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P13051

- UNG_HUMAN

UniProt

P13051 - UNG_HUMAN

Protein

Uracil-DNA glycosylase

Gene

UNG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (10 Oct 2003)
      Previous versions | rss
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    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: ProtInc
    2. DNA repair Source: ProtInc
    3. negative regulation of apoptotic process Source: Ensembl
    4. somatic hypermutation of immunoglobulin genes Source: Ensembl
    5. somatic recombination of immunoglobulin gene segments Source: Ensembl
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair, Host-virus interaction

    Enzyme and pathway databases

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12572. UNG.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency with hyper-IgM 5 (HIGM5) [MIM:608106]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 1 Publication
    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

    ArrayExpressiP13051.
    BgeeiP13051.
    CleanExiHS_UNG.
    GenevestigatoriP13051.

    Organism-specific databases

    HPAiCAB011605.

    Interactioni

    Subunit structurei

    Monomer. Interacts with FAM72A. Interacts with HIV-1 Vpr.2 PublicationsUniRule annotation

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi113220. 16 interactions.
    DIPiDIP-24194N.
    IntActiP13051. 6 interactions.
    MINTiMINT-1507980.
    STRINGi9606.ENSP00000242576.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000229528.
    HOVERGENiHBG000396.
    InParanoidiP13051.
    KOiK03648.
    OMAiIGHNNDE.
    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. Align

    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

    MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK    50
    APAGQEEPGT PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK 100
    HLSGEFGKPY FIKLMGFVAE ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI 150
    LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE NIYKELSTDI EDFVHPGHGD 200
    LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS WLNQNSNGLV 250
    FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL 300
    QKSGKKPIDW KEL 313
    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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9124.1. [P13051-1 ]
    CCDS9125.1. [P13051-2 ]
    PIRi S05964. A60472.
    RefSeqi NP_003353.1. NM_003362.3. [P13051-2 ]
    NP_550433.1. NM_080911.2. [P13051-1 ]
    UniGenei Hs.191334.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AKZ X-ray 1.57 A 94-313 [» ]
    1DPU NMR - B 73-88 [» ]
    1EMH X-ray 1.80 A 94-313 [» ]
    1EMJ X-ray 2.00 A 94-313 [» ]
    1Q3F X-ray 1.90 A 94-313 [» ]
    1SSP X-ray 1.90 E 94-313 [» ]
    1UGH X-ray 1.90 E 94-313 [» ]
    1YUO X-ray 1.95 A 91-313 [» ]
    2HXM X-ray 1.30 A 94-313 [» ]
    2OXM X-ray 2.50 A 94-313 [» ]
    2OYT X-ray 2.00 A 94-313 [» ]
    2SSP X-ray 2.25 E 94-313 [» ]
    3FCF X-ray 1.84 A 94-313 [» ]
    3FCI X-ray 1.27 A 94-313 [» ]
    3FCK X-ray 1.64 B 94-313 [» ]
    3FCL X-ray 1.70 A/B 94-313 [» ]
    3TKB X-ray 1.50 A 94-313 [» ]
    4SKN X-ray 2.90 E 94-313 [» ]
    ProteinModelPortali P13051.
    SMRi P13051. Positions 94-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113220. 16 interactions.
    DIPi DIP-24194N.
    IntActi P13051. 6 interactions.
    MINTi MINT-1507980.
    STRINGi 9606.ENSP00000242576.

    Chemistry

    BindingDBi P13051.
    ChEMBLi CHEMBL3277.

    PTM databases

    PhosphoSitei P13051.

    Polymorphism databases

    DMDMi 37999897.

    Proteomic databases

    MaxQBi P13051.
    PaxDbi P13051.
    PRIDEi P13051.

    Protocols and materials databases

    DNASUi 7374.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242576 ; ENSP00000242576 ; ENSG00000076248 . [P13051-1 ]
    ENST00000336865 ; ENSP00000337398 ; ENSG00000076248 . [P13051-2 ]
    GeneIDi 7374.
    KEGGi hsa:7374.
    UCSCi uc001tnz.2. human. [P13051-1 ]

    Organism-specific databases

    CTDi 7374.
    GeneCardsi GC12P109535.
    HGNCi HGNC:12572. UNG.
    HPAi CAB011605.
    MIMi 191525. gene.
    608106. phenotype.
    neXtProti NX_P13051.
    Orphaneti 101092. Hyper-IgM syndrome type 5.
    PharmGKBi PA364.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0692.
    HOGENOMi HOG000229528.
    HOVERGENi HBG000396.
    InParanoidi P13051.
    KOi K03648.
    OMAi IGHNNDE.
    OrthoDBi EOG786H4X.
    PhylomeDBi P13051.
    TreeFami TF315028.

    Enzyme and pathway databases

    SABIO-RK P13051.

    Miscellaneous databases

    ChiTaRSi UNG. human.
    EvolutionaryTracei P13051.
    GeneWikii Uracil-DNA_glycosylase.
    GenomeRNAii 7374.
    NextBioi 28874.
    PROi P13051.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13051.
    Bgeei P13051.
    CleanExi HS_UNG.
    Genevestigatori P13051.

    Family and domain databases

    Gene3Di 3.40.470.10. 1 hit.
    HAMAPi MF_00148. UDG.
    InterProi IPR018085. Ura-DNA_Glyclase_AS.
    IPR002043. Ura_DNA_glycsylse.
    IPR005122. Uracil-DNA_glycosylase-like.
    [Graphical view ]
    PANTHERi PTHR11264. PTHR11264. 1 hit.
    Pfami PF03167. UDG. 1 hit.
    [Graphical view ]
    SMARTi SM00986. UDG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52141. SSF52141. 1 hit.
    TIGRFAMsi TIGR00628. ung. 1 hit.
    PROSITEi PS00130. U_DNA_GLYCOSYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1989) [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(1994) [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(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    4. NIEHS SNPs program
      Submitted (JUL-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(2004) [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(2004) [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(1993) [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(1996) [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(1996) [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(1998) [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(2006) [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(2008) [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(2008) [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(2009) [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(2009) [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(2009) [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(2010) [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(2011) [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(1995) [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(1995) [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(1996) [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(1998) [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(2003) [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(2005) [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: October 1, 2014
    This is version 166 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