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Q9UIF7

- MUTYH_HUMAN

UniProt

Q9UIF7 - MUTYH_HUMAN

Protein

A/G-specific adenine DNA glycosylase

Gene

MUTYH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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.1 Publication

    Cofactori

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi287 – 2871Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi294 – 2941Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi297 – 2971Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi303 – 3031Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. MutSalpha complex binding Source: HGNC
    5. protein binding Source: HGNC

    GO - Biological processi

    1. base-excision repair Source: Reactome
    2. base-excision repair, AP site formation Source: Reactome
    3. depurination Source: Reactome
    4. DNA repair Source: Reactome
    5. mismatch repair Source: ProtInc

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
    REACT_1729. Cleavage of the damaged purine.
    REACT_2176. Recognition and association of DNA glycosylase with site containing an affected purine.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A/G-specific adenine DNA glycosylase (EC:3.2.2.-)
    Alternative name(s):
    MutY homolog
    Short name:
    hMYH
    Gene namesi
    Name:MUTYH
    Synonyms:MYH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7527. MUTYH.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Familial adenomatous polyposis 2 (FAP2) [MIM:608456]: A condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251Y → H in FAP2. 1 Publication
    VAR_026045
    Natural varianti128 – 1281W → R in FAP2. 1 Publication
    VAR_026046
    Natural varianti148 – 1481G → IW in FAP2; dysfunctional in base excision repair assay.
    VAR_064938
    Natural varianti176 – 1761Y → C in FAP2; dysfunctional in base excision repair assay. 4 Publications
    Corresponds to variant rs34612342 [ dbSNP | Ensembl ].
    VAR_018873
    Natural varianti179 – 1791R → C in FAP2. 1 Publication
    VAR_064939
    Natural varianti179 – 1791R → H in FAP2. 1 Publication
    VAR_026047
    Natural varianti182 – 1821R → W in FAP2; dysfunctional in base excision repair assay. 2 Publications
    VAR_064940
    Natural varianti238 – 2381R → W in FAP2. 1 Publication
    Corresponds to variant rs34126013 [ dbSNP | Ensembl ].
    VAR_026048
    Natural varianti393 – 3931G → D in FAP2; shows a glycosylase activity very similar to the wild-type protein. 4 Publications
    Corresponds to variant rs36053993 [ dbSNP | Ensembl ].
    VAR_018875
    Natural varianti477 – 4771Missing in FAP2; dysfunctional in base excision repair assay.
    VAR_064941
    Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations contribute to the development of a sub-set of sporadic gastric cancers in carriers of Helicobacter pylori (PubMed:15273732).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti402 – 4021P → S in GASC; sporadic. 1 Publication
    VAR_026049
    Natural varianti411 – 4111Q → R in GASC; sporadic. 1 Publication
    VAR_026050

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi608456. phenotype.
    613659. phenotype.
    Orphaneti26106. Familial gastric cancer.
    247798. MUTYH-related attenuated familial adenomatous polyposis.
    PharmGKBiPA31328.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546A/G-specific adenine DNA glycosylasePRO_0000102239Add
    BLAST

    Proteomic databases

    MaxQBiQ9UIF7.
    PaxDbiQ9UIF7.
    PRIDEiQ9UIF7.

    PTM databases

    PhosphoSiteiQ9UIF7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UIF7.
    BgeeiQ9UIF7.
    CleanExiHS_MUTYH.
    GenevestigatoriQ9UIF7.

    Organism-specific databases

    HPAiHPA008732.

    Interactioni

    Protein-protein interaction databases

    BioGridi110681. 8 interactions.
    DIPiDIP-41972N.
    IntActiQ9UIF7. 1 interaction.
    MINTiMINT-151684.
    STRINGi9606.ENSP00000408176.

    Structurei

    Secondary structure

    1
    546
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi87 – 10418
    Helixi109 – 1168
    Helixi120 – 13516
    Helixi139 – 15214
    Helixi156 – 1605
    Helixi164 – 1718
    Helixi177 – 19317
    Helixi202 – 2087
    Helixi214 – 22411
    Helixi234 – 24310
    Helixi253 – 26614
    Helixi272 – 28514
    Beta strandi289 – 2913
    Helixi300 – 3023
    Helixi304 – 31613
    Helixi330 – 3323
    Beta strandi358 – 3603
    Beta strandi366 – 37712
    Beta strandi379 – 38810
    Beta strandi403 – 4053
    Helixi410 – 42415
    Beta strandi447 – 45610
    Beta strandi470 – 4745
    Helixi475 – 4806
    Helixi485 – 49511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X51NMR-A356-497[»]
    3N5NX-ray2.30X/Y76-362[»]
    ProteinModelPortaliQ9UIF7.
    SMRiQ9UIF7. Positions 79-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIF7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini364 – 495132Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi404 – 42623Nudix boxAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1194.
    HOVERGENiHBG052540.
    InParanoidiQ9UIF7.
    KOiK03575.
    PhylomeDBiQ9UIF7.
    TreeFamiTF328549.

    Family and domain databases

    Gene3Di1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    3.90.79.10. 1 hit.
    InterProiIPR011257. DNA_glycosylase.
    IPR004036. Endonuclease-III-like_CS2.
    IPR004035. Endouclease-III_FeS-bd_BS.
    IPR003651. Endouclease3_FeS-loop_motif.
    IPR003265. HhH-GPD_domain.
    IPR023170. HTH_base_excis_C.
    IPR029119. MutY_C.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00730. 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.
    PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
    PS01155. ENDONUCLEASE_III_2. 1 hit.
    PS51462. NUDIX. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform Alpha-1 (identifier: Q9UIF7-1) [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

    MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA    50
    CDGMIAECPG APAGLARQPE EVVLQASVSS YHLFRDVAEV TAFRGSLLSW 100
    YDQEKRDLPW RRRAEDEMDL DRRAYAVWVS EVMLQQTQVA TVINYYTGWM 150
    QKWPTLQDLA SASLEEVNQL WAGLGYYSRG RRLQEGARKV VEELGGHMPR 200
    TAETLQQLLP GVGRYTAGAI ASIAFGQATG VVDGNVARVL CRVRAIGADP 250
    SSTLVSQQLW GLAQQLVDPA RPGDFNQAAM ELGATVCTPQ RPLCSQCPVE 300
    SLCRARQRVE QEQLLASGSL SGSPDVEECA PNTGQCHLCL PPSEPWDQTL 350
    GVVNFPRKAS RKPPREESSA TCVLEQPGAL GAQILLVQRP NSGLLAGLWE 400
    FPSVTWEPSE QLQRKALLQE LQRWAGPLPA THLRHLGEVV HTFSHIKLTY 450
    QVYGLALEGQ TPVTTVPPGA RWLTQEEFHT AAVSTAMKKV FRVYQGQQPG 500
    TCMGSKRSQV SSPCSRKKPR MGQQVLDNFF RSHISTDAHS LNSAAQ 546
    Length:546
    Mass (Da):60,069
    Last modified:May 1, 2000 - v1
    Checksum:i6C79BDB34345DD10
    GO
    Isoform Alpha-2 (identifier: Q9UIF7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-62: Missing.

    Show »
    Length:536
    Mass (Da):59,142
    Checksum:i09F58E89627B124D
    GO
    Isoform Alpha-3 (identifier: Q9UIF7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-63: Missing.

    Show »
    Length:535
    Mass (Da):59,071
    Checksum:iB035F73FE7E5EC88
    GO
    Isoform Beta-1 (identifier: Q9UIF7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.

    Show »
    Length:532
    Mass (Da):58,444
    Checksum:i51845EFF75321F12
    GO
    Isoform Gamma-2 (identifier: Q9UIF7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         53-62: Missing.

    Show »
    Length:522
    Mass (Da):57,517
    Checksum:i8E913C90D72DF87E
    GO
    Isoform Gamma-3 (identifier: Q9UIF7-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         53-63: Missing.

    Show »
    Length:521
    Mass (Da):57,446
    Checksum:i7487EE8AB10FDF6E
    GO

    Sequence cautioni

    The sequence BAA89339.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence BAA89345.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence BAA89339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA89345.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221V → M.2 Publications
    Corresponds to variant rs3219484 [ dbSNP | Ensembl ].
    VAR_018872
    Natural varianti125 – 1251Y → H in FAP2. 1 Publication
    VAR_026045
    Natural varianti128 – 1281W → R in FAP2. 1 Publication
    VAR_026046
    Natural varianti148 – 1481G → IW in FAP2; dysfunctional in base excision repair assay.
    VAR_064938
    Natural varianti176 – 1761Y → C in FAP2; dysfunctional in base excision repair assay. 4 Publications
    Corresponds to variant rs34612342 [ dbSNP | Ensembl ].
    VAR_018873
    Natural varianti179 – 1791R → C in FAP2. 1 Publication
    VAR_064939
    Natural varianti179 – 1791R → H in FAP2. 1 Publication
    VAR_026047
    Natural varianti182 – 1821R → W in FAP2; dysfunctional in base excision repair assay. 2 Publications
    VAR_064940
    Natural varianti238 – 2381R → W in FAP2. 1 Publication
    Corresponds to variant rs34126013 [ dbSNP | Ensembl ].
    VAR_026048
    Natural varianti335 – 3351Q → H.2 Publications
    Corresponds to variant rs3219489 [ dbSNP | Ensembl ].
    VAR_018874
    Natural varianti370 – 3701A → V.
    Corresponds to variant rs35352891 [ dbSNP | Ensembl ].
    VAR_048262
    Natural varianti393 – 3931G → D in FAP2; shows a glycosylase activity very similar to the wild-type protein. 4 Publications
    Corresponds to variant rs36053993 [ dbSNP | Ensembl ].
    VAR_018875
    Natural varianti402 – 4021P → S in GASC; sporadic. 1 Publication
    VAR_026049
    Natural varianti411 – 4111Q → R in GASC; sporadic. 1 Publication
    VAR_026050
    Natural varianti477 – 4771Missing in FAP2; dysfunctional in base excision repair assay.
    VAR_064941
    Natural varianti500 – 5001G → E.1 Publication
    Corresponds to variant rs3219494 [ dbSNP | Ensembl ].
    VAR_018876
    Natural varianti512 – 5121S → F.1 Publication
    Corresponds to variant rs140118273 [ dbSNP | Ensembl ].
    VAR_026051
    Natural varianti526 – 5261L → M.1 Publication
    Corresponds to variant rs3219496 [ dbSNP | Ensembl ].
    VAR_018877
    Natural varianti531 – 5311R → Q.1 Publication
    Corresponds to variant rs3219497 [ dbSNP | Ensembl ].
    VAR_018878

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1414Missing in isoform Beta-1, isoform Gamma-2 and isoform Gamma-3. 1 PublicationVSP_010548Add
    BLAST
    Alternative sequencei53 – 6311Missing in isoform Alpha-3 and isoform Gamma-3. 2 PublicationsVSP_010550Add
    BLAST
    Alternative sequencei53 – 6210Missing in isoform Alpha-2 and isoform Gamma-2. 1 PublicationVSP_010549

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63329 Genomic DNA. Translation: AAC50618.1.
    AB032920 mRNA. Translation: BAA89336.1.
    AB032921 mRNA. Translation: BAA89337.1.
    AB032922 mRNA. Translation: BAA89338.1.
    AB032923 mRNA. Translation: BAA89339.1. Sequence problems.
    AB032924 mRNA. Translation: BAA89340.1.
    AB032925 mRNA. Translation: BAA89341.1.
    AB032926 mRNA. Translation: BAA89342.1.
    AB032927 mRNA. Translation: BAA89343.1.
    AB032928 mRNA. Translation: BAA89344.1.
    AB032929 mRNA. Translation: BAA89345.1. Sequence problems.
    HQ205466 Genomic DNA. Translation: ADP90937.1.
    HQ205468 Genomic DNA. Translation: ADP90947.1.
    HQ205469 Genomic DNA. Translation: ADP90952.1.
    HQ205470 Genomic DNA. Translation: ADP90957.1.
    HQ205472 Genomic DNA. Translation: ADP90967.1.
    HQ205473 Genomic DNA. Translation: ADP90972.1.
    HQ205474 Genomic DNA. Translation: ADP90977.1.
    HQ205475 Genomic DNA. Translation: ADP90982.1.
    HQ205476 Genomic DNA. Translation: ADP90987.1.
    HQ205477 Genomic DNA. Translation: ADP90992.1.
    HQ205479 Genomic DNA. Translation: ADP91002.1.
    HQ205480 Genomic DNA. Translation: ADP91007.1.
    HQ205481 Genomic DNA. Translation: ADP91012.1.
    HQ205482 Genomic DNA. Translation: ADP91017.1.
    HQ205483 Genomic DNA. Translation: ADP91022.1.
    HQ205484 Genomic DNA. Translation: ADP91027.1.
    HQ205485 Genomic DNA. Translation: ADP91032.1.
    HQ205486 Genomic DNA. Translation: ADP91037.1.
    HQ205487 Genomic DNA. Translation: ADP91042.1.
    HQ205488 Genomic DNA. Translation: ADP91047.1.
    HQ205489 Genomic DNA. Translation: ADP91052.1.
    HQ205490 Genomic DNA. Translation: ADP91057.1.
    HQ205491 Genomic DNA. Translation: ADP91062.1.
    HQ205492 Genomic DNA. Translation: ADP91067.1.
    HQ205493 Genomic DNA. Translation: ADP91072.1.
    HQ205494 Genomic DNA. Translation: ADP91077.1.
    HQ205495 Genomic DNA. Translation: ADP91082.1.
    HQ205496 Genomic DNA. Translation: ADP91087.1.
    HQ205497 Genomic DNA. Translation: ADP91092.1.
    HQ205498 Genomic DNA. Translation: ADP91097.1.
    HQ205499 Genomic DNA. Translation: ADP91102.1.
    HQ205500 Genomic DNA. Translation: ADP91107.1.
    HQ205501 Genomic DNA. Translation: ADP91112.1.
    HQ205502 Genomic DNA. Translation: ADP91117.1.
    HQ205503 Genomic DNA. Translation: ADP91122.1.
    HQ205505 Genomic DNA. Translation: ADP91132.1.
    AF527839 Genomic DNA. Translation: AAM78555.1.
    AL359540 Genomic DNA. Translation: CAI21713.1.
    AL359540 Genomic DNA. Translation: CAI21714.1.
    AL359540 Genomic DNA. Translation: CAI21718.1.
    AL359540 Genomic DNA. Translation: CAI21719.1.
    AL359540 Genomic DNA. Translation: CAI21720.1.
    CH471059 Genomic DNA. Translation: EAX06993.1.
    CH471059 Genomic DNA. Translation: EAX06996.1.
    CH471059 Genomic DNA. Translation: EAX06997.1.
    BC003178 mRNA. Translation: AAH03178.1.
    CCDSiCCDS41320.1. [Q9UIF7-3]
    CCDS41321.1. [Q9UIF7-5]
    CCDS41322.1. [Q9UIF7-6]
    CCDS520.1. [Q9UIF7-1]
    RefSeqiNP_001041636.1. NM_001048171.1. [Q9UIF7-3]
    NP_001041637.1. NM_001048172.1. [Q9UIF7-5]
    NP_001041638.1. NM_001048173.1. [Q9UIF7-6]
    NP_001041639.1. NM_001048174.1. [Q9UIF7-6]
    NP_001121897.1. NM_001128425.1.
    NP_036354.1. NM_012222.2. [Q9UIF7-1]
    XP_006710711.1. XM_006710648.1. [Q9UIF7-4]
    UniGeneiHs.271353.

    Genome annotation databases

    EnsembliENST00000354383; ENSP00000346354; ENSG00000132781. [Q9UIF7-5]
    ENST00000355498; ENSP00000347685; ENSG00000132781. [Q9UIF7-6]
    ENST00000372098; ENSP00000361170; ENSG00000132781. [Q9UIF7-1]
    ENST00000372104; ENSP00000361176; ENSG00000132781. [Q9UIF7-6]
    ENST00000372110; ENSP00000361182; ENSG00000132781. [Q9UIF7-2]
    ENST00000372115; ENSP00000361187; ENSG00000132781. [Q9UIF7-3]
    ENST00000448481; ENSP00000409718; ENSG00000132781. [Q9UIF7-4]
    ENST00000456914; ENSP00000407590; ENSG00000132781. [Q9UIF7-6]
    GeneIDi4595.
    KEGGihsa:4595.
    UCSCiuc001cnf.3. human. [Q9UIF7-6]
    uc001cng.3. human. [Q9UIF7-1]
    uc001cnn.3. human. [Q9UIF7-2]

    Polymorphism databases

    DMDMi48428272.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63329 Genomic DNA. Translation: AAC50618.1 .
    AB032920 mRNA. Translation: BAA89336.1 .
    AB032921 mRNA. Translation: BAA89337.1 .
    AB032922 mRNA. Translation: BAA89338.1 .
    AB032923 mRNA. Translation: BAA89339.1 . Sequence problems.
    AB032924 mRNA. Translation: BAA89340.1 .
    AB032925 mRNA. Translation: BAA89341.1 .
    AB032926 mRNA. Translation: BAA89342.1 .
    AB032927 mRNA. Translation: BAA89343.1 .
    AB032928 mRNA. Translation: BAA89344.1 .
    AB032929 mRNA. Translation: BAA89345.1 . Sequence problems.
    HQ205466 Genomic DNA. Translation: ADP90937.1 .
    HQ205468 Genomic DNA. Translation: ADP90947.1 .
    HQ205469 Genomic DNA. Translation: ADP90952.1 .
    HQ205470 Genomic DNA. Translation: ADP90957.1 .
    HQ205472 Genomic DNA. Translation: ADP90967.1 .
    HQ205473 Genomic DNA. Translation: ADP90972.1 .
    HQ205474 Genomic DNA. Translation: ADP90977.1 .
    HQ205475 Genomic DNA. Translation: ADP90982.1 .
    HQ205476 Genomic DNA. Translation: ADP90987.1 .
    HQ205477 Genomic DNA. Translation: ADP90992.1 .
    HQ205479 Genomic DNA. Translation: ADP91002.1 .
    HQ205480 Genomic DNA. Translation: ADP91007.1 .
    HQ205481 Genomic DNA. Translation: ADP91012.1 .
    HQ205482 Genomic DNA. Translation: ADP91017.1 .
    HQ205483 Genomic DNA. Translation: ADP91022.1 .
    HQ205484 Genomic DNA. Translation: ADP91027.1 .
    HQ205485 Genomic DNA. Translation: ADP91032.1 .
    HQ205486 Genomic DNA. Translation: ADP91037.1 .
    HQ205487 Genomic DNA. Translation: ADP91042.1 .
    HQ205488 Genomic DNA. Translation: ADP91047.1 .
    HQ205489 Genomic DNA. Translation: ADP91052.1 .
    HQ205490 Genomic DNA. Translation: ADP91057.1 .
    HQ205491 Genomic DNA. Translation: ADP91062.1 .
    HQ205492 Genomic DNA. Translation: ADP91067.1 .
    HQ205493 Genomic DNA. Translation: ADP91072.1 .
    HQ205494 Genomic DNA. Translation: ADP91077.1 .
    HQ205495 Genomic DNA. Translation: ADP91082.1 .
    HQ205496 Genomic DNA. Translation: ADP91087.1 .
    HQ205497 Genomic DNA. Translation: ADP91092.1 .
    HQ205498 Genomic DNA. Translation: ADP91097.1 .
    HQ205499 Genomic DNA. Translation: ADP91102.1 .
    HQ205500 Genomic DNA. Translation: ADP91107.1 .
    HQ205501 Genomic DNA. Translation: ADP91112.1 .
    HQ205502 Genomic DNA. Translation: ADP91117.1 .
    HQ205503 Genomic DNA. Translation: ADP91122.1 .
    HQ205505 Genomic DNA. Translation: ADP91132.1 .
    AF527839 Genomic DNA. Translation: AAM78555.1 .
    AL359540 Genomic DNA. Translation: CAI21713.1 .
    AL359540 Genomic DNA. Translation: CAI21714.1 .
    AL359540 Genomic DNA. Translation: CAI21718.1 .
    AL359540 Genomic DNA. Translation: CAI21719.1 .
    AL359540 Genomic DNA. Translation: CAI21720.1 .
    CH471059 Genomic DNA. Translation: EAX06993.1 .
    CH471059 Genomic DNA. Translation: EAX06996.1 .
    CH471059 Genomic DNA. Translation: EAX06997.1 .
    BC003178 mRNA. Translation: AAH03178.1 .
    CCDSi CCDS41320.1. [Q9UIF7-3 ]
    CCDS41321.1. [Q9UIF7-5 ]
    CCDS41322.1. [Q9UIF7-6 ]
    CCDS520.1. [Q9UIF7-1 ]
    RefSeqi NP_001041636.1. NM_001048171.1. [Q9UIF7-3 ]
    NP_001041637.1. NM_001048172.1. [Q9UIF7-5 ]
    NP_001041638.1. NM_001048173.1. [Q9UIF7-6 ]
    NP_001041639.1. NM_001048174.1. [Q9UIF7-6 ]
    NP_001121897.1. NM_001128425.1.
    NP_036354.1. NM_012222.2. [Q9UIF7-1 ]
    XP_006710711.1. XM_006710648.1. [Q9UIF7-4 ]
    UniGenei Hs.271353.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X51 NMR - A 356-497 [» ]
    3N5N X-ray 2.30 X/Y 76-362 [» ]
    ProteinModelPortali Q9UIF7.
    SMRi Q9UIF7. Positions 79-497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110681. 8 interactions.
    DIPi DIP-41972N.
    IntActi Q9UIF7. 1 interaction.
    MINTi MINT-151684.
    STRINGi 9606.ENSP00000408176.

    PTM databases

    PhosphoSitei Q9UIF7.

    Polymorphism databases

    DMDMi 48428272.

    Proteomic databases

    MaxQBi Q9UIF7.
    PaxDbi Q9UIF7.
    PRIDEi Q9UIF7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354383 ; ENSP00000346354 ; ENSG00000132781 . [Q9UIF7-5 ]
    ENST00000355498 ; ENSP00000347685 ; ENSG00000132781 . [Q9UIF7-6 ]
    ENST00000372098 ; ENSP00000361170 ; ENSG00000132781 . [Q9UIF7-1 ]
    ENST00000372104 ; ENSP00000361176 ; ENSG00000132781 . [Q9UIF7-6 ]
    ENST00000372110 ; ENSP00000361182 ; ENSG00000132781 . [Q9UIF7-2 ]
    ENST00000372115 ; ENSP00000361187 ; ENSG00000132781 . [Q9UIF7-3 ]
    ENST00000448481 ; ENSP00000409718 ; ENSG00000132781 . [Q9UIF7-4 ]
    ENST00000456914 ; ENSP00000407590 ; ENSG00000132781 . [Q9UIF7-6 ]
    GeneIDi 4595.
    KEGGi hsa:4595.
    UCSCi uc001cnf.3. human. [Q9UIF7-6 ]
    uc001cng.3. human. [Q9UIF7-1 ]
    uc001cnn.3. human. [Q9UIF7-2 ]

    Organism-specific databases

    CTDi 4595.
    GeneCardsi GC01M045794.
    GeneReviewsi MUTYH.
    HGNCi HGNC:7527. MUTYH.
    HPAi HPA008732.
    MIMi 604933. gene.
    608456. phenotype.
    613659. phenotype.
    neXtProti NX_Q9UIF7.
    Orphaneti 26106. Familial gastric cancer.
    247798. MUTYH-related attenuated familial adenomatous polyposis.
    PharmGKBi PA31328.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1194.
    HOVERGENi HBG052540.
    InParanoidi Q9UIF7.
    KOi K03575.
    PhylomeDBi Q9UIF7.
    TreeFami TF328549.

    Enzyme and pathway databases

    Reactomei REACT_1064. Displacement of DNA glycosylase by APE1.
    REACT_1729. Cleavage of the damaged purine.
    REACT_2176. Recognition and association of DNA glycosylase with site containing an affected purine.

    Miscellaneous databases

    EvolutionaryTracei Q9UIF7.
    GeneWikii MUTYH.
    GenomeRNAii 4595.
    NextBioi 17664.
    PROi Q9UIF7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UIF7.
    Bgeei Q9UIF7.
    CleanExi HS_MUTYH.
    Genevestigatori Q9UIF7.

    Family and domain databases

    Gene3Di 1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    3.90.79.10. 1 hit.
    InterProi IPR011257. DNA_glycosylase.
    IPR004036. Endonuclease-III-like_CS2.
    IPR004035. Endouclease-III_FeS-bd_BS.
    IPR003651. Endouclease3_FeS-loop_motif.
    IPR003265. HhH-GPD_domain.
    IPR023170. HTH_base_excis_C.
    IPR029119. MutY_C.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view ]
    Pfami PF00730. HhH-GPD. 1 hit.
    PF14815. NUDIX_4. 1 hit.
    [Graphical view ]
    SMARTi SM00478. ENDO3c. 1 hit.
    SM00525. FES. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48150. SSF48150. 1 hit.
    SSF55811. SSF55811. 1 hit.
    PROSITEi PS00764. ENDONUCLEASE_III_1. 1 hit.
    PS01155. ENDONUCLEASE_III_2. 1 hit.
    PS51462. NUDIX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage."
      Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F., Miller J.H.
      J. Bacteriol. 178:3885-3892(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-3).
    2. "Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria."
      Ohtsubo T., Nishioka K., Imaiso Y., Iwai S., Shimokawa H., Oda H., Fujikawa T., Nakabeppu Y.
      Nucleic Acids Res. 28:1355-1364(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; ALPHA-3; BETA-1; GAMMA-2 AND GAMMA-3), FUNCTION.
    3. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
      Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
      Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-22; HIS-335; GLU-500; MET-526 AND GLN-531.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 ALPHA-3).
      Tissue: Kidney.
    8. "Solution structure of the NUDIX domain from human A/G-specific adenine DNA glycosylase alpha-3 splice isoform."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 356-497.
    9. "Inherited variants of MYH associated with somatic G:C-->T:A mutations in colorectal tumors."
      Al-Tassan N., Chmiel N.H., Maynard J., Fleming N., Livingston A.L., Williams G.T., Hodges A.K., Davies D.R., David S.S., Sampson J.R., Cheadle J.P.
      Nat. Genet. 30:227-232(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP2 CYS-176 AND ASP-393.
    10. "Autosomal recessive colorectal adenomatous polyposis due to inherited mutations of MYH."
      Sampson J.R., Dolwani S., Jones S., Eccles D., Ellis A., Evans D.G., Frayling I., Jordan S., Maher E.R., Mak T., Maynard J., Pigatto F., Shaw J., Cheadle J.P.
      Lancet 362:39-41(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP2 ARG-128; CYS-176 AND ASP-393.
    11. Cited for: VARIANTS FAP2 CYS-176 AND ASP-393, VARIANTS MET-22; HIS-335 AND PHE-512.
    12. Cited for: VARIANTS FAP2 HIS-125; HIS-179 AND TRP-238.
    13. Cited for: VARIANTS GASC SER-402 AND ARG-411.
    14. "Heterogeneous molecular mechanisms underlie attenuated familial adenomatous polyposis."
      Cattaneo F., Molatore S., Mihalatos M., Apessos A., Venesio T., Bione S., Grignani P., Nasioulas G., Ranzani G.N.
      Genet. Med. 9:836-841(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP2 CYS-176; CYS-179; TRP-182 AND ASP-393.
    15. "MUTYH mutations associated with familial adenomatous polyposis: functional characterization by a mammalian cell-based assay."
      Molatore S., Russo M.T., D'Agostino V.G., Barone F., Matsumoto Y., Albertini A.M., Minoprio A., Degan P., Mazzei F., Bignami M., Ranzani G.N.
      Hum. Mutat. 31:159-166(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP2 148-GLY ILE-TRP DELINS; TRP-182 AND 477-GLU DEL, CHARACTERIZATION OF VARIANTS FAP2 148-GLY ILE-TRP DELINS; CYS-176; TRP-182; ASP-393 AND 477-GLU DEL.

    Entry informationi

    Entry nameiMUTYH_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIF7
    Secondary accession number(s): D3DPZ4
    , Q15830, Q9UBP2, Q9UBS7, Q9UIF4, Q9UIF5, Q9UIF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3