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Q9UIF7

- MUTYH_HUMAN

UniProt

Q9UIF7 - MUTYH_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UIF7.
CleanExiHS_MUTYH.
ExpressionAtlasiQ9UIF7. baseline.
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 – 10418Combined sources
Helixi109 – 1168Combined sources
Helixi120 – 13516Combined sources
Helixi139 – 15214Combined sources
Helixi156 – 1605Combined sources
Helixi164 – 1718Combined sources
Helixi177 – 19317Combined sources
Helixi202 – 2087Combined sources
Helixi214 – 22411Combined sources
Helixi234 – 24310Combined sources
Helixi253 – 26614Combined sources
Helixi272 – 28514Combined sources
Beta strandi289 – 2913Combined sources
Helixi300 – 3023Combined sources
Helixi304 – 31613Combined sources
Helixi330 – 3323Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi366 – 37712Combined sources
Beta strandi379 – 38810Combined sources
Beta strandi403 – 4053Combined sources
Helixi410 – 42415Combined sources
Beta strandi447 – 45610Combined sources
Beta strandi470 – 4745Combined sources
Helixi475 – 4806Combined sources
Helixi485 – 49511Combined sources

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.
GeneTreeiENSGT00510000047220.
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

        10         20         30         40         50
MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA
60 70 80 90 100
CDGMIAECPG APAGLARQPE EVVLQASVSS YHLFRDVAEV TAFRGSLLSW
110 120 130 140 150
YDQEKRDLPW RRRAEDEMDL DRRAYAVWVS EVMLQQTQVA TVINYYTGWM
160 170 180 190 200
QKWPTLQDLA SASLEEVNQL WAGLGYYSRG RRLQEGARKV VEELGGHMPR
210 220 230 240 250
TAETLQQLLP GVGRYTAGAI ASIAFGQATG VVDGNVARVL CRVRAIGADP
260 270 280 290 300
SSTLVSQQLW GLAQQLVDPA RPGDFNQAAM ELGATVCTPQ RPLCSQCPVE
310 320 330 340 350
SLCRARQRVE QEQLLASGSL SGSPDVEECA PNTGQCHLCL PPSEPWDQTL
360 370 380 390 400
GVVNFPRKAS RKPPREESSA TCVLEQPGAL GAQILLVQRP NSGLLAGLWE
410 420 430 440 450
FPSVTWEPSE QLQRKALLQE LQRWAGPLPA THLRHLGEVV HTFSHIKLTY
460 470 480 490 500
QVYGLALEGQ TPVTTVPPGA RWLTQEEFHT AAVSTAMKKV FRVYQGQQPG
510 520 530 540
TCMGSKRSQV SSPCSRKKPR MGQQVLDNFF RSHISTDAHS LNSAAQ
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]
CCDS72776.1. [Q9UIF7-4]
CCDS72777.1. [Q9UIF7-2]
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_001280119.1. NM_001293190.1. [Q9UIF7-2]
NP_001280120.1. NM_001293191.1. [Q9UIF7-4]
NP_001280121.1. NM_001293192.1.
NP_001280124.1. NM_001293195.1. [Q9UIF7-6]
NP_001280125.1. NM_001293196.1.
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 ]
CCDS72776.1. [Q9UIF7-4 ]
CCDS72777.1. [Q9UIF7-2 ]
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_001280119.1. NM_001293190.1. [Q9UIF7-2 ]
NP_001280120.1. NM_001293191.1. [Q9UIF7-4 ]
NP_001280121.1. NM_001293192.1.
NP_001280124.1. NM_001293195.1. [Q9UIF7-6 ]
NP_001280125.1. NM_001293196.1.
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.
GeneTreei ENSGT00510000047220.
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

Bgeei Q9UIF7.
CleanExi HS_MUTYH.
ExpressionAtlasi Q9UIF7. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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