13051.
PRIDEiP13051.

PTM databases

iPTMnetiP13051.
PhosphoSitePlusiP13051.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed with the highest expression in skeletal muscle, heart and testicles. Isoform 2 has the highest expression levels in tissues containing proliferating cells.

Gene expression databases

BgeeiENSG00000076248.
CleanExiHS_UNG.
ExpressionAtlasiP13051. baseline and differential.
GenevisibleiP13051. HS.

Organism-specific databases

HPAiCAB011605.

Interactioni

Subunit structurei

Monomer. Interacts with FAM72A. Interacts with HIV-1 Vpr.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPA2P159276EBI-1025947,EBI-621404

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113220. 19 interactors.
DIPiDIP-24194N.
IntActiP13051. 10 interactors.
MINTiMINT-1507980.
STRINGi9606.ENSP00000242576.

Chemistry databases

BindingDBiP13051.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi77 – 86Combined sources10
Helixi96 – 102Combined sources7
Helixi103 – 105Combined sources3
Helixi109 – 124Combined sources16
Beta strandi127 – 129Combined sources3
Helixi131 – 133Combined sources3
Helixi136 – 138Combined sources3
Beta strandi139 – 141Combined sources3
Helixi143 – 145Combined sources3
Beta strandi148 – 152Combined sources5
Turni159 – 161Combined sources3
Beta strandi163 – 165Combined sources3
Helixi177 – 189Combined sources13
Turni190 – 192Combined sources3
Helixi202 – 205Combined sources4
Turni206 – 208Combined sources3
Beta strandi209 – 215Combined sources7
Turni223 – 228Combined sources6
Helixi231 – 245Combined sources15
Beta strandi250 – 255Combined sources6
Helixi256 – 261Combined sources6
Turni262 – 264Combined sources3
Turni267 – 269Combined sources3
Beta strandi270 – 275Combined sources6
Turni280 – 282Combined sources3
Helixi283 – 285Combined sources3
Turni286 – 289Combined sources4
Helixi292 – 302Combined sources11
Turni310 – 313Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKZX-ray1.57A94-313[»]
1DPUNMR-B73-88[»]
1EMHX-ray1.80A94-313[»]
1EMJX-ray2.00A94-313[»]
1Q3FX-ray1.90A94-313[»]
1SSPX-ray1.90E94-313[»]
1UGHX-ray1.90E94-313[»]
1YUOX-ray1.95A91-313[»]
2HXMX-ray1.30A94-313[»]
2OXMX-ray2.50A94-313[»]
2OYTX-ray2.00A94-313[»]
2SSPX-ray2.25E94-313[»]
3FCFX-ray1.84A94-313[»]
3FCIX-ray1.27A94-313[»]
3FCKX-ray1.64B94-313[»]
3FCLX-ray1.70A/B94-313[»]
3TKBX-ray1.50A94-313[»]
4SKNX-ray2.90E94-313[»]
5AYRX-ray2.40A/C94-313[»]
5JK7X-ray3.49D/G94-313[»]
ProteinModelPortaliP13051.
SMRiP13051.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13051.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 25FAM72A-bindingAdd BLAST25

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG2994. Eukaryota.
COG0692. LUCA.
GeneTreeiENSGT00390000003405.
HOGENOMiHOG000229528.
HOVERGENiHBG000396.
InParanoidiP13051.
KOiK03648.
OMAiKEPINWK.
OrthoDBiEOG091G0HEH.
PhylomeDBiP13051.
TreeFamiTF315028.

Family and domain databases

CDDicd10027. UDG_F1. 1 hit.
Gene3Di3.40.470.10. 1 hit.
HAMAPiMF_00148. UDG. 1 hit.
InterProiIPR002043. UDG_fam1.
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERiPTHR11264. PTHR11264. 1 hit.
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SMARTiSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
TIGRFAMsiTIGR00628. ung. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P13051-1) [UniParc]FASTAAdd to basket
Also known as: UNG2

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
MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK
60 70 80 90 100
APAGQEEPGT PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK
110 120 130 140 150
HLSGEFGKPY FIKLMGFVAE ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI
160 170 180 190 200
LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE NIYKELSTDI EDFVHPGHGD
210 220 230 240 250
LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS WLNQNSNGLV
260 270 280 290 300
FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL
310
QKSGKKPIDW KEL
Length:313
Mass (Da):34,645
Last modified:October 10, 2003 - v2
Checksum:iA4B27E6198AFE9C0
GO
Isoform 1 (identifier: P13051-2) [UniParc]FASTAAdd to basket
Also known as: UNG1

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MIGQKTLYSF...GVPEESGDAA → MGVFCLGPWGLGRKLRTPGKGPLQLLSRLCGDHLQ

Show »
Length:304
Mass (Da):33,924
Checksum:i32998C244E47B215
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0526974Q → R.Corresponds to variant rs7488798dbSNPEnsembl.1
Natural variantiVAR_017094251F → S in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus. 2 PublicationsCorresponds to variant rs104894380dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0085131 – 44MIGQK…SGDAA → MGVFCLGPWGLGRKLRTPGK GPLQLLSRLCGDHLQ in isoform 1. 3 PublicationsAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15653 mRNA. Translation: CAA33679.1.
X89398 Genomic DNA. Translation: CAA61578.1.
X89398 Genomic DNA. Translation: CAA61579.1.
Y09008 mRNA. Translation: CAA70211.1.
AF526277 Genomic DNA. Translation: AAM77695.1.
AK291341 mRNA. Translation: BAF84030.1.
AK313552 mRNA. Translation: BAG36328.1.
CH471054 Genomic DNA. Translation: EAW97846.1.
CH471054 Genomic DNA. Translation: EAW97847.1.
BC015205 mRNA. Translation: AAH15205.1.
BC050634 mRNA. Translation: AAH50634.1.
CCDSiCCDS9124.1. [P13051-1]
CCDS9125.1. [P13051-2]
PIRiS05964. A60472.
RefSeqiNP_003353.1. NM_003362.3. [P13051-2]
NP_550433.1. NM_080911.2. [P13051-1]
UniGeneiHs.191334.

Genome annotation databases

EnsembliENST00000242576; ENSP00000242576; ENSG00000076248. [P13051-1]
ENST00000336865; ENSP00000337398; ENSG00000076248. [P13051-2]
GeneIDi7374.
KEGGihsa:7374.
UCSCiuc001tnz.3. human. [P13051-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
UNGbase

UNG mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15653 mRNA. Translation: CAA33679.1.
X89398 Genomic DNA. Translation: CAA61578.1.
X89398 Genomic DNA. Translation: CAA61579.1.
Y09008 mRNA. Translation: CAA70211.1.
AF526277 Genomic DNA. Translation: AAM77695.1.
AK291341 mRNA. Translation: BAF84030.1.
AK313552 mRNA. Translation: BAG36328.1.
CH471054 Genomic DNA. Translation: EAW97846.1.
CH471054 Genomic DNA. Translation: EAW97847.1.
BC015205 mRNA. Translation: AAH15205.1.
BC050634 mRNA. Translation: AAH50634.1.
CCDSiCCDS9124.1. [P13051-1]
CCDS9125.1. [P13051-2]
PIRiS05964. A60472.
RefSeqiNP_003353.1. NM_003362.3. [P13051-2]
NP_550433.1. NM_080911.2. [P13051-1]
UniGeneiHs.191334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKZX-ray1.57A94-313[»]
1DPUNMR-B73-88[»]
1EMHX-ray1.80A94-313[»]
1EMJX-ray2.00A94-313[»]
1Q3FX-ray1.90A94-313[»]
1SSPX-ray1.90E94-313[»]
1UGHX-ray1.90E94-313[»]
1YUOX-ray1.95A91-313[»]
2HXMX-ray1.30A94-313[»]
2OXMX-ray2.50A94-313[»]
2OYTX-ray2.00A94-313[»]
2SSPX-ray2.25E94-313[»]
3FCFX-ray1.84A94-313[»]
3FCIX-ray1.27A94-313[»]
3FCKX-ray1.64B94-313[»]
3FCLX-ray1.70A/B94-313[»]
3TKBX-ray1.50A94-313[»]
4SKNX-ray2.90E94-313[»]
5AYRX-ray2.40A/C94-313[»]
5JK7X-ray3.49D/G94-313[»]
ProteinModelPortaliP13051.
SMRiP13051.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113220. 19 interactors.
DIPiDIP-24194N.
IntActiP13051. 10 interactors.
MINTiMINT-1507980.
STRINGi9606.ENSP00000242576.

Chemistry databases

BindingDBiP13051.
ChEMBLiCHEMBL3277.

PTM databases

iPTMnetiP13051.
PhosphoSitePlusiP13051.

Polymorphism and mutation databases

BioMutaiUNG.
DMDMi37999897.

Proteomic databases

EPDiP13051.
MaxQBiP13051.
PaxDbiP13051.
PeptideAtlasiP13051.
PRIDEiP13051.

Protocols and materials databases

DNASUi7374.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242576; ENSP00000242576; ENSG00000076248. [P13051-1]
ENST00000336865; ENSP00000337398; ENSG00000076248. [P13051-2]
GeneIDi7374.
KEGGihsa:7374.
UCSCiuc001tnz.3. human. [P13051-1]

Organism-specific databases

CTDi7374.
DisGeNETi7374.
GeneCardsiUNG.
HGNCiHGNC:12572. UNG.
HPAiCAB011605.
MalaCardsiUNG.
MIMi191525. gene.
608106. phenotype.
neXtProtiNX_P13051.
OpenTargetsiENSG00000076248.
Orphaneti101092. Hyper-IgM syndrome type 5.
PharmGKBiPA364.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2994. Eukaryota.
COG0692. LUCA.
GeneTreeiENSGT00390000003405.
HOGENOMiHOG000229528.
HOVERGENiHBG000396.
InParanoidiP13051.
KOiK03648.
OMAiKEPINWK.
OrthoDBiEOG091G0HEH.
PhylomeDBiP13051.
TreeFamiTF315028.

Enzyme and pathway databases

BioCyciZFISH:HS01204-MONOMER.
BRENDAi3.2.2.27. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.
SABIO-RKP13051.

Miscellaneous databases

ChiTaRSiUNG. human.
EvolutionaryTraceiP13051.
GeneWikiiUracil-DNA_glycosylase.
GenomeRNAii7374.
PROiP13051.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000076248.
CleanExiHS_UNG.
ExpressionAtlasiP13051. baseline and differential.
GenevisibleiP13051. HS.

Family and domain databases

CDDicd10027. UDG_F1. 1 hit.
Gene3Di3.40.470.10. 1 hit.
HAMAPiMF_00148. UDG. 1 hit.
InterProiIPR002043. UDG_fam1.
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERiPTHR11264. PTHR11264. 1 hit.
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SMARTiSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
TIGRFAMsiTIGR00628. ung. 1 hit.
PROSITEiPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUNG_HUMAN
AccessioniPrimary (citable) accession number: P13051
Secondary accession number(s): A8K5M6
, B2R8Y1, O00637, O00719, Q93028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 10, 2003
Last modified: November 30, 2016
This is version 190 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.