Q9UIF7 (MUTYH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Protein existence	Evidence 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 is not important for the catalytic activity, 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Tumor suppressor
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	depurination Traceable author statement. Source: Reactome mismatch repair Traceable author statement PubMed 7823963. Source: ProtInc
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW MutSalpha complex binding Inferred from direct assay PubMed 11801590. Source: HGNC endonuclease activity Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 546

546

A/G-specific adenine DNA glycosylase

PRO_0000102239

Regions

Domain

364 – 495

132

Nudix hydrolase

Motif

404 – 426

23

Nudix box

Sites

Metal binding

287

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

294

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

297

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

303

1

Iron-sulfur (4Fe-4S) By similarity

Natural variations

Alternative sequence

1 – 14

14

Missing in isoform Beta-1, isoform Gamma-2 and isoform Gamma-3.

VSP_010548

Alternative sequence

53 – 63

11

Missing in isoform Alpha-3 and isoform Gamma-3.

VSP_010550

Alternative sequence

53 – 62

10

Missing in isoform Alpha-2 and isoform Gamma-2.

VSP_010549

Natural variant

22

1

V → M. Ref.4 Ref.11
Corresponds to variant rs3219484 [ dbSNP | Ensembl ].

VAR_018872

Natural variant

125

1

Y → H in FAP2. Ref.12

VAR_026045

Natural variant

128

1

W → R in FAP2. Ref.10

VAR_026046

Natural variant

148

1

G → IW in FAP2; dysfunctional in base excision repair assay.

VAR_064938

Natural variant

176

1

Y → 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 variant

179

1

R → C in FAP2. Ref.14

VAR_064939

Natural variant

179

1

R → H in FAP2. Ref.12

VAR_026047

Natural variant

182

1

R → W in FAP2; dysfunctional in base excision repair assay. Ref.14 Ref.15

VAR_064940

Natural variant

238

1

R → W in FAP2. Ref.12
Corresponds to variant rs34126013 [ dbSNP | Ensembl ].

VAR_026048

Natural variant

335

1

Q → H. Ref.4 Ref.11
Corresponds to variant rs3219489 [ dbSNP | Ensembl ].

VAR_018874

Natural variant

370

1

A → V.
Corresponds to variant rs35352891 [ dbSNP | Ensembl ].

VAR_048262

Natural variant

393

1

G → 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 variant

402

1

P → S in GASC; sporadic. Ref.13

VAR_026049

Natural variant

411

1

Q → R in GASC; sporadic. Ref.13

VAR_026050

Natural variant

477

1

Missing in FAP2; dysfunctional in base excision repair assay.

VAR_064941

Natural variant

500

1

G → E. Ref.4
Corresponds to variant rs3219494 [ dbSNP | Ensembl ].

VAR_018876

Natural variant

512

1

S → F. Ref.11

VAR_026051

Natural variant

526

1

L → M. Ref.4
Corresponds to variant rs3219496 [ dbSNP | Ensembl ].

VAR_018877

Natural variant

531

1

R → Q. Ref.4
Corresponds to variant rs3219497 [ dbSNP | Ensembl ].

VAR_018878

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

546

Helix Strand Turn

Details...

Helix

87 – 104

18

Helix

109 – 116

8

Helix

120 – 135

16

Helix

139 – 152

14

Helix

156 – 160

5

Helix

164 – 171

8

Helix

177 – 193

17

Helix

202 – 208

7

Helix

214 – 224

11

Helix

234 – 243

10

Helix

253 – 266

14

Helix

272 – 285

14

Beta strand

289 – 291

3

Helix

300 – 302

3

Helix

304 – 316

13

Helix

330 – 332

3

Beta strand

358 – 360

3

Beta strand

366 – 377

12

Beta strand

379 – 388

10

Beta strand

403 – 405

3

Helix

410 – 424

15

Beta strand

447 – 456

10

Beta strand

470 – 474

5

Helix

475 – 480

6

Helix

485 – 495

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6C79BDB34345DD10	FASTA	546	60,069
	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
	Isoform Alpha-2 [UniParc]. Checksum: 09F58E89627B124D	FASTA	536	59,142
	10 20 30 40 50 60 MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA CDAGLARQPE 70 80 90 100 110 120 EVVLQASVSS YHLFRDVAEV TAFRGSLLSW YDQEKRDLPW RRRAEDEMDL DRRAYAVWVS 130 140 150 160 170 180 EVMLQQTQVA TVINYYTGWM QKWPTLQDLA SASLEEVNQL WAGLGYYSRG RRLQEGARKV 190 200 210 220 230 240 VEELGGHMPR TAETLQQLLP GVGRYTAGAI ASIAFGQATG VVDGNVARVL CRVRAIGADP 250 260 270 280 290 300 SSTLVSQQLW GLAQQLVDPA RPGDFNQAAM ELGATVCTPQ RPLCSQCPVE SLCRARQRVE 310 320 330 340 350 360 QEQLLASGSL SGSPDVEECA PNTGQCHLCL PPSEPWDQTL GVVNFPRKAS RKPPREESSA 370 380 390 400 410 420 TCVLEQPGAL GAQILLVQRP NSGLLAGLWE FPSVTWEPSE QLQRKALLQE LQRWAGPLPA 430 440 450 460 470 480 THLRHLGEVV HTFSHIKLTY QVYGLALEGQ TPVTTVPPGA RWLTQEEFHT AAVSTAMKKV 490 500 510 520 530 FRVYQGQQPG TCMGSKRSQV SSPCSRKKPR MGQQVLDNFF RSHISTDAHS LNSAAQ
	Isoform Alpha-3 [UniParc]. Checksum: B035F73FE7E5EC88	FASTA	535	59,071
	10 20 30 40 50 60 MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA CDGLARQPEE 70 80 90 100 110 120 VVLQASVSSY HLFRDVAEVT AFRGSLLSWY DQEKRDLPWR RRAEDEMDLD RRAYAVWVSE 130 140 150 160 170 180 VMLQQTQVAT VINYYTGWMQ KWPTLQDLAS ASLEEVNQLW AGLGYYSRGR RLQEGARKVV 190 200 210 220 230 240 EELGGHMPRT AETLQQLLPG VGRYTAGAIA SIAFGQATGV VDGNVARVLC RVRAIGADPS 250 260 270 280 290 300 STLVSQQLWG LAQQLVDPAR PGDFNQAAME LGATVCTPQR PLCSQCPVES LCRARQRVEQ 310 320 330 340 350 360 EQLLASGSLS GSPDVEECAP NTGQCHLCLP PSEPWDQTLG VVNFPRKASR KPPREESSAT 370 380 390 400 410 420 CVLEQPGALG AQILLVQRPN SGLLAGLWEF PSVTWEPSEQ LQRKALLQEL QRWAGPLPAT 430 440 450 460 470 480 HLRHLGEVVH TFSHIKLTYQ VYGLALEGQT PVTTVPPGAR WLTQEEFHTA AVSTAMKKVF 490 500 510 520 530 RVYQGQQPGT CMGSKRSQVS SPCSRKKPRM GQQVLDNFFR SHISTDAHSL NSAAQ
	Isoform Beta-1 [UniParc]. Checksum: 51845EFF75321F12	FASTA	532	58,444
	10 20 30 40 50 60 MRKPRAAVGS GHRKQAASQE GRQKHAKNNS QAKPSACDGM IAECPGAPAG LARQPEEVVL 70 80 90 100 110 120 QASVSSYHLF RDVAEVTAFR GSLLSWYDQE KRDLPWRRRA EDEMDLDRRA YAVWVSEVML 130 140 150 160 170 180 QQTQVATVIN YYTGWMQKWP TLQDLASASL EEVNQLWAGL GYYSRGRRLQ EGARKVVEEL 190 200 210 220 230 240 GGHMPRTAET LQQLLPGVGR YTAGAIASIA FGQATGVVDG NVARVLCRVR AIGADPSSTL 250 260 270 280 290 300 VSQQLWGLAQ QLVDPARPGD FNQAAMELGA TVCTPQRPLC SQCPVESLCR ARQRVEQEQL 310 320 330 340 350 360 LASGSLSGSP DVEECAPNTG QCHLCLPPSE PWDQTLGVVN FPRKASRKPP REESSATCVL 370 380 390 400 410 420 EQPGALGAQI LLVQRPNSGL LAGLWEFPSV TWEPSEQLQR KALLQELQRW AGPLPATHLR 430 440 450 460 470 480 HLGEVVHTFS HIKLTYQVYG LALEGQTPVT TVPPGARWLT QEEFHTAAVS TAMKKVFRVY 490 500 510 520 530 QGQQPGTCMG SKRSQVSSPC SRKKPRMGQQ VLDNFFRSHI STDAHSLNSA AQ
	Isoform Gamma-2 [UniParc]. Checksum: 8E913C90D72DF87E	FASTA	522	57,517
	10 20 30 40 50 60 MRKPRAAVGS GHRKQAASQE GRQKHAKNNS QAKPSACDAG LARQPEEVVL QASVSSYHLF 70 80 90 100 110 120 RDVAEVTAFR GSLLSWYDQE KRDLPWRRRA EDEMDLDRRA YAVWVSEVML QQTQVATVIN 130 140 150 160 170 180 YYTGWMQKWP TLQDLASASL EEVNQLWAGL GYYSRGRRLQ EGARKVVEEL GGHMPRTAET 190 200 210 220 230 240 LQQLLPGVGR YTAGAIASIA FGQATGVVDG NVARVLCRVR AIGADPSSTL VSQQLWGLAQ 250 260 270 280 290 300 QLVDPARPGD FNQAAMELGA TVCTPQRPLC SQCPVESLCR ARQRVEQEQL LASGSLSGSP 310 320 330 340 350 360 DVEECAPNTG QCHLCLPPSE PWDQTLGVVN FPRKASRKPP REESSATCVL EQPGALGAQI 370 380 390 400 410 420 LLVQRPNSGL LAGLWEFPSV TWEPSEQLQR KALLQELQRW AGPLPATHLR HLGEVVHTFS 430 440 450 460 470 480 HIKLTYQVYG LALEGQTPVT TVPPGARWLT QEEFHTAAVS TAMKKVFRVY QGQQPGTCMG 490 500 510 520 SKRSQVSSPC SRKKPRMGQQ VLDNFFRSHI STDAHSLNSA AQ
	Isoform Gamma-3 [UniParc]. Checksum: 7487EE8AB10FDF6E	FASTA	521	57,446
	10 20 30 40 50 60 MRKPRAAVGS GHRKQAASQE GRQKHAKNNS QAKPSACDGL ARQPEEVVLQ ASVSSYHLFR 70 80 90 100 110 120 DVAEVTAFRG SLLSWYDQEK RDLPWRRRAE DEMDLDRRAY AVWVSEVMLQ QTQVATVINY 130 140 150 160 170 180 YTGWMQKWPT LQDLASASLE EVNQLWAGLG YYSRGRRLQE GARKVVEELG GHMPRTAETL 190 200 210 220 230 240 QQLLPGVGRY TAGAIASIAF GQATGVVDGN VARVLCRVRA IGADPSSTLV SQQLWGLAQQ 250 260 270 280 290 300 LVDPARPGDF NQAAMELGAT VCTPQRPLCS QCPVESLCRA RQRVEQEQLL ASGSLSGSPD 310 320 330 340 350 360 VEECAPNTGQ CHLCLPPSEP WDQTLGVVNF PRKASRKPPR EESSATCVLE QPGALGAQIL 370 380 390 400 410 420 LVQRPNSGLL AGLWEFPSVT WEPSEQLQRK ALLQELQRWA GPLPATHLRH LGEVVHTFSH 430 440 450 460 470 480 IKLTYQVYGL ALEGQTPVTT VPPGARWLTQ EEFHTAAVST AMKKVFRVYQ GQQPGTCMGS 490 500 510 520 KRSQVSSPCS RKKPRMGQQV LDNFFRSHIS TDAHSLNSAA Q

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

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.

IPI

IPI00414235.
IPI00414236.
IPI00414237.
IPI00456700.
IPI00746950.
IPI00844241.

RefSeq

NP_001041636.1. NM_001048171.1.
NP_001041637.1. NM_001048172.1.
NP_001041638.1. NM_001048173.1.
NP_001041639.1. NM_001048174.1.
NP_001121897.1. NM_001128425.1.
NP_036354.1. NM_012222.2.

UniGene

Hs.271353.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X51	NMR	-	A	356-497	[»]
3N5N	X-ray	2.30	X/Y	76-362	[»]

ProteinModelPortal

Q9UIF7.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41972N.

IntAct

Q9UIF7. 1 interaction.

STRING

9606.ENSP00000408176.

PTM databases

PhosphoSite

Q9UIF7.

Polymorphism databases

DMDM

48428272.

Proteomic databases

PaxDb

Q9UIF7.

PRIDE

Q9UIF7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354383; ENSP00000346354; ENSG00000132781.
ENST00000355498; ENSP00000347685; ENSG00000132781.
ENST00000372098; ENSP00000361170; ENSG00000132781.
ENST00000372100; ENSP00000361172; ENSG00000132781.
ENST00000372104; ENSP00000361176; ENSG00000132781.
ENST00000372110; ENSP00000361182; ENSG00000132781.
ENST00000372115; ENSP00000361187; ENSG00000132781.
ENST00000448481; ENSP00000409718; ENSG00000132781.
ENST00000456914; ENSP00000407590; ENSG00000132781.

GeneID

4595.

KEGG

hsa:4595.

UCSC

uc001cnf.3. human.
uc001cng.3. human.
uc001cnn.3. human.

Organism-specific databases

CTD

4595.

GeneCards

GC01M045794.

HGNC

HGNC:7527. MUTYH.

HPA

HPA008732.

MIM

604933. gene.
608456. phenotype.
613659. phenotype.

neXtProt

NX_Q9UIF7.

Orphanet

733. Familial adenomatous polyposis.
26106. Familial gastric cancer.
247798. MUTYH-related attenuated familial adenomatous polyposis.

PharmGKB

PA31328.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1194.

HOVERGEN

HBG052540.

InParanoid

Q9UIF7.

KO

K03575.

OrthoDB

EOG4HX50Q.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q9UIF7.

Bgee

Q9UIF7.

CleanEx

HS_MUTYH.

Genevestigator

Q9UIF7.

GermOnline

ENSG00000132781. Homo sapiens.

Family and domain databases

Gene3D

1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.

InterPro

IPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Pfam

PF00730. HhH-GPD. 1 hit.
[Graphical view]

SMART

SM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]

SUPFAM

SSF48150. DNA_glycsylse. 1 hit.
SSF55811. NUDIX_hydrolase. 1 hit.

PROSITE

PS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UIF7.

GenomeRNAi

4595.

NextBio

17664.

SOURCE

Search...

Entry information

Entry name

MUTYH_HUMAN

Accession

Primary (citable) accession number: Q9UIF7
Secondary accession number(s): D3DPZ4 , Q15830, Q9UBP2, Q9UBS7, Q9UIF4, Q9UIF5, Q9UIF6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.