G/T mismatch-specific thymine DNA glycosylase

<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

<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

• Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine. EC:3.2.2.29

<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

• ATP binding Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.7

    "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-330.
• chloride ion binding Source: CAFAInferred from direct assayⁱ
  • Ref.15

    "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
• damaged DNA binding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions."
    Barrett T.E., Savva R., Panayotou G., Brown T., Barlow T., Jiricny J., Pearl L.H.
    Cell 92:117-129(1998) [PubMed] [Europe PMC] [Abstract]
• DNA binding Source: UniProtKB
• DNA N-glycosylase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites."
    Maiti A., Drohat A.C.
    J. Biol. Chem. 286:35334-35338(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • Ref.18

    "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
• double-stranded DNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
• G/U mismatch-specific uracil-DNA glycosylase activity Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding."
    Smet-Nocca C., Wieruszeski J.M., Chaar V., Leroy A., Benecke A.
    Biochemistry 47:6519-6530(2008) [PubMed] [Europe PMC] [Abstract]
• magnesium ion binding Source: CAFAInferred from direct assayⁱ
  • Ref.15

    "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
• mismatched DNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA."
    Maiti A., Noon M.S., MacKerell A.D. Jr., Pozharski E., Drohat A.C.
    Proc. Natl. Acad. Sci. U.S.A. 109:8091-8096(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, MUTAGENESIS OF ALA-145; HIS-151; ASN-191 AND THR-197.
• protein domain specific binding Source: Ensembl
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
• protein kinase C binding Source: Ensembl
• protein self-association Source: CAFAInferred from direct assayⁱ
  • "The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding."
    Smet-Nocca C., Wieruszeski J.M., Chaar V., Leroy A., Benecke A.
    Biochemistry 47:6519-6530(2008) [PubMed] [Europe PMC] [Abstract]
• pyrimidine-specific mismatch base pair DNA N-glycosylase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA."
    Maiti A., Noon M.S., MacKerell A.D. Jr., Pozharski E., Drohat A.C.
    Proc. Natl. Acad. Sci. U.S.A. 109:8091-8096(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, MUTAGENESIS OF ALA-145; HIS-151; ASN-191 AND THR-197.
  • Ref.1

    "Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase."
    Neddermann P., Gallinari P., Lettieri T., Schmid D., Truong O., Hsuan J.J., Wiebauer K., Jiricny J.
    J. Biol. Chem. 271:12767-12774(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
• sodium ion binding Source: CAFAInferred from direct assayⁱ
  • Ref.15

    "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
• SUMO binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.7

    "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-330.
  • Ref.15

    "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
  • Ref.16

    "Crystal structure of SUMO-3-modified thymine-DNA glycosylase."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    J. Mol. Biol. 359:137-147(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO2, MUTAGENESIS OF GLU-310.
• transcription coregulator activity Source: Ensembl
• transcription factor binding Source: Ensembl
• uracil DNA N-glycosylase activity Source: CAFAInferred from direct assayⁱ
  • Ref.7

    "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-330.

GO - Biological processⁱ

• base-excision repair Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites."
    Maiti A., Drohat A.C.
    J. Biol. Chem. 286:35334-35338(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • Ref.18

    "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
• base-excision repair, AP site formation Source: CAFAInferred from direct assayⁱ
  • Ref.7

    "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-330.
• chromatin organization Source: UniProtKB-KW
• depyrimidination Source: Reactome
• DNA demethylation Source: UniProtKB
• mismatch repair Source: UniProtKBInferred from direct assayⁱ
  • Ref.20

    "Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA."
    Maiti A., Noon M.S., MacKerell A.D. Jr., Pozharski E., Drohat A.C.
    Proc. Natl. Acad. Sci. U.S.A. 109:8091-8096(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, MUTAGENESIS OF ALA-145; HIS-151; ASN-191 AND THR-197.
• negative regulation of chromatin binding Source: Ensembl
• negative regulation of protein binding Source: Ensembl
• negative regulation of transcription by RNA polymerase II Source: Ensembl
• oxidative DNA demethylation Source: Reactome
• regulation of DNA N-glycosylase activity Source: CAFAInferred from mutant phenotypeⁱ
  • "The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding."
    Smet-Nocca C., Wieruszeski J.M., Chaar V., Leroy A., Benecke A.
    Biochemistry 47:6519-6530(2008) [PubMed] [Europe PMC] [Abstract]
• regulation of embryonic development Source: UniProtKB
• regulation of gene expression, epigenetic Source: UniProtKB

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Keywords - Cellular componentⁱ

<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

Mutagenesis

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation databases

<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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

Organism-specific databases

<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">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<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

GO - Molecular functionⁱ

• protein domain specific binding Source: Ensembl
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
• protein kinase C binding Source: Ensembl
• protein self-association Source: CAFAInferred from direct assayⁱ
  • "The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding."
    Smet-Nocca C., Wieruszeski J.M., Chaar V., Leroy A., Benecke A.
    Biochemistry 47:6519-6530(2008) [PubMed] [Europe PMC] [Abstract]
• SUMO binding Source: CAFAInferred from physical interactionⁱ
  • Ref.7

    "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUMOYLATION AT LYS-330.
  • Ref.15

    "Crystal structure of thymine DNA glycosylase conjugated to SUMO-1."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    Nature 435:979-982(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
  • Ref.16

    "Crystal structure of SUMO-3-modified thymine-DNA glycosylase."
    Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
    J. Mol. Biol. 359:137-147(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO2, MUTAGENESIS OF GLU-310.
• transcription factor binding Source: Ensembl

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Phylogenomic databases

Family and domain databases

<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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MEAENAGSYS LQQAQAFYTF PFQQLMAEAP NMAVVNEQQM PEEVPAPAPA 
        60         70         80         90        100
QEPVQEAPKG RKRKPRTTEP KQPVEPKKPV ESKKSGKSAK SKEKQEKITD 
       110        120        130        140        150
TFKVKRKVDR FNGVSEAELL TKTLPDILTF NLDIVIIGIN PGLMAAYKGH 
       160        170        180        190        200
HYPGPGNHFW KCLFMSGLSE VQLNHMDDHT LPGKYGIGFT NMVERTTPGS 
       210        220        230        240        250
KDLSSKEFRE GGRILVQKLQ KYQPRIAVFN GKCIYEIFSK EVFGVKVKNL 
       260        270        280        290        300
EFGLQPHKIP DTETLCYVMP SSSARCAQFP RAQDKVHYYI KLKDLRDQLK 
       310        320        330        340        350
GIERNMDVQE VQYTFDLQLA QEDAKKMAVK EEKYDPGYEA AYGGAYGENP 
       360        370        380        390        400
CSSEPCGFSS NGLIESVELR GESAFSGIPN GQWMTQSFTD QIPSFSNHCG 
       410
TQEQEEESHA                                             

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. Human chromosome 12
   Human chromosome 12: entries, gene names and cross-references to MIM