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P13051 (UNG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uracil-DNA glycosylase

Short name=UDG
EC=3.2.2.27
Gene names
Name:UNG
Synonyms:DGU, UNG1, UNG15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03166

Catalytic activity

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP-Rule MF_03166

Subunit structure

Monomer. Interacts with FAM72A. Interacts with HIV-1 Vpr. Ref.10 Ref.13

Subcellular location

Isoform 1: Mitochondrion Ref.8 Ref.11.

Isoform 2: Nucleus Ref.8 Ref.11.

Tissue specificity

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.

Post-translational modification

Isoform 1 is processed by cleavage of a transit peptide. HAMAP-Rule MF_03166

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26

Sequence similarities

Belongs to the uracil-DNA glycosylase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P13051-1)

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.
Isoform 1 (identifier: P13051-2)

Also known as: UNG1;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Uracil-DNA glycosylase HAMAP-Rule MF_03166
PRO_0000176173

Regions

Region1 – 2525FAM72A-binding HAMAP-Rule MF_03166

Sites

Active site1541Proton acceptor By similarity

Amino acid modifications

Modified residue121Phosphoserine Ref.15 Ref.19
Modified residue141Phosphoserine Ref.15 Ref.17 Ref.19
Modified residue231Phosphoserine Ref.15 Ref.17 Ref.19 Ref.20
Modified residue601Phosphothreonine Ref.15 Ref.17 Ref.19 Ref.20
Modified residue641Phosphoserine Ref.15 Ref.17
Modified residue2951N6-acetyllysine Ref.18

Natural variations

Alternative sequence1 – 4444MIGQK…SGDAA → MGVFCLGPWGLGRKLRTPGK GPLQLLSRLCGDHLQ in isoform 1.
VSP_008513
Natural variant41Q → R.
Corresponds to variant rs7488798 [ dbSNP | Ensembl ].
VAR_052697
Natural variant2511F → S in HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus. Ref.25 Ref.26
VAR_017094

Experimental info

Mutagenesis1541D → E or N: Loss of activity.
Mutagenesis1561Y → A, C or S: Thymine-DNA glycosylase activity.
Mutagenesis2131N → D: Cytosine-DNA glycosylase activity.

Secondary structure

............................................... 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (UNG2) [UniParc].

Last modified October 10, 2003. Version 2.
Checksum: A4B27E6198AFE9C0

FASTA31334,645
        10         20         30         40         50         60 
MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK APAGQEEPGT 

        70         80         90        100        110        120 
PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK HLSGEFGKPY FIKLMGFVAE 

       130        140        150        160        170        180 
ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE 

       190        200        210        220        230        240 
NIYKELSTDI EDFVHPGHGD LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS 

       250        260        270        280        290        300 
WLNQNSNGLV FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL 

       310 
QKSGKKPIDW KEL 

« Hide

Isoform 1 (UNG1) [UniParc].

Checksum: 32998C244E47B215
Show »

FASTA30433,924

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
UNGbase

UNG mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9124.1. [P13051-1]
CCDS9125.1. [P13051-2]
PIRA60472. S05964.
RefSeqNP_003353.1. NM_003362.3. [P13051-2]
NP_550433.1. NM_080911.2. [P13051-1]
UniGeneHs.191334.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP13051.
SMRP13051. Positions 94-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113220. 16 interactions.
DIPDIP-24194N.
IntActP13051. 6 interactions.
MINTMINT-1507980.
STRING9606.ENSP00000242576.

Chemistry

BindingDBP13051.
ChEMBLCHEMBL3277.

PTM databases

PhosphoSiteP13051.

Polymorphism databases

DMDM37999897.

Proteomic databases

MaxQBP13051.
PaxDbP13051.
PRIDEP13051.

Protocols and materials databases

DNASU7374.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242576; ENSP00000242576; ENSG00000076248. [P13051-1]
ENST00000336865; ENSP00000337398; ENSG00000076248. [P13051-2]
GeneID7374.
KEGGhsa:7374.
UCSCuc001tnz.2. human. [P13051-1]

Organism-specific databases

CTD7374.
GeneCardsGC12P109535.
HGNCHGNC:12572. UNG.
HPACAB011605.
MIM191525. gene.
608106. phenotype.
neXtProtNX_P13051.
Orphanet101092. Hyper-IgM syndrome type 5.
PharmGKBPA364.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0692.
HOGENOMHOG000229528.
HOVERGENHBG000396.
InParanoidP13051.
KOK03648.
OMAIGHNNDE.
OrthoDBEOG786H4X.
PhylomeDBP13051.
TreeFamTF315028.

Enzyme and pathway databases

SABIO-RKP13051.

Gene expression databases

ArrayExpressP13051.
BgeeP13051.
CleanExHS_UNG.
GenevestigatorP13051.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_00148. UDG.
InterProIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR11264. PTHR11264. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. SSF52141. 1 hit.
TIGRFAMsTIGR00628. ung. 1 hit.
PROSITEPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUNG. human.
EvolutionaryTraceP13051.
GeneWikiUracil-DNA_glycosylase.
GenomeRNAi7374.
NextBio28874.
PROP13051.
SOURCESearch...

Entry information

Entry nameUNG_HUMAN
AccessionPrimary (citable) accession number: P13051
Secondary accession number(s): A8K5M6 expand/collapse secondary AC list , B2R8Y1, O00637, O00719, Q93028
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 10, 2003
Last modified: July 9, 2014
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM