P13051 (UNG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uracil-DNA glycosylase
Short name=UDG
EC=3.2.2.27

Gene names

Name:	UNG
Synonyms:	DGU, UNG1, UNG15

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Subunit structure	Monomer. Interacts with HIV-1 Vpr. Ref.10
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.
Involvement in disease	Defects in UNG are a cause of immunodeficiency with hyper-IgM type 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. Ref.24 Ref.25
Sequence similarities	Belongs to the uracil-DNA glycosylase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Host-virus interaction
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Molecular function	Glycosidase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	base-excision repair Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Non-traceable author statement Ref.3. Source: UniProtKB
Molecular function	uracil DNA N-glycosylase activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Uracil-DNA glycosylase

PRO_0000176173

Sites

Active site

154

1

Proton acceptor By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.19

Modified residue

5

1

N6-acetyllysine Ref.19

Modified residue

12

1

Phosphoserine Ref.15 Ref.16

Modified residue

14

1

Phosphoserine Ref.15 Ref.16 Ref.18

Modified residue

23

1

Phosphoserine Ref.13 Ref.16 Ref.17 Ref.18

Modified residue

60

1

Phosphothreonine Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18

Modified residue

63

1

Phosphoserine Ref.14 Ref.16 Ref.17

Modified residue

64

1

Phosphoserine Ref.16 Ref.17 Ref.18

Modified residue

67

1

Phosphoserine Ref.17

Modified residue

295

1

N6-acetyllysine Ref.19

Natural variations

Alternative sequence

1 – 44

44

MIGQK…SGDAA → MGVFCLGPWGLGRKLRTPGK GPLQLLSRLCGDHLQ in isoform 1.

VSP_008513

Natural variant

4

1

Q → R.
Corresponds to variant rs7488798 [ dbSNP | Ensembl ].

VAR_052697

Natural variant

251

1

F → S in HIGM5; fully active and stable when expressed in E. coli; mistargeted to mitochondria rather than the nucleus. Ref.24 Ref.25

VAR_017094

Experimental info

Mutagenesis

154

1

D → E or N: Loss of activity.

Mutagenesis

156

1

Y → A, C or S: Thymine-DNA glycosylase activity.

Mutagenesis

213

1

N → D: Cytosine-DNA glycosylase activity.

Secondary structure

1

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313

Helix Strand Turn

Details...

Helix

77 – 86

10

Helix

96 – 102

7

Helix

103 – 105

3

Helix

109 – 124

16

Beta strand

127 – 129

3

Helix

131 – 133

3

Helix

136 – 138

3

Helix

143 – 145

3

Beta strand

148 – 152

5

Turn

159 – 161

3

Helix

177 – 189

13

Helix

202 – 206

5

Beta strand

209 – 215

7

Turn

223 – 228

6

Helix

231 – 245

15

Beta strand

250 – 255

6

Helix

256 – 261

6

Turn

262 – 264

3

Turn

267 – 269

3

Beta strand

270 – 275

6

Turn

280 – 282

3

Helix

283 – 285

3

Turn

286 – 289

4

Helix

292 – 302

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (UNG2) [UniParc]. Last modified October 10, 2003. Version 2. Checksum: A4B27E6198AFE9C0	FASTA	313	34,645
	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
	Isoform 1 (UNG1) [UniParc]. Checksum: 32998C244E47B215	FASTA	304	33,924
	10 20 30 40 50 60 MGVFCLGPWG LGRKLRTPGK GPLQLLSRLC GDHLQAIPAK KAPAGQEEPG TPPSSPLSAE 70 80 90 100 110 120 QLDRIQRNKA AALLRLAARN VPVGFGESWK KHLSGEFGKP YFIKLMGFVA EERKHYTVYP 130 140 150 160 170 180 PPHQVFTWTQ MCDIKDVKVV ILGQDPYHGP NQAHGLCFSV QRPVPPPPSL ENIYKELSTD 190 200 210 220 230 240 IEDFVHPGHG DLSGWAKQGV LLLNAVLTVR AHQANSHKER GWEQFTDAVV SWLNQNSNGL 250 260 270 280 290 300 VFLLWGSYAQ KKGSAIDRKR HHVLQTAHPS PLSVYRGFFG CRHFSKTNEL LQKSGKKPID WKEL

References

	« Hide 'large scale' referencesShow '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: 2555154] [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: 7926048] [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: 9016624] [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: 14702039] [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. , 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: 15489334] [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: 8332455] [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: 8670846] [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: 8551605] [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: 9753728] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-60, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60 AND SER-63, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23; THR-60; SER-63 AND SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; THR-60; SER-63; SER-64 AND SER-67, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; THR-60 AND SER-64, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5 AND LYS-295, MASS SPECTROMETRY.
[20]	"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: 7697717] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[21]	"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: 7671300] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[22]	"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: 8900285] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[23]	"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: 9724657] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-313.
[24]	"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: 12958596] [Abstract] Cited for: VARIANT HIGM5 SER-251.
[25]	"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: 15967827] [Abstract] Cited for: CHARACTERIZATION OF VARIANT HIGM5 SER-251.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00006516.
IPI00011069.

PIR

A60472. S05964.

RefSeq

NP_003353.1. NM_003362.3.
NP_550433.1. NM_080911.2.

UniGene

Hs.191334.

3D structure databases

PDBe
RCSB PDB
PDBj

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	94-304	[»]
1SSP	X-ray	1.90	E	94-313	[»]
1UGH	X-ray	1.90	E	94-313	[»]
1YUO	X-ray	1.95	A	94-313	[»]
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	[»]

ProteinModelPortal

P13051.

SMR

P13051. Positions 94-313.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24194N.

IntAct

P13051. 3 interactions.

STRING

P13051.

PTM databases

PhosphoSite

P13051.

Polymorphism databases

DMDM

37999897.

Proteomic databases

PRIDE

P13051.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000242576; ENSP00000242576; ENSG00000076248.

GeneID

7374.

KEGG

hsa:7374.

UCSC

uc001tnz.1. human.
uc001toa.1. human.

Organism-specific databases

CTD

7374.

GeneCards

GC12P109535.

H-InvDB

HIX0010973.

HGNC

HGNC:12572. UNG.

HPA

CAB011605.

MIM

191525. gene.
608106. phenotype.

neXtProt

NX_P13051.

Orphanet

101092. Hyper-IgM syndrome type 5.

PharmGKB

PA364.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08710.

GeneTree

ENSGT00390000003405.

HOGENOM

HBG605450.

HOVERGEN

HBG000396.

InParanoid

P13051.

OMA

MLWGNYA.

OrthoDB

EOG4STS54.

PhylomeDB

P13051.

Gene expression databases

ArrayExpress

P13051.

Bgee

P13051.

CleanEx

HS_UNG.

Genevestigator

P13051.

GermOnline

ENSG00000076248. Homo sapiens.

Family and domain databases

InterPro

IPR002043. UDNA_glycsylse.
IPR018085. Ura-DNA_Glyclase_AS.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]

Gene3D

G3DSA:3.40.470.10. Uracil-DNA_glycosylase-like. 1 hit.

KO

K03648.

PANTHER

PTHR11264. UDNA_glycsylse. 1 hit.

Pfam

PF03167. UDG. 1 hit.
[Graphical view]

SMART

SM00986. UDG. 1 hit.
[Graphical view]

SUPFAM

SSF52141. UDNA_glycsylseSF. 1 hit.

TIGRFAMs

TIGR00628. Ung. 1 hit.

PROSITE

PS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

28874.

SOURCE

Search...

Entry information

Entry name

UNG_HUMAN

Accession

Primary (citable) accession number: P13051
Secondary accession number(s): A8K5M6 , B2R8Y1, O00637, O00719, Q93028

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 10, 2003
Last modified:	January 25, 2012
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.