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Q9UIF7 (MUTYH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A/G-specific adenine DNA glycosylase

EC=3.2.2.-
Alternative name(s):
MutY homolog
Short name=hMYH
Gene names
Name:MUTYH
Synonyms:MYH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Cofactor

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.

Subcellular location

Nucleus.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

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.
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 (Ref.13). Ref.13

Sequence similarities

Belongs to the Nth/MutY family.

Contains 1 nudix hydrolase domain.

Sequence caution

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

The sequence BAA89339.1 differs from that shown. Reason: Probable cloning artifact.

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

The sequence BAA89345.1 differs from that shown. Reason: Probable cloning artifact.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha-1 (identifier: Q9UIF7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Alpha-2 (identifier: Q9UIF7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     53-62: Missing.
Isoform Alpha-3 (identifier: Q9UIF7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-63: Missing.
Isoform Beta-1 (identifier: Q9UIF7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
Isoform Gamma-2 (identifier: Q9UIF7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
     53-62: Missing.
Isoform Gamma-3 (identifier: Q9UIF7-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546A/G-specific adenine DNA glycosylase
PRO_0000102239

Regions

Domain364 – 495132Nudix hydrolase
Motif404 – 42623Nudix box

Sites

Metal binding2871Iron-sulfur (4Fe-4S) By similarity
Metal binding2941Iron-sulfur (4Fe-4S) By similarity
Metal binding2971Iron-sulfur (4Fe-4S) By similarity
Metal binding3031Iron-sulfur (4Fe-4S) By similarity

Natural variations

Alternative sequence1 – 1414Missing in isoform Beta-1, isoform Gamma-2 and isoform Gamma-3.
VSP_010548
Alternative sequence53 – 6311Missing in isoform Alpha-3 and isoform Gamma-3.
VSP_010550
Alternative sequence53 – 6210Missing in isoform Alpha-2 and isoform Gamma-2.
VSP_010549
Natural variant221V → M. Ref.4 Ref.11
Corresponds to variant rs3219484 [ dbSNP | Ensembl ].
VAR_018872
Natural variant1251Y → H in FAP2. Ref.12
VAR_026045
Natural variant1281W → R in FAP2. Ref.10
VAR_026046
Natural variant1481G → IW in FAP2; dysfunctional in base excision repair assay.
VAR_064938
Natural variant1761Y → C in FAP2; dysfunctional in base excision repair assay. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Corresponds to variant rs34612342 [ dbSNP | Ensembl ].
VAR_018873
Natural variant1791R → C in FAP2. Ref.14
VAR_064939
Natural variant1791R → H in FAP2. Ref.12
VAR_026047
Natural variant1821R → W in FAP2; dysfunctional in base excision repair assay. Ref.14 Ref.15
VAR_064940
Natural variant2381R → W in FAP2. Ref.12
Corresponds to variant rs34126013 [ dbSNP | Ensembl ].
VAR_026048
Natural variant3351Q → H. Ref.4 Ref.11
Corresponds to variant rs3219489 [ dbSNP | Ensembl ].
VAR_018874
Natural variant3701A → V.
Corresponds to variant rs35352891 [ dbSNP | Ensembl ].
VAR_048262
Natural variant3931G → D in FAP2; shows a glycosylase activity very similar to the wild-type protein. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Corresponds to variant rs36053993 [ dbSNP | Ensembl ].
VAR_018875
Natural variant4021P → S in GASC; sporadic. Ref.13
VAR_026049
Natural variant4111Q → R in GASC; sporadic. Ref.13
VAR_026050
Natural variant4771Missing in FAP2; dysfunctional in base excision repair assay.
VAR_064941
Natural variant5001G → E. Ref.4
Corresponds to variant rs3219494 [ dbSNP | Ensembl ].
VAR_018876
Natural variant5121S → F. Ref.11
Corresponds to variant rs140118273 [ dbSNP | Ensembl ].
VAR_026051
Natural variant5261L → M. Ref.4
Corresponds to variant rs3219496 [ dbSNP | Ensembl ].
VAR_018877
Natural variant5311R → Q. Ref.4
Corresponds to variant rs3219497 [ dbSNP | Ensembl ].
VAR_018878

Secondary structure

.................................................. 546
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6C79BDB34345DD10

FASTA54660,069
        10         20         30         40         50         60 
MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA CDGMIAECPG 

        70         80         90        100        110        120 
APAGLARQPE EVVLQASVSS YHLFRDVAEV TAFRGSLLSW YDQEKRDLPW RRRAEDEMDL 

       130        140        150        160        170        180 
DRRAYAVWVS EVMLQQTQVA TVINYYTGWM QKWPTLQDLA SASLEEVNQL WAGLGYYSRG 

       190        200        210        220        230        240 
RRLQEGARKV VEELGGHMPR TAETLQQLLP GVGRYTAGAI ASIAFGQATG VVDGNVARVL 

       250        260        270        280        290        300 
CRVRAIGADP SSTLVSQQLW GLAQQLVDPA RPGDFNQAAM ELGATVCTPQ RPLCSQCPVE 

       310        320        330        340        350        360 
SLCRARQRVE QEQLLASGSL SGSPDVEECA PNTGQCHLCL PPSEPWDQTL GVVNFPRKAS 

       370        380        390        400        410        420 
RKPPREESSA TCVLEQPGAL GAQILLVQRP NSGLLAGLWE FPSVTWEPSE QLQRKALLQE 

       430        440        450        460        470        480 
LQRWAGPLPA THLRHLGEVV HTFSHIKLTY QVYGLALEGQ TPVTTVPPGA RWLTQEEFHT 

       490        500        510        520        530        540 
AAVSTAMKKV FRVYQGQQPG TCMGSKRSQV SSPCSRKKPR MGQQVLDNFF RSHISTDAHS 


LNSAAQ 

« Hide

Isoform Alpha-2 [UniParc].

Checksum: 09F58E89627B124D
Show »

FASTA53659,142
Isoform Alpha-3 [UniParc].

Checksum: B035F73FE7E5EC88
Show »

FASTA53559,071
Isoform Beta-1 [UniParc].

Checksum: 51845EFF75321F12
Show »

FASTA53258,444
Isoform Gamma-2 [UniParc].

Checksum: 8E913C90D72DF87E
Show »

FASTA52257,517
Isoform Gamma-3 [UniParc].

Checksum: 7487EE8AB10FDF6E
Show »

FASTA52157,446

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [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]"Multiple colorectal adenomas, classic adenomatous polyposis, and germ-line mutations in MYH."
Sieber O.M., Lipton L., Crabtree M., Heinimann K., Fidalgo P., Phillips R.K.S., Bisgaard M.-L., Orntoft T.F., Aaltonen L.A., Hodgson S.V., Thomas H.J.W., Tomlinson I.P.M.
N. Engl. J. Med. 348:791-799(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FAP2 CYS-176 AND ASP-393, VARIANTS MET-22; HIS-335 AND PHE-512.
[12]"Germline MUTYH (MYH) mutations in Portuguese individuals with multiple colorectal adenomas."
Isidro G., Laranjeira F., Pires A., Leite J., Regateiro F., Castro e Sousa F., Soares J., Castro C., Giria J., Brito M.J., Medeira A., Teixeira R., Morna H., Gaspar I., Marinho C., Jorge R., Brehm A., Ramos J.S., Boavida M.G.
Hum. Mutat. 24:353-354(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FAP2 HIS-125; HIS-179 AND TRP-238.
[13]"Genetic alterations of the MYH gene in gastric cancer."
Kim C.J., Cho Y.G., Park C.H., Kim S.Y., Nam S.W., Lee S.H., Yoo N.J., Lee J.Y., Park W.S.
Oncogene 23:6820-6822(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41320.1. [Q9UIF7-3]
CCDS41321.1. [Q9UIF7-5]
CCDS41322.1. [Q9UIF7-6]
CCDS520.1. [Q9UIF7-1]
RefSeqNP_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_005270937.1. XM_005270880.2. [Q9UIF7-2]
XP_005270938.1. XM_005270881.2. [Q9UIF7-4]
XP_005270941.1. XM_005270884.2.
XP_005270942.1. XM_005270885.1.
XP_006710711.1. XM_006710648.1. [Q9UIF7-4]
XP_006710712.1. XM_006710649.1. [Q9UIF7-6]
UniGeneHs.271353.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X51NMR-A356-497[»]
3N5NX-ray2.30X/Y76-362[»]
ProteinModelPortalQ9UIF7.
SMRQ9UIF7. Positions 79-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110681. 8 interactions.
DIPDIP-41972N.
IntActQ9UIF7. 1 interaction.
MINTMINT-151684.
STRING9606.ENSP00000408176.

PTM databases

PhosphoSiteQ9UIF7.

Polymorphism databases

DMDM48428272.

Proteomic databases

MaxQBQ9UIF7.
PaxDbQ9UIF7.
PRIDEQ9UIF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354383; ENSP00000346354; ENSG00000132781. [Q9UIF7-5]
ENST00000355498; ENSP00000347685; ENSG00000132781. [Q9UIF7-6]
ENST00000372098; ENSP00000361170; ENSG00000132781. [Q9UIF7-1]
ENST00000372100; ENSP00000361172; ENSG00000132781. [Q9UIF7-4]
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]
GeneID4595.
KEGGhsa:4595.
UCSCuc001cnf.3. human. [Q9UIF7-6]
uc001cng.3. human. [Q9UIF7-1]
uc001cnn.3. human. [Q9UIF7-2]

Organism-specific databases

CTD4595.
GeneCardsGC01M045794.
GeneReviewsMUTYH.
HGNCHGNC:7527. MUTYH.
HPAHPA008732.
MIM604933. gene.
608456. phenotype.
613659. phenotype.
neXtProtNX_Q9UIF7.
Orphanet26106. Familial gastric cancer.
247798. MUTYH-related attenuated familial adenomatous polyposis.
PharmGKBPA31328.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1194.
HOVERGENHBG052540.
InParanoidQ9UIF7.
KOK03575.
PhylomeDBQ9UIF7.
TreeFamTF328549.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ9UIF7.
BgeeQ9UIF7.
CleanExHS_MUTYH.
GenevestigatorQ9UIF7.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProIPR011257. 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]
PfamPF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
PS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UIF7.
GeneWikiMUTYH.
GenomeRNAi4595.
NextBio17664.
PROQ9UIF7.
SOURCESearch...

Entry information

Entry nameMUTYH_HUMAN
AccessionPrimary (citable) accession number: Q9UIF7
Secondary accession number(s): D3DPZ4 expand/collapse secondary AC list , Q15830, Q9UBP2, Q9UBS7, Q9UIF4, Q9UIF5, Q9UIF6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM