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Protein

Adenine DNA glycosylase

Gene

MUTYH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei131Proton donor/acceptorBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei233Transition state stabilizerBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi287Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi294Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi297Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi303Iron-sulfur (4Fe-4S)By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Source: GO_Central
  • adenine/guanine mispair binding Source: GO_Central
  • DNA N-glycosylase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • MutSalpha complex binding Source: HGNC
  • oxidized purine DNA binding Source: GO_Central
  • purine-specific mismatch base pair DNA N-glycosylase activity Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processDNA damage, DNA repair
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-110330 Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331 Cleavage of the damaged purine
R-HSA-110357 Displacement of DNA glycosylase by APEX1
R-HSA-9608287 Defective MUTYH substrate binding
R-HSA-9608290 Defective MUTYH substrate processing

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9UIF7

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Adenine DNA glycosylase (EC:3.2.2.311 Publication)
Alternative name(s):
MutY homolog
Short name:
hMYH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MUTYH
Synonyms:MYH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000132781.17

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7527 MUTYH

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604933 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UIF7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Familial adenomatous polyposis 2 (FAP2)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by the development of multiple colorectal adenomatous polyps, benign neoplasms derived from glandular epithelium. Some affected individuals may develop colorectal carcinoma.
See also OMIM:608456
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07764018P → L in FAP2; also found in multiple polyposis, colorectal and lung cancer cases; unknown pathological significance; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs79777494EnsemblClinVar.1
Natural variantiVAR_026045125Y → H in FAP2; decreased function in DNA repair. 2 Publications1
Natural variantiVAR_026046128W → R in FAP2; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs730881832Ensembl.1
Natural variantiVAR_064938148G → GIW in FAP2; reduced DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair. 3 Publications1
Natural variantiVAR_077646154P → L in FAP2; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs777184451Ensembl.1
Natural variantiVAR_018873176Y → C in FAP2; loss of DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair. 12 PublicationsCorresponds to variant dbSNP:rs34612342Ensembl.1
Natural variantiVAR_077647177Y → S in FAP2. 1 Publication1
Natural variantiVAR_064939179R → C in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs747993448Ensembl.1
Natural variantiVAR_026047179R → H in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs143353451Ensembl.1
Natural variantiVAR_077648182R → Q in FAP2; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs533899702Ensembl.1
Natural variantiVAR_064940182R → W in FAP2; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs750592289Ensembl.1
Natural variantiVAR_077649186G → E in FAP2; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs754155145Ensembl.1
Natural variantiVAR_077650213G → E in FAP2. 1 PublicationCorresponds to variant dbSNP:rs768553551Ensembl.1
Natural variantiVAR_077651220I → V in FAP2; also found in multiple polyposis case; unknown pathological significance; reduced DNA glycosylase activity; no effect on function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs200872702Ensembl.1
Natural variantiVAR_077654235N → S in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs1057517765Ensembl.1
Natural variantiVAR_026048238R → W in FAP2; also found in a case of sporadic colorectal cancer; unknown pathological significance; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs34126013Ensembl.1
Natural variantiVAR_077656242R → H in FAP2; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs140342925Ensembl.1
Natural variantiVAR_077659271R → W in FAP2; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs769237459Ensembl.1
Natural variantiVAR_077660280M → V in FAP2; reduced DNA glycosylase activity. 2 PublicationsCorresponds to variant dbSNP:rs876659676Ensembl.1
Natural variantiVAR_077661283G → E in FAP2; also found in a patient with multiple polyps; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs730881833Ensembl.1
Natural variantiVAR_077663292P → L in FAP2; also found in multiple polyposis cases; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs374950566Ensembl.1
Natural variantiVAR_077664306R → C in FAP2; also found in multiple polyposis cases; unknown pathological significance; does not affect DNA glycosylase activity; slightly decreased function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs138089183Ensembl.1
Natural variantiVAR_077667377P → T in FAP2; decreased function in DNA repair. 1 Publication1
Natural variantiVAR_077668385L → P in FAP2; also found in multiple polyposis cases; loss of DNA glycosylase activity; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs1060501335Ensembl.1
Natural variantiVAR_018875393G → D in FAP2; reduced DNA glycosylase activity; decreased DNA binding; decreased function in DNA repair. 12 PublicationsCorresponds to variant dbSNP:rs36053993Ensembl.1
Natural variantiVAR_077669402P → L in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of DNA glycosylase activity; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs529008617Ensembl.1
Natural variantiVAR_077670417L → M in FAP2; also found in patient with multiple polyps and in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs144079536Ensembl.1
Natural variantiVAR_077671423R → C in FAP2; unknown pathological significance; does not affect function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs150792276Ensembl.1
Natural variantiVAR_077674470A → D in FAP2; loss of function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs200844166Ensembl.1
Natural variantiVAR_077676474T → M in FAP2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs767747402Ensembl.1
Natural variantiVAR_064941477Missing in FAP2; also found in a case of sporadic colorectal cancer; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair. 6 Publications1
Natural variantiVAR_077677486A → T in FAP2; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587782263Ensembl.1
Natural variantiVAR_077678490V → F in FAP2; found also in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs587782228Ensembl.1
Gastric cancer (GASC)2 Publications
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
Disease descriptionA 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.
See also OMIM:613659
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026049402P → S in GASC; sporadic; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs121908382Ensembl.1
Natural variantiVAR_026050411Q → R in GASC; sporadic; unknown pathological significance; does not affect function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs121908383Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi233D → N: Loss of DNA glycosylase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
4595

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
MUTYH

MalaCards human disease database

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MalaCardsi
MUTYH
MIMi608456 phenotype
613659 phenotype

Open Targets

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OpenTargetsi
ENSG00000132781

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
247798 MUTYH-related attenuated familial adenomatous polyposis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA31328

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MUTYH

Domain mapping of disease mutations (DMDM)

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DMDMi
48428272

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001022391 – 546Adenine DNA glycosylaseAdd BLAST546

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9UIF7

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9UIF7

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9UIF7

PeptideAtlas

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PeptideAtlasi
Q9UIF7

PRoteomics IDEntifications database

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PRIDEi
Q9UIF7

ProteomicsDB human proteome resource

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ProteomicsDBi
84500
84501 [Q9UIF7-2]
84502 [Q9UIF7-3]
84503 [Q9UIF7-4]
84504 [Q9UIF7-5]
84505 [Q9UIF7-6]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9UIF7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9UIF7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000132781 Expressed in 212 organ(s), highest expression level in right hemisphere of cerebellum

CleanEx database of gene expression profiles

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CleanExi
HS_MUTYH

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9UIF7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UIF7 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA008732

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-10321956,EBI-741181

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110681, 11 interactors

Database of interacting proteins

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DIPi
DIP-41972N

Protein interaction database and analysis system

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IntActi
Q9UIF7, 15 interactors

Molecular INTeraction database

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MINTi
Q9UIF7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000361170

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X51NMR-A356-497[»]
3N5NX-ray2.30X/Y76-362[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9UIF7

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9UIF7

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9UIF7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini364 – 495Nudix hydrolasePROSITE-ProRule annotationAdd BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi404 – 426Nudix boxAdd BLAST23

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Nth/MutY family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2457 Eukaryota
COG1194 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000047220

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052540

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UIF7

KEGG Orthology (KO)

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KOi
K03575

Database of Orthologous Groups

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OrthoDBi
616758at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UIF7

TreeFam database of animal gene trees

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TreeFami
TF328549

Family and domain databases

Conserved Domains Database

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CDDi
cd03431 DNA_Glycosylase_C, 1 hit
cd00056 ENDO3c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1670.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003651 Endonuclease3_FeS-loop_motif
IPR004035 Endouclease-III_FeS-bd_BS
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR029119 MutY_C
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
PF14815 NUDIX_4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00478 ENDO3c, 1 hit
SM00525 FES, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48150 SSF48150, 1 hit
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00764 ENDONUCLEASE_III_1, 1 hit
PS01155 ENDONUCLEASE_III_2, 1 hit
PS51462 NUDIX, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 16 potential isoforms that are computationally mapped.Show allAlign All

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.

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        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 16 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5KP25E5KP25_HUMAN
A/G-specific adenine DNA glycosylas...
MUTYH
549Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PM53E9PM53_HUMAN
Adenine DNA glycosylase
MUTYH
535Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5T418Q5T418_HUMAN
Adenine DNA glycosylase
MUTYH
215Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5T413Q5T413_HUMAN
Adenine DNA glycosylase
MUTYH
291Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YCY5H0YCY5_HUMAN
Adenine DNA glycosylase
MUTYH
213Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YEI2H0YEI2_HUMAN
Adenine DNA glycosylase
MUTYH
184Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PNY0E9PNY0_HUMAN
Adenine DNA glycosylase
MUTYH
216Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PMH1E9PMH1_HUMAN
Adenine DNA glycosylase
MUTYH
185Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PP34E9PP34_HUMAN
Adenine DNA glycosylase
MUTYH
94Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PLT4E9PLT4_HUMAN
Adenine DNA glycosylase
MUTYH
62Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07764018P → L in FAP2; also found in multiple polyposis, colorectal and lung cancer cases; unknown pathological significance; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs79777494EnsemblClinVar.1
Natural variantiVAR_01887222V → M Polymorphism; does not affect function in DNA repair. 6 PublicationsCorresponds to variant dbSNP:rs3219484EnsemblClinVar.1
Natural variantiVAR_07764125G → D Polymorphism; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs75321043EnsemblClinVar.1
Natural variantiVAR_07764272V → E Polymorphism; does not affect DNA glycosylase activity. 1 Publication1
Natural variantiVAR_077643100W → R Found in sporadic hepatocellular carcinoma; unknown pathological significance; loss of function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs1140507Ensembl.1
Natural variantiVAR_077644102D → N Found in multiple polyposis and sporadic colorectal cancer cases; unknown pathological significance; does not affect DNA glycosylase activity; does not affect function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs587780746Ensembl.1
Natural variantiVAR_077645121D → G Polymorphism; does not affect DNA glycosylase activity; does not affect function in DNA repair. 1 Publication1
Natural variantiVAR_026045125Y → H in FAP2; decreased function in DNA repair. 2 Publications1
Natural variantiVAR_026046128W → R in FAP2; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs730881832Ensembl.1
Natural variantiVAR_064938148G → GIW in FAP2; reduced DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair. 3 Publications1
Natural variantiVAR_077646154P → L in FAP2; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs777184451Ensembl.1
Natural variantiVAR_018873176Y → C in FAP2; loss of DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair. 12 PublicationsCorresponds to variant dbSNP:rs34612342Ensembl.1
Natural variantiVAR_077647177Y → S in FAP2. 1 Publication1
Natural variantiVAR_064939179R → C in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs747993448Ensembl.1
Natural variantiVAR_026047179R → H in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs143353451Ensembl.1
Natural variantiVAR_077648182R → Q in FAP2; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs533899702Ensembl.1
Natural variantiVAR_064940182R → W in FAP2; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs750592289Ensembl.1
Natural variantiVAR_077649186G → E in FAP2; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs754155145Ensembl.1
Natural variantiVAR_077650213G → E in FAP2. 1 PublicationCorresponds to variant dbSNP:rs768553551Ensembl.1
Natural variantiVAR_077651220I → V in FAP2; also found in multiple polyposis case; unknown pathological significance; reduced DNA glycosylase activity; no effect on function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs200872702Ensembl.1
Natural variantiVAR_077652224A → V Functional polymorphism; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs11545695Ensembl.1
Natural variantiVAR_077653231V → M Probable disease-associated mutation found in a case of familial colorectal cancer; no significant effect on DNA glycosylase activity; slightly decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs200165598Ensembl.1
Natural variantiVAR_077654235N → S in FAP2; loss of DNA glycosylase activity; loss of function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs1057517765Ensembl.1
Natural variantiVAR_026048238R → W in FAP2; also found in a case of sporadic colorectal cancer; unknown pathological significance; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs34126013Ensembl.1
Natural variantiVAR_077655242R → C Probable disease-associated mutation found in multiple polyposis cases; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs200495564Ensembl.1
Natural variantiVAR_077656242R → H in FAP2; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs140342925Ensembl.1
Natural variantiVAR_077657243V → F Polymorphism; does not affect function. 1 PublicationCorresponds to variant dbSNP:rs587780749Ensembl.1
Natural variantiVAR_077658244R → G Functional polymorphism; reduced DNA glycosylase activity; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587782885Ensembl.1
Natural variantiVAR_077659271R → W in FAP2; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs769237459Ensembl.1
Natural variantiVAR_077660280M → V in FAP2; reduced DNA glycosylase activity. 2 PublicationsCorresponds to variant dbSNP:rs876659676Ensembl.1
Natural variantiVAR_077661283G → E in FAP2; also found in a patient with multiple polyps; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs730881833Ensembl.1
Natural variantiVAR_077662287C → W Found in a case of sporadic lung cancer; unknown pathological significance; loss of function in DNA repair. 1 Publication1
Natural variantiVAR_077663292P → L in FAP2; also found in multiple polyposis cases; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs374950566Ensembl.1
Natural variantiVAR_077664306R → C in FAP2; also found in multiple polyposis cases; unknown pathological significance; does not affect DNA glycosylase activity; slightly decreased function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs138089183Ensembl.1
Natural variantiVAR_077665319S → N Polymorphism; does not affect DNA glycosylase activity; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587781810Ensembl.1
Natural variantiVAR_018874335Q → H Polymorphism; does not affect function in DNA repair. 6 PublicationsCorresponds to variant dbSNP:rs3219489Ensembl.1
Natural variantiVAR_077666335Q → R Found in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs199742231Ensembl.1
Natural variantiVAR_048262370A → V Polymorphism; does not affect DNA glycosylase activity. 1 PublicationCorresponds to variant dbSNP:rs35352891Ensembl.1
Natural variantiVAR_077667377P → T in FAP2; decreased function in DNA repair. 1 Publication1
Natural variantiVAR_077668385L → P in FAP2; also found in multiple polyposis cases; loss of DNA glycosylase activity; loss of function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs1060501335Ensembl.1
Natural variantiVAR_018875393G → D in FAP2; reduced DNA glycosylase activity; decreased DNA binding; decreased function in DNA repair. 12 PublicationsCorresponds to variant dbSNP:rs36053993Ensembl.1
Natural variantiVAR_077669402P → L in FAP2; also found in multiple polyposis and colorectal cancer cases; loss of DNA glycosylase activity; loss of function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs529008617Ensembl.1
Natural variantiVAR_026049402P → S in GASC; sporadic; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs121908382Ensembl.1
Natural variantiVAR_026050411Q → R in GASC; sporadic; unknown pathological significance; does not affect function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs121908383Ensembl.1
Natural variantiVAR_077670417L → M in FAP2; also found in patient with multiple polyps and in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs144079536Ensembl.1
Natural variantiVAR_077671423R → C in FAP2; unknown pathological significance; does not affect function in DNA repair. 3 PublicationsCorresponds to variant dbSNP:rs150792276Ensembl.1
Natural variantiVAR_077672434R → P Found in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair. 1 Publication1
Natural variantiVAR_077673434R → Q Polymorphism; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587782120Ensembl.1
Natural variantiVAR_077674470A → D in FAP2; loss of function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs200844166Ensembl.1
Natural variantiVAR_077675470A → T Found in patient with multiple polyposis; unknown pathological significance; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs192816572Ensembl.1
Natural variantiVAR_077676474T → M in FAP2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs767747402Ensembl.1
Natural variantiVAR_064941477Missing in FAP2; also found in a case of sporadic colorectal cancer; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair. 6 Publications1
Natural variantiVAR_077677486A → T in FAP2; decreased function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587782263Ensembl.1
Natural variantiVAR_077678490V → F in FAP2; found also in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs587782228Ensembl.1
Natural variantiVAR_018876500G → E Functional polymorphism; decreased function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs3219494Ensembl.1
Natural variantiVAR_026051512S → F Polymorphism; does not affect DNA glycosylase activity; does not affect function in DNA repair. 4 PublicationsCorresponds to variant dbSNP:rs140118273Ensembl.1
Natural variantiVAR_077679513P → L Polymorphism; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs587778542Ensembl.1
Natural variantiVAR_077680520R → H Polymorphism; does not affect DNA glycosylase activity; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs374655042Ensembl.1
Natural variantiVAR_018877526L → M Polymorphism; does not affect function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs3219496Ensembl.1
Natural variantiVAR_018878531R → Q Polymorphism; does not affect function in DNA repair. 2 PublicationsCorresponds to variant dbSNP:rs3219497Ensembl.1
Natural variantiVAR_077681536T → A Polymorphism; does not affect DNA glycosylase activity; does not affect function in DNA repair. 1 PublicationCorresponds to variant dbSNP:rs151196169Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0105481 – 14Missing in isoform Beta-1, isoform Gamma-2 and isoform Gamma-3. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_01055053 – 63Missing in isoform Alpha-3 and isoform Gamma-3. 2 PublicationsAdd BLAST11
Alternative sequenceiVSP_01054953 – 62Missing in isoform Alpha-2 and isoform Gamma-2. 1 Publication10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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 No translation available.
CH471059 Genomic DNA Translation: EAX06993.1
CH471059 Genomic DNA Translation: EAX06996.1
CH471059 Genomic DNA Translation: EAX06997.1
BC003178 mRNA Translation: AAH03178.1

The Consensus CDS (CCDS) project

More...
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]

NCBI Reference Sequences

More...
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_011539806.1, XM_011541504.2 [Q9UIF7-4]
XP_016856823.1, XM_017001334.1 [Q9UIF7-5]
XP_016856824.1, XM_017001335.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.271353

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
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]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4595

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4595

UCSC genome browser

More...
UCSCi
uc001cnf.4 human [Q9UIF7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
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_011539806.1, XM_011541504.2 [Q9UIF7-4]
XP_016856823.1, XM_017001334.1 [Q9UIF7-5]
XP_016856824.1, XM_017001335.1
UniGeneiHs.271353

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X51NMR-A356-497[»]
3N5NX-ray2.30X/Y76-362[»]
ProteinModelPortaliQ9UIF7
SMRiQ9UIF7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110681, 11 interactors
DIPiDIP-41972N
IntActiQ9UIF7, 15 interactors
MINTiQ9UIF7
STRINGi9606.ENSP00000361170

PTM databases

iPTMnetiQ9UIF7
PhosphoSitePlusiQ9UIF7

Polymorphism and mutation databases

BioMutaiMUTYH
DMDMi48428272

Proteomic databases

EPDiQ9UIF7
jPOSTiQ9UIF7
PaxDbiQ9UIF7
PeptideAtlasiQ9UIF7
PRIDEiQ9UIF7
ProteomicsDBi84500
84501 [Q9UIF7-2]
84502 [Q9UIF7-3]
84503 [Q9UIF7-4]
84504 [Q9UIF7-5]
84505 [Q9UIF7-6]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4 human [Q9UIF7-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4595
DisGeNETi4595
EuPathDBiHostDB:ENSG00000132781.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MUTYH
GeneReviewsiMUTYH
HGNCiHGNC:7527 MUTYH
HPAiHPA008732
MalaCardsiMUTYH
MIMi604933 gene
608456 phenotype
613659 phenotype
neXtProtiNX_Q9UIF7
OpenTargetsiENSG00000132781
Orphaneti247798 MUTYH-related attenuated familial adenomatous polyposis
PharmGKBiPA31328

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2457 Eukaryota
COG1194 LUCA
GeneTreeiENSGT00510000047220
HOVERGENiHBG052540
InParanoidiQ9UIF7
KOiK03575
OrthoDBi616758at2759
PhylomeDBiQ9UIF7
TreeFamiTF328549

Enzyme and pathway databases

ReactomeiR-HSA-110330 Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331 Cleavage of the damaged purine
R-HSA-110357 Displacement of DNA glycosylase by APEX1
R-HSA-9608287 Defective MUTYH substrate binding
R-HSA-9608290 Defective MUTYH substrate processing
SIGNORiQ9UIF7

Miscellaneous databases

EvolutionaryTraceiQ9UIF7

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MUTYH

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4595

Protein Ontology

More...
PROi
PR:Q9UIF7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000132781 Expressed in 212 organ(s), highest expression level in right hemisphere of cerebellum
CleanExiHS_MUTYH
ExpressionAtlasiQ9UIF7 baseline and differential
GenevisibleiQ9UIF7 HS

Family and domain databases

CDDicd03431 DNA_Glycosylase_C, 1 hit
cd00056 ENDO3c, 1 hit
Gene3Di1.10.1670.10, 1 hit
InterProiView protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003651 Endonuclease3_FeS-loop_motif
IPR004035 Endouclease-III_FeS-bd_BS
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR029119 MutY_C
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
PF14815 NUDIX_4, 1 hit
SMARTiView protein in SMART
SM00478 ENDO3c, 1 hit
SM00525 FES, 1 hit
SUPFAMiSSF48150 SSF48150, 1 hit
SSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS00764 ENDONUCLEASE_III_1, 1 hit
PS01155 ENDONUCLEASE_III_2, 1 hit
PS51462 NUDIX, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMUTYH_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UIF7
Secondary accession number(s): D3DPZ4
, Q15830, Q9UBP2, Q9UBS7, Q9UIF4, Q9UIF5, Q9UIF6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 1, 2000
Last modified: January 16, 2019
This is version 179 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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