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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei154 – 1541Proton acceptorUniRule annotation

GO - Molecular functioni

  1. uracil DNA N-glycosylase activity Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: Reactome
  2. base-excision repair, AP site formation Source: Reactome
  3. depyrimidination Source: Reactome
  4. DNA repair Source: Reactome
  5. negative regulation of apoptotic process Source: Ensembl
  6. somatic hypermutation of immunoglobulin genes Source: Ensembl
  7. somatic recombination of immunoglobulin gene segments Source: Ensembl
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction

Enzyme and pathway databases

BRENDAi3.2.2.27. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_2156. Cleavage of the damaged pyrimidine.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
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
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12572. UNG.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti251 – 2511F → S in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus. 2 Publications
VAR_017094

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541D → E or N: Loss of activity. 1 Publication
Mutagenesisi156 – 1561Y → A, C or S: Thymine-DNA glycosylase activity. 1 Publication
Mutagenesisi213 – 2131N → D: Cytosine-DNA glycosylase activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608106. phenotype.
Orphaneti101092. Hyper-IgM syndrome type 5.
PharmGKBiPA364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Uracil-DNA glycosylasePRO_0000176173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine2 Publications
Modified residuei14 – 141Phosphoserine3 Publications
Modified residuei23 – 231Phosphoserine4 Publications
Modified residuei60 – 601Phosphothreonine4 Publications
Modified residuei64 – 641Phosphoserine2 Publications
Modified residuei295 – 2951N6-acetyllysine1 Publication

Post-translational modificationi

Isoform 1 is processed by cleavage of a transit peptide.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13051.
PaxDbiP13051.
PRIDEiP13051.

PTM databases

PhosphoSiteiP13051.

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

BgeeiP13051.
CleanExiHS_UNG.
ExpressionAtlasiP13051. baseline and differential.
GenevestigatoriP13051.

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

Protein-protein interaction databases

BioGridi113220. 15 interactions.
DIPiDIP-24194N.
IntActiP13051. 7 interactions.
MINTiMINT-1507980.
STRINGi9606.ENSP00000242576.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi77 – 8610Combined sources
Helixi96 – 1027Combined sources
Helixi103 – 1053Combined sources
Helixi109 – 12416Combined sources
Beta strandi127 – 1293Combined sources
Helixi131 – 1333Combined sources
Helixi136 – 1383Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1453Combined sources
Beta strandi148 – 1525Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 1653Combined sources
Helixi177 – 18913Combined sources
Turni190 – 1923Combined sources
Helixi202 – 2054Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 2157Combined sources
Turni223 – 2286Combined sources
Helixi231 – 24515Combined sources
Beta strandi250 – 2556Combined sources
Helixi256 – 2616Combined sources
Turni262 – 2643Combined sources
Turni267 – 2693Combined sources
Beta strandi270 – 2756Combined sources
Turni280 – 2823Combined sources
Helixi283 – 2853Combined sources
Turni286 – 2894Combined sources
Helixi292 – 30211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP13051.
SMRiP13051. Positions 94-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13051.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2525FAM72A-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0692.
GeneTreeiENSGT00390000003405.
HOGENOMiHOG000229528.
HOVERGENiHBG000396.
InParanoidiP13051.
KOiK03648.
OMAiYPAPKNI.
OrthoDBiEOG786H4X.
PhylomeDBiP13051.
TreeFamiTF315028.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
HAMAPiMF_00148. UDG.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41Q → R.
Corresponds to variant rs7488798 [ dbSNP | Ensembl ].
VAR_052697
Natural varianti251 – 2511F → S in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus. 2 Publications
VAR_017094

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444MIGQK…SGDAA → MGVFCLGPWGLGRKLRTPGK GPLQLLSRLCGDHLQ in isoform 1. 3 PublicationsVSP_008513Add
BLAST

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.2. human. [P13051-1]

Polymorphism databases

DMDMi37999897.

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
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[»]
ProteinModelPortaliP13051.
SMRiP13051. Positions 94-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113220. 15 interactions.
DIPiDIP-24194N.
IntActiP13051. 7 interactions.
MINTiMINT-1507980.
STRINGi9606.ENSP00000242576.

Chemistry

BindingDBiP13051.
ChEMBLiCHEMBL3277.

PTM databases

PhosphoSiteiP13051.

Polymorphism databases

DMDMi37999897.

Proteomic databases

MaxQBiP13051.
PaxDbiP13051.
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.2. human. [P13051-1]

Organism-specific databases

CTDi7374.
GeneCardsiGC12P109535.
HGNCiHGNC:12572. UNG.
HPAiCAB011605.
MIMi191525. gene.
608106. phenotype.
neXtProtiNX_P13051.
Orphaneti101092. Hyper-IgM syndrome type 5.
PharmGKBiPA364.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0692.
GeneTreeiENSGT00390000003405.
HOGENOMiHOG000229528.
HOVERGENiHBG000396.
InParanoidiP13051.
KOiK03648.
OMAiYPAPKNI.
OrthoDBiEOG786H4X.
PhylomeDBiP13051.
TreeFamiTF315028.

Enzyme and pathway databases

BRENDAi3.2.2.27. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_2156. Cleavage of the damaged pyrimidine.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
SABIO-RKP13051.

Miscellaneous databases

ChiTaRSiUNG. human.
EvolutionaryTraceiP13051.
GeneWikiiUracil-DNA_glycosylase.
GenomeRNAii7374.
NextBioi28874.
PROiP13051.
SOURCEiSearch...

Gene expression databases

BgeeiP13051.
CleanExiHS_UNG.
ExpressionAtlasiP13051. baseline and differential.
GenevestigatoriP13051.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
HAMAPiMF_00148. UDG.
InterProiIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme."
    Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E.
    EMBO J. 8:3121-3125(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 87-113.
    Tissue: Placenta.
  2. "Structure of the gene for human uracil-DNA glycosylase and analysis of the promoter function."
    Haug T., Skorpen F., Lund H., Krokan H.E.
    FEBS Lett. 353:180-184(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene."
    Nilsen H., Solum K., Haug T., Krokan H.E.
    Nucleic Acids Res. 25:750-755(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  4. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Tongue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  8. "Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene."
    Slupphaug G., Markussen F.-H., Olsen L.C., Aasland R., Aarsaether N., Bakke O., Krokan H.E., Helland D.E.
    Nucleic Acids Res. 21:2579-2584(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase."
    Kavli B., Slupphaug G., Mol C.D., Arvai A.S., Petersen S.B., Tainer J.A., Krohan H.E.
    EMBO J. 15:3442-3447(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  10. "Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme."
    Bouhamdan M., Benichou S., Rey F., Navarro J.-M., Agostini I., Spire B., Camonis J., Slupphaug G., Vigne R., Benarous R., Sire J.
    J. Virol. 70:697-704(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 VPR.
  11. "Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively."
    Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T., Krokan H.E.
    Nucleic Acids Res. 26:4611-4617(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Ugene, a newly identified protein that is commonly overexpressed in cancer and binds uracil DNA glycosylase."
    Guo C., Zhang X., Fink S.P., Platzer P., Wilson K., Willson J.K., Wang Z., Markowitz S.D.
    Cancer Res. 68:6118-6126(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM72A.
  14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23; THR-60 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; THR-60 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23 AND THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis."
    Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krohan H.E., Tainer J.A.
    Cell 80:869-878(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  22. "Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA."
    Mol C.D., Arvai A.S., Sanderson R.J., Slupphaug G., Kavli B., Krokan H.E., Mosbaugh D.W., Tainer J.A.
    Cell 82:701-708(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  23. "A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA."
    Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krohan H.E., Tainer J.A.
    Nature 384:87-92(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
  24. "Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA."
    Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., Tainer J.A.
    EMBO J. 17:5214-5226(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-313.
  25. "Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination."
    Imai K., Slupphaug G., Lee W.-I., Revy P., Nonoyama S., Catalan N., Yel L., Forveille M., Kavli B., Krokan H.E., Ochs H.D., Fischer A., Durandy A.
    Nat. Immunol. 4:1023-1028(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIGM5 SER-251.
  26. "B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil."
    Kavli B., Andersen S., Otterlei M., Liabakk N.B., Imai K., Fischer A., Durandy A., Krokan H.E., Slupphaug G.
    J. Exp. Med. 201:2011-2021(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT HIGM5 SER-251.

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: April 1, 2015
This is version 172 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

External Data

Dasty 3

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 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.