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Protein

Adenine DNA glycosylase

Gene

Mutyh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities (By similarity).By similarity

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051Proton donor/acceptorBy similarity
Sitei207 – 2071Transition state stabilizerBy similarity
Metal bindingi261 – 2611Iron-sulfur (4Fe-4S)By similarity
Metal bindingi268 – 2681Iron-sulfur (4Fe-4S)By similarity
Metal bindingi271 – 2711Iron-sulfur (4Fe-4S)By similarity
Metal bindingi277 – 2771Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: InterPro
  • response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine DNA glycosylase (EC:3.2.2.-)
Alternative name(s):
MutY homolog
Short name:
rMYH
Gene namesi
Name:Mutyh
Synonyms:Myh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620045. Mutyh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Adenine DNA glycosylasePRO_0000102241Add
BLAST

Proteomic databases

PaxDbiQ8R5G2.
PRIDEiQ8R5G2.

PTM databases

PhosphoSiteiQ8R5G2.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024375.

Structurei

3D structure databases

ProteinModelPortaliQ8R5G2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini335 – 467133Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi376 – 39823Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nth/MutY family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2457. Eukaryota.
COG1194. LUCA.
HOGENOMiHOG000028743.
HOVERGENiHBG052540.
InParanoidiQ8R5G2.
KOiK03575.
PhylomeDBiQ8R5G2.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
PS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R5G2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLRASVRS HKKQPANHKR RGKCALSSSQ AKPSGLDGLA KQKREELLKT
60 70 80 90 100
PVSPYHLFSD IADVTAFRRN LLSWYDQEKR DLPWRKRVKE ETNLDRRAYA
110 120 130 140 150
VWVSEVMLQQ TQVATVIDYY TRWMQKWPTL QDLASASLEE VNQLWSGLGY
160 170 180 190 200
YSRGRRLQEG ARKVVEELGG HVPRTAETLQ QLLPGVGRYT AGAIASIAFD
210 220 230 240 250
QVTGVVDGNV IRVLCRVRAI GADPTSSFVS HHLWDLAQQL VDPARPGDFN
260 270 280 290 300
QAAMELGATV CTPQRPLCNH CPVQSLCRAH QRVGQGRLSA LPGSPDIEEC
310 320 330 340 350
ALNTRQCQLC LPSTNPWDPN MGVVNFPRKA SRRPPREEYS ATCVVEQPGA
360 370 380 390 400
TGGPLILLVQ RPNSGLLAGL WEFPSVTLEP SGQHQHKALL QELQHWSAPL
410 420 430 440 450
PTTPLQHLGE VIHVFSHIKL TYQVYSLALE GQTPASTTLP GARWLTWEEF
460 470 480 490 500
RNAAVSTAMK KVFRVYEEHR RGTCKGSKRP QVCTPSSRKK PSRGQQVLDR
510
FFQRHIPTHK PNSTTQ
Length:516
Mass (Da):57,919
Last modified:June 1, 2002 - v1
Checksum:iE42FD4AC86BE3467
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478683 mRNA. Translation: AAL79551.1.
RefSeqiNP_579850.1. NM_133316.1.
UniGeneiRn.44045.

Genome annotation databases

GeneIDi170841.
KEGGirno:170841.
UCSCiRGD:620045. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478683 mRNA. Translation: AAL79551.1.
RefSeqiNP_579850.1. NM_133316.1.
UniGeneiRn.44045.

3D structure databases

ProteinModelPortaliQ8R5G2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024375.

PTM databases

PhosphoSiteiQ8R5G2.

Proteomic databases

PaxDbiQ8R5G2.
PRIDEiQ8R5G2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170841.
KEGGirno:170841.
UCSCiRGD:620045. rat.

Organism-specific databases

CTDi4595.
RGDi620045. Mutyh.

Phylogenomic databases

eggNOGiKOG2457. Eukaryota.
COG1194. LUCA.
HOGENOMiHOG000028743.
HOVERGENiHBG052540.
InParanoidiQ8R5G2.
KOiK03575.
PhylomeDBiQ8R5G2.

Miscellaneous databases

PROiQ8R5G2.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
PS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Hypoxia induces mitochondrial DNA damage and stimulates expression of a DNA repair enzyme, the Escherichia coli MutY DNA glycosylase homolog (MYH), in vivo, in the rat brain."
    Lee H.-M., Wang C., Hu Z., Greeley G.H. Jr., Makalowski W., Hellmich H.L., Englander E.W.
    J. Neurochem. 80:928-937(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Cerebellum.

Entry informationi

Entry nameiMUTYH_RAT
AccessioniPrimary (citable) accession number: Q8R5G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 94 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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.