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Protein

Single-strand selective monofunctional uracil DNA glycosylase

Gene

SMUG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate; via amide nitrogenBy similarity
Binding sitei98 – 981Substrate; via amide nitrogen
Binding sitei163 – 1631Substrate
Binding sitei239 – 2391Substrate

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA N-glycosylase activity Source: HGNC
  • oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Source: GO_Central
  • single-strand selective uracil DNA N-glycosylase activity Source: HGNC
  • uracil DNA N-glycosylase activity Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BRENDAi3.2.2.27. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Single-strand selective monofunctional uracil DNA glycosylase (EC:3.2.2.-)
Gene namesi
Name:SMUG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17148. SMUG1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: HGNC
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851N → A: Markedly impaired damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C. 1 Publication
Mutagenesisi87 – 871G → A or S: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. 1 Publication
Mutagenesisi87 – 871G → F: Loss of damage-excising activity. 1 Publication
Mutagenesisi89 – 891F → A, G or S: No effect on damage-excising activity for U/G, hoU/G, hmU/A and fU/A. 1 Publication
Mutagenesisi90 – 901G → A: Loss of damage-excising activity for U/G. Weak, but significant activity toward hoU/G, hmU/A and fU/A. 1 Publication
Mutagenesisi91 – 911M → A: No effect on damage-excising activity for U/G, hoU/G, hmU/A and fU/A. 1 Publication
Mutagenesisi98 – 981F → L: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. 1 Publication
Mutagenesisi163 – 1631N → D: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C. hoC-excising activity for hoC/A, hoC/T and hoC/C. 1 Publication
Mutagenesisi239 – 2391H → L or N: Markedly impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. 1 Publication

Organism-specific databases

PharmGKBiPA142670895.

Polymorphism and mutation databases

BioMutaiSMUG1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Single-strand selective monofunctional uracil DNA glycosylasePRO_0000071992Add
BLAST

Proteomic databases

EPDiQ53HV7.
MaxQBiQ53HV7.
PaxDbiQ53HV7.
PRIDEiQ53HV7.
TopDownProteomicsiQ53HV7-2. [Q53HV7-2]

PTM databases

PhosphoSiteiQ53HV7.

Expressioni

Gene expression databases

BgeeiQ53HV7.
CleanExiHS_SMUG1.
ExpressionAtlasiQ53HV7. baseline and differential.
GenevisibleiQ53HV7. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RBPMSQ930622EBI-749970,EBI-740322
VAC14Q08AM63EBI-749970,EBI-2107455

Protein-protein interaction databases

BioGridi117118. 5 interactions.
IntActiQ53HV7. 4 interactions.
MINTiMINT-6631537.
STRINGi9606.ENSP00000338606.

Structurei

3D structure databases

ProteinModelPortaliQ53HV7.
SMRiQ53HV7. Positions 26-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 18715DNA bindingBy similarityAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IFBA. Eukaryota.
ENOG410XQUR. LUCA.
GeneTreeiENSGT00390000004897.
HOGENOMiHOG000220288.
HOVERGENiHBG084399.
InParanoidiQ53HV7.
KOiK10800.
OMAiIMHPSPR.
PhylomeDBiQ53HV7.
TreeFamiTF324356.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q53HV7-1) [UniParc]FASTAAdd to basket

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
MPQAFLLGSI HEPAGALMEP QPCPGSLAES FLEEELRLNA ELSQLQFSEP
60 70 80 90 100
VGIIYNPVEY AWEPHRNYVT RYCQGPKEVL FLGMNPGPFG MAQTGVPFGE
110 120 130 140 150
VSMVRDWLGI VGPVLTPPQE HPKRPVLGLE CPQSEVSGAR FWGFFRNLCG
160 170 180 190 200
QPEVFFHHCF VHNLCPLLFL APSGRNLTPA ELPAKQREQL LGICDAALCR
210 220 230 240 250
QVQLLGVRLV VGVGRLAEQR ARRALAGLMP EVQVEGLLHP SPRNPQANKG
260 270
WEAVAKERLN ELGLLPLLLK
Length:270
Mass (Da):29,862
Last modified:October 17, 2006 - v2
Checksum:i2AB18F6F757F6DD7
GO
Isoform 2 (identifier: Q53HV7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-177: VSGARFWGFF...LFLAPSGRNL → GPRQSMGHEI...VRRPGFSSQL
     178-270: Missing.

Note: No experimental confirmation available.
Show »
Length:177
Mass (Da):19,627
Checksum:i9525274EE6797F61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301S → G AA sequence (PubMed:11526119).Curated
Sequence conflicti48 – 481S → L in BAC03670 (PubMed:14702039).Curated
Sequence conflicti50 – 501P → I AA sequence (PubMed:11526119).Curated
Sequence conflicti54 – 541I → V AA sequence (PubMed:11526119).Curated
Sequence conflicti66 – 174109Missing in BAC03670 (PubMed:14702039).CuratedAdd
BLAST
Sequence conflicti70 – 701T → I in BAD96193 (Ref. 4) Curated
Sequence conflicti103 – 1031M → V AA sequence (PubMed:11526119).Curated
Sequence conflicti157 – 1571H → R AA sequence (PubMed:11526119).Curated
Sequence conflicti193 – 1931I → V AA sequence (PubMed:11526119).Curated
Sequence conflicti227 – 2271G → S AA sequence (PubMed:11526119).Curated
Sequence conflicti259 – 2602LN → NL AA sequence (PubMed:11526119).Curated
Sequence conflicti269 – 2702LK → TS AA sequence (PubMed:11526119).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151G → V.1 Publication
Corresponds to variant rs2233920 [ dbSNP | Ensembl ].
VAR_023243
Natural varianti105 – 1051R → W.1 Publication
Corresponds to variant rs3136389 [ dbSNP | Ensembl ].
VAR_023244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei136 – 17742VSGAR…SGRNL → GPRQSMGHEIKSELLMGGCS WIRGKIQCDRVQVRRPGFSS QL in isoform 2. 1 PublicationVSP_015150Add
BLAST
Alternative sequencei178 – 27093Missing in isoform 2. 1 PublicationVSP_015151Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125182 mRNA. Translation: AAD17301.1.
AK001235 mRNA. Translation: BAA91571.1.
AK091468 mRNA. Translation: BAC03670.1.
AK222473 mRNA. Translation: BAD96193.1.
AK290274 mRNA. Translation: BAF82963.1.
AF489699 Genomic DNA. Translation: AAL86910.1.
CH471054 Genomic DNA. Translation: EAW96752.1.
CH471054 Genomic DNA. Translation: EAW96756.1.
BC000417 mRNA. Translation: AAH00417.1.
BC088352 mRNA. Translation: AAH88352.1.
BC105607 mRNA. Translation: AAI05608.1.
CCDSiCCDS58239.1. [Q53HV7-2]
CCDS8874.1. [Q53HV7-1]
RefSeqiNP_001230716.1. NM_001243787.1. [Q53HV7-1]
NP_001230717.1. NM_001243788.1. [Q53HV7-1]
NP_001230718.1. NM_001243789.1. [Q53HV7-2]
NP_001230719.1. NM_001243790.1. [Q53HV7-2]
NP_001230720.1. NM_001243791.1. [Q53HV7-2]
NP_055126.1. NM_014311.2. [Q53HV7-1]
XP_006719382.1. XM_006719319.2. [Q53HV7-1]
XP_006719383.1. XM_006719320.2. [Q53HV7-1]
XP_006719384.1. XM_006719321.2. [Q53HV7-1]
XP_006719385.1. XM_006719322.2. [Q53HV7-2]
XP_011536411.1. XM_011538109.1. [Q53HV7-1]
XP_011536412.1. XM_011538110.1. [Q53HV7-1]
XP_011536413.1. XM_011538111.1. [Q53HV7-1]
XP_011536414.1. XM_011538112.1. [Q53HV7-1]
XP_011536415.1. XM_011538113.1. [Q53HV7-1]
XP_011536416.1. XM_011538114.1. [Q53HV7-1]
XP_011536417.1. XM_011538115.1. [Q53HV7-1]
XP_011536418.1. XM_011538116.1. [Q53HV7-1]
XP_011536419.1. XM_011538117.1. [Q53HV7-1]
XP_011536420.1. XM_011538118.1. [Q53HV7-1]
XP_011536421.1. XM_011538119.1. [Q53HV7-1]
XP_011536422.1. XM_011538120.1. [Q53HV7-1]
XP_011536423.1. XM_011538121.1. [Q53HV7-1]
XP_011536424.1. XM_011538122.1. [Q53HV7-2]
UniGeneiHs.632721.
Hs.731659.

Genome annotation databases

EnsembliENST00000243112; ENSP00000243112; ENSG00000123415. [Q53HV7-2]
ENST00000337581; ENSP00000338606; ENSG00000123415. [Q53HV7-1]
ENST00000401977; ENSP00000384828; ENSG00000123415. [Q53HV7-1]
ENST00000506595; ENSP00000421206; ENSG00000123415. [Q53HV7-2]
ENST00000508394; ENSP00000424191; ENSG00000123415. [Q53HV7-1]
ENST00000513838; ENSP00000423629; ENSG00000123415. [Q53HV7-2]
ENST00000514685; ENSP00000421139; ENSG00000123415. [Q53HV7-2]
GeneIDi23583.
KEGGihsa:23583.
UCSCiuc001sfb.5. human. [Q53HV7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125182 mRNA. Translation: AAD17301.1.
AK001235 mRNA. Translation: BAA91571.1.
AK091468 mRNA. Translation: BAC03670.1.
AK222473 mRNA. Translation: BAD96193.1.
AK290274 mRNA. Translation: BAF82963.1.
AF489699 Genomic DNA. Translation: AAL86910.1.
CH471054 Genomic DNA. Translation: EAW96752.1.
CH471054 Genomic DNA. Translation: EAW96756.1.
BC000417 mRNA. Translation: AAH00417.1.
BC088352 mRNA. Translation: AAH88352.1.
BC105607 mRNA. Translation: AAI05608.1.
CCDSiCCDS58239.1. [Q53HV7-2]
CCDS8874.1. [Q53HV7-1]
RefSeqiNP_001230716.1. NM_001243787.1. [Q53HV7-1]
NP_001230717.1. NM_001243788.1. [Q53HV7-1]
NP_001230718.1. NM_001243789.1. [Q53HV7-2]
NP_001230719.1. NM_001243790.1. [Q53HV7-2]
NP_001230720.1. NM_001243791.1. [Q53HV7-2]
NP_055126.1. NM_014311.2. [Q53HV7-1]
XP_006719382.1. XM_006719319.2. [Q53HV7-1]
XP_006719383.1. XM_006719320.2. [Q53HV7-1]
XP_006719384.1. XM_006719321.2. [Q53HV7-1]
XP_006719385.1. XM_006719322.2. [Q53HV7-2]
XP_011536411.1. XM_011538109.1. [Q53HV7-1]
XP_011536412.1. XM_011538110.1. [Q53HV7-1]
XP_011536413.1. XM_011538111.1. [Q53HV7-1]
XP_011536414.1. XM_011538112.1. [Q53HV7-1]
XP_011536415.1. XM_011538113.1. [Q53HV7-1]
XP_011536416.1. XM_011538114.1. [Q53HV7-1]
XP_011536417.1. XM_011538115.1. [Q53HV7-1]
XP_011536418.1. XM_011538116.1. [Q53HV7-1]
XP_011536419.1. XM_011538117.1. [Q53HV7-1]
XP_011536420.1. XM_011538118.1. [Q53HV7-1]
XP_011536421.1. XM_011538119.1. [Q53HV7-1]
XP_011536422.1. XM_011538120.1. [Q53HV7-1]
XP_011536423.1. XM_011538121.1. [Q53HV7-1]
XP_011536424.1. XM_011538122.1. [Q53HV7-2]
UniGeneiHs.632721.
Hs.731659.

3D structure databases

ProteinModelPortaliQ53HV7.
SMRiQ53HV7. Positions 26-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117118. 5 interactions.
IntActiQ53HV7. 4 interactions.
MINTiMINT-6631537.
STRINGi9606.ENSP00000338606.

PTM databases

PhosphoSiteiQ53HV7.

Polymorphism and mutation databases

BioMutaiSMUG1.

Proteomic databases

EPDiQ53HV7.
MaxQBiQ53HV7.
PaxDbiQ53HV7.
PRIDEiQ53HV7.
TopDownProteomicsiQ53HV7-2. [Q53HV7-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243112; ENSP00000243112; ENSG00000123415. [Q53HV7-2]
ENST00000337581; ENSP00000338606; ENSG00000123415. [Q53HV7-1]
ENST00000401977; ENSP00000384828; ENSG00000123415. [Q53HV7-1]
ENST00000506595; ENSP00000421206; ENSG00000123415. [Q53HV7-2]
ENST00000508394; ENSP00000424191; ENSG00000123415. [Q53HV7-1]
ENST00000513838; ENSP00000423629; ENSG00000123415. [Q53HV7-2]
ENST00000514685; ENSP00000421139; ENSG00000123415. [Q53HV7-2]
GeneIDi23583.
KEGGihsa:23583.
UCSCiuc001sfb.5. human. [Q53HV7-1]

Organism-specific databases

CTDi23583.
GeneCardsiSMUG1.
H-InvDBHIX0010683.
HGNCiHGNC:17148. SMUG1.
MIMi607753. gene.
neXtProtiNX_Q53HV7.
PharmGKBiPA142670895.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFBA. Eukaryota.
ENOG410XQUR. LUCA.
GeneTreeiENSGT00390000004897.
HOGENOMiHOG000220288.
HOVERGENiHBG084399.
InParanoidiQ53HV7.
KOiK10800.
OMAiIMHPSPR.
PhylomeDBiQ53HV7.
TreeFamiTF324356.

Enzyme and pathway databases

BRENDAi3.2.2.27. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.

Miscellaneous databases

GeneWikiiSMUG1.
GenomeRNAii23583.
NextBioi46196.
PROiQ53HV7.
SOURCEiSearch...

Gene expression databases

BgeeiQ53HV7.
CleanExiHS_SMUG1.
ExpressionAtlasiQ53HV7. baseline and differential.
GenevisibleiQ53HV7. HS.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors."
    Haushalter K.A., Stukenberg P.T., Kirschner M.W., Verdine G.L.
    Curr. Biol. 9:174-185(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Ovary.
  2. "Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions."
    Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H., Ohyama Y., Karino N., Matsuda A., Ide H.
    Biochemistry 42:5003-5012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Liver.
  3. "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] (ISOFORM 1).
    Tissue: Brain and Colon.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adipose tissue.
  5. NIEHS SNPs program
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-15 AND TRP-105.
  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 2).
    Tissue: Muscle and Uterus.
  8. "Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1."
    Boorstein R.J., Cummings A. Jr., Marenstein D.R., Chan M.K., Ma Y., Neubert T.A., Brown S.M., Teebor G.W.
    J. Biol. Chem. 276:41991-41997(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 13-21; 26-37; 46-66; 79-105; 124-140; 141-146; 147-157; 188-200; 201-208; 224-243 AND 259-270, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup."
    Kavli B., Sundheim O., Akbari M., Otterlei M., Nilsen H., Skorpen F., Aas P.A., Hagen L., Krokan H.E., Slupphaug G.
    J. Biol. Chem. 277:39926-39936(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase."
    Matsubara M., Tanaka T., Terato H., Ohmae E., Izumi S., Katayanagi K., Ide H.
    Nucleic Acids Res. 32:5291-5302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-85; GLY-87; PHE-89; GLY-90; MET-91; PHE-98; ASN-163 AND HIS-239.

Entry informationi

Entry nameiSMUG1_HUMAN
AccessioniPrimary (citable) accession number: Q53HV7
Secondary accession number(s): A8K2K9
, O95862, Q0D2M0, Q8NB71, Q9BWC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 17, 2006
Last modified: March 16, 2016
This is version 100 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

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

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 one 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.