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P97931

- UNG_MOUSE

UniProt

P97931 - UNG_MOUSE

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Protein

Uracil-DNA glycosylase

Gene

Ung

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 sitei147 – 1471Proton acceptorUniRule annotation

GO - Molecular functioni

  1. uracil DNA N-glycosylase activity Source: MGI

GO - Biological processi

  1. base-excision repair Source: UniProtKB-HAMAP
  2. DNA repair Source: MGI
  3. negative regulation of apoptotic process Source: Ensembl
  4. somatic hypermutation of immunoglobulin genes Source: MGI
  5. somatic recombination of immunoglobulin gene segments Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Uracil-DNA glycosylaseUniRule annotation (EC:3.2.2.27UniRule annotation)
Short name:
UDGUniRule annotation
Gene namesi
Name:Ung
Synonyms:Ung1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:109352. Ung.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Uracil-DNA glycosylasePRO_0000176174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei288 – 2881N6-acetyllysineBy similarity

Post-translational modificationi

Isoform 1 is processed by cleavage of a transit peptide.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP97931.

PTM databases

PhosphoSiteiP97931.

Expressioni

Gene expression databases

BgeeiP97931.
CleanExiMM_UNG.
ExpressionAtlasiP97931. baseline and differential.
GenevestigatoriP97931.

Interactioni

Subunit structurei

Monomer. Interacts with FAM72A.UniRule annotation

Protein-protein interaction databases

IntActiP97931. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP97931.
SMRiP97931. Positions 87-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the uracil-DNA glycosylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0692.
GeneTreeiENSGT00390000003405.
HOGENOMiHOG000229528.
HOVERGENiHBG000396.
InParanoidiP97931.
KOiK03648.
OMAiMNQITTH.
OrthoDBiEOG786H4X.
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: P97931-1) [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 FSPTPTGKRT TRSPEPVPGS GVAAEIGGDA VASPAKKARV
60 70 80 90 100
EQNEQGSPLS AEQLVRIQRN KAAALLRLAA RNVPAGFGES WKQQLCGEFG
110 120 130 140 150
KPYFVKLMGF VAEERNHHKV YPPPEQVFTW TQMCDIRDVK VVILGQDPYH
160 170 180 190 200
GPNQAHGLCF SVQRPVPPPP SLENIFKELS TDIDGFVHPG HGDLSGWARQ
210 220 230 240 250
GVLLLNAVLT VRAHQANSHK ERGWEQFTDA VVSWLNQNLS GLVFLLWGSY
260 270 280 290 300
AQKKGSVIDR KRHHVLQTAH PSPLSVHRGF LGCRHFSKAN ELLQKSGKKP

INWKEL
Length:306
Mass (Da):33,926
Last modified:July 27, 2011 - v3
Checksum:iCE2D5192936CE6EA
GO
Isoform 1 (identifier: P97931-2) [UniParc]FASTAAdd to Basket

Also known as: UNG1

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MIGQKTLYSFFSPTPTGKRTTRSPEPVPGSGVAAEIGGDAV → MGVLGRRSLRLARRAGLRSLTPNPDSDSRQ

Show »
Length:295
Mass (Da):33,054
Checksum:i7E66E56DEC55B851
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771H → Y in CAA67489. (PubMed:9016624)Curated
Sequence conflicti277 – 2771H → Y in CAA70168. (PubMed:9016624)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141MIGQK…GGDAV → MGVLGRRSLRLARRAGLRSL TPNPDSDSRQ in isoform 1. 5 PublicationsVSP_008514Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55040 Genomic DNA. Translation: AAB39511.1.
U55041 mRNA. Translation: AAC53197.1.
X99018 mRNA. Translation: CAA67489.1.
Y08975 mRNA. Translation: CAA70168.1.
AF174485 Genomic DNA. Translation: AAF76936.1.
AK146178 mRNA. Translation: BAE26956.1.
CH466529 Genomic DNA. Translation: EDL19920.1.
BC011039 mRNA. Translation: AAH11039.1.
BC052853 mRNA. Translation: AAH52853.1.
CCDSiCCDS19560.1. [P97931-2]
CCDS39221.1. [P97931-1]
RefSeqiNP_001035781.1. NM_001040691.1. [P97931-1]
NP_035807.2. NM_011677.2. [P97931-2]
UniGeneiMm.1393.

Genome annotation databases

EnsembliENSMUST00000031587; ENSMUSP00000031587; ENSMUSG00000029591. [P97931-1]
ENSMUST00000102584; ENSMUSP00000099644; ENSMUSG00000029591. [P97931-2]
GeneIDi22256.
KEGGimmu:22256.
UCSCiuc008yzf.1. mouse. [P97931-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55040 Genomic DNA. Translation: AAB39511.1 .
U55041 mRNA. Translation: AAC53197.1 .
X99018 mRNA. Translation: CAA67489.1 .
Y08975 mRNA. Translation: CAA70168.1 .
AF174485 Genomic DNA. Translation: AAF76936.1 .
AK146178 mRNA. Translation: BAE26956.1 .
CH466529 Genomic DNA. Translation: EDL19920.1 .
BC011039 mRNA. Translation: AAH11039.1 .
BC052853 mRNA. Translation: AAH52853.1 .
CCDSi CCDS19560.1. [P97931-2 ]
CCDS39221.1. [P97931-1 ]
RefSeqi NP_001035781.1. NM_001040691.1. [P97931-1 ]
NP_035807.2. NM_011677.2. [P97931-2 ]
UniGenei Mm.1393.

3D structure databases

ProteinModelPortali P97931.
SMRi P97931. Positions 87-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97931. 1 interaction.

PTM databases

PhosphoSitei P97931.

Proteomic databases

PRIDEi P97931.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031587 ; ENSMUSP00000031587 ; ENSMUSG00000029591 . [P97931-1 ]
ENSMUST00000102584 ; ENSMUSP00000099644 ; ENSMUSG00000029591 . [P97931-2 ]
GeneIDi 22256.
KEGGi mmu:22256.
UCSCi uc008yzf.1. mouse. [P97931-1 ]

Organism-specific databases

CTDi 7374.
MGIi MGI:109352. Ung.

Phylogenomic databases

eggNOGi COG0692.
GeneTreei ENSGT00390000003405.
HOGENOMi HOG000229528.
HOVERGENi HBG000396.
InParanoidi P97931.
KOi K03648.
OMAi MNQITTH.
OrthoDBi EOG786H4X.
TreeFami TF315028.

Miscellaneous databases

NextBioi 302339.
PROi P97931.
SOURCEi Search...

Gene expression databases

Bgeei P97931.
CleanExi MM_UNG.
ExpressionAtlasi P97931. baseline and differential.
Genevestigatori P97931.

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

« Hide 'large scale' publications
  1. "The mouse uracil-DNA glycosylase gene: isolation of cDNA and genomic clones and mapping ung to mouse chromosome 5."
    Svendsen P.C., Yee H.A., Winkfein R.J., van de Sande J.H.
    Gene 189:175-181(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. "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 [MRNA] (ISOFORMS 1 AND 2).
  3. "Analysis of uracil-DNA glycosylases from the murine Ung gene reveals differential expression in tissues and in embryonic development and a subcellular sorting pattern that differs from the human homologues."
    Nilsen H., Steinsbekk K.S., Otterlei M., Slupphaug G., Aas P.A., Krokan H.E.
    Nucleic Acids Res. 28:2277-2285(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: 129/Sv.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: DBA/2.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Strain: C3H/He and Czech II.
    Tissue: Mammary tumor and Osteoblast.

Entry informationi

Entry nameiUNG_MOUSE
AccessioniPrimary (citable) accession number: P97931
Secondary accession number(s): P97285
, P97509, Q7TPW8, Q9JIW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

External Data

Dasty 3