Probable tRNA(His) guanylyltransferase

<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%5Fsection">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

• 5'-end ribonucleotide-tRNA^His

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  + ATP

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  + GTP

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  + H₂O

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  = a 5'-phospho-guanosine-ribonucleotide-tRNA^His

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  + AMP

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  + 2 diphosphate

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  + H⁺

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
  EC:2.7.7.79
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  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  5'-end ribonucleotide-tRNA^His

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  5'-end ribonucleotide residue

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  zoom

  +

  ATP

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  +

  GTP

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  +

  H₂O

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  =

  a 5'-phospho-guanosine-ribonucleotide-tRNA^His

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  5'-phospho-guanosine-ribonucleotide residue

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  zoom

  +

  AMP

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  +

  2

  diphosphate

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  zoom

  +

  H⁺

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

<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

Sites

Regions

<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: BHF-UCL <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• GTP binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• identical protein binding Source: IntAct <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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
  • "Next-generation sequencing to generate interactome datasets."
    Yu H., Tardivo L., Tam S., Weiner E., Gebreab F., Fan C., Svrzikapa N., Hirozane-Kishikawa T., Rietman E., Yang X., Sahalie J., Salehi-Ashtiani K., Hao T., Cusick M.E., Hill D.E., Roth F.P., Braun P., Vidal M.
    Nat. Methods 8:478-480(2011) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]
• magnesium ion binding Source: BHF-UCLInferred from direct assayⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• nucleotidyltransferase activity Source: ReactomeInferred from experimentⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• tRNA binding Source: BHF-UCL <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%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• tRNA guanylyltransferase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.

GO - Biological processⁱ

• protein homotetramerization Source: UniProtKBInferred from physical interactionⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
• tRNA modification Source: UniProtKB
• tRNA processing Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.

<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

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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

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%5Fsection">'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%5Fsection">'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%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.8

    "tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases."
    Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
    Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 30-298 IN COMPLEX WITH MAGNESIUM; TRIPHOSPHATE AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-58; HIS-63; SER-104; ASP-105; GLU-106; THR-127; HIS-181; LYS-216 AND ASN-227.
  • "Next-generation sequencing to generate interactome datasets."
    Yu H., Tardivo L., Tam S., Weiner E., Gebreab F., Fan C., Svrzikapa N., Hirozane-Kishikawa T., Rietman E., Yang X., Sahalie J., Salehi-Ashtiani K., Hao T., Cusick M.E., Hill D.E., Roth F.P., Braun P., Vidal M.
    Nat. Methods 8:478-480(2011) [PubMed] [Europe PMC] [Abstract]
  • "A proteome-scale map of the human interactome network."
    Rolland T., Tasan M., Charloteaux B., Pevzner S.J., Zhong Q., Sahni N., Yi S., Lemmens I., Fontanillo C., Mosca R., Kamburov A., Ghiassian S.D., Yang X., Ghamsari L., Balcha D., Begg B.E., Braun P., Brehme M.

    , Broly M.P., Carvunis A.R., Convery-Zupan D., Corominas R., Coulombe-Huntington J., Dann E., Dreze M., Dricot A., Fan C., Franzosa E., Gebreab F., Gutierrez B.J., Hardy M.F., Jin M., Kang S., Kiros R., Lin G.N., Luck K., MacWilliams A., Menche J., Murray R.R., Palagi A., Poulin M.M., Rambout X., Rasla J., Reichert P., Romero V., Ruyssinck E., Sahalie J.M., Scholz A., Shah A.A., Sharma A., Shen Y., Spirohn K., Tam S., Tejeda A.O., Trigg S.A., Twizere J.C., Vega K., Walsh J., Cusick M.E., Xia Y., Barabasi A.L., Iakoucheva L.M., Aloy P., De Las Rivas J., Tavernier J., Calderwood M.A., Hill D.E., Hao T., Roth F.P., Vidal M.
    Cell 159:1212-1226(2014) [PubMed] [Europe PMC] [Abstract]

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MWGACKVKVH DSLATISITL RRYLRLGATM AKSKFEYVRD FEADDTCLAH 
        60         70         80         90        100
CWVVVRLDGR NFHRFAEKHN FAKPNDSRAL QLMTKCAQTV MEELEDIVIA 
       110        120        130        140        150
YGQSDEYSFV FKRKTNWFKR RASKFMTHVA SQFASSYVFY WRDYFEDQPL 
       160        170        180        190        200
LYPPGFDGRV VVYPSNQTLK DYLSWRQADC HINNLYNTVF WALIQQSGLT 
       210        220        230        240        250
PVQAQGRLQG TLAADKNEIL FSEFNINYNN ELPMYRKGTV LIWQKVDEVM 
       260        270        280        290 
TKEIKLPTEM EGKKMAVTRT RTKPVPLHCD IIGDAFWKEH PEILDEDS   

<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

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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials 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 5
   Human chromosome 5: entries, gene names and cross-references to MIM