UniProtKB - Q16769 (QPCT_HUMAN)
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- BLAST>sp|Q16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase OS=Homo sapiens OX=9606 GN=QPCT PE=1 SV=1 MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGT SISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSF SNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLS LKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYG GVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLH L
- Align
Glutaminyl-peptide cyclotransferase
QPCT
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>Select a section on the left to see content.
<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>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions."
Schilling S., Hoffmann T., Manhart S., Hoffmann M., Demuth H.U.
FEBS Lett. 563:191-196(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS GLUTAMYL CYCLASE. - Ref.7"Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S.
J. Mol. Biol. 379:966-980(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.11"Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S.
J. Mol. Biol. 379:966-980(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.8"Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation."
Huang K.-F., Liu Y.-L., Cheng W.-J., Ko T.-P., Wang A.H.-J.
Proc. Natl. Acad. Sci. U.S.A. 102:13117-13122(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-144; PHE-146; GLU-201; TRP-207; ASP-248; GLN-304; ASP-305; PHE-325 AND TRP-329, CHARACTERIZATION OF VARIANT TRP-54. - Ref.9"A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
Huang K.F., Wang Y.R., Chang E.C., Chou T.L., Wang A.H.
Biochem. J. 411:181-190(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319. - Ref.11"Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
Huang K.F., Wang Y.R., Chang E.C., Chou T.L., Wang A.H.
Biochem. J. 411:181-190(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319. - Ref.11"Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
Huang K.F., Wang Y.R., Chang E.C., Chou T.L., Wang A.H.
Biochem. J. 411:181-190(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319. - Ref.11"Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 159 | Zinc; catalytic | 1 | |
| <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 sitei | 201 | Proton acceptor1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 202 | Zinc; catalytic | 1 | |
| <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 sitei | 248 | Proton acceptor1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 bindingi | 330 | Zinc; catalytic | 1 |
<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
- glutaminyl-peptide cyclotransferase activity Source: UniProtKB <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
- zinc ion binding Source: UniProtKB <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
<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 - Biological processi
- cellular protein modification process 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
- neutrophil degranulation Source: Reactome
- peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Source: UniProtKB <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
<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 function | Acyltransferase, Transferase |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS03941-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.2.5 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6798695 Neutrophil degranulation |
Protein family/group databases
MEROPS protease database More...MEROPSi | M28.974 |
<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: Glutaminyl-peptide cyclotransferase (EC:2.3.2.5)Alternative name(s): Glutaminyl cyclase Short name: QC Short name: sQC Glutaminyl-tRNA cyclotransferase Glutamyl cyclase Short name: EC |
| <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:QPCT |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000115828.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:9753 QPCT |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607065 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q16769 |
<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
- Secreted 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S.
J. Mol. Biol. 379:966-980(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Secreted 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: Reactome
Other locations
- ficolin-1-rich granule lumen Source: Reactome
- specific granule lumen Source: Reactome
- tertiary granule lumen Source: Reactome
<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>Keywords - Cellular componenti
Secreted<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 144 | K → A: Lowers activity by approximately 40%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 146 | F → A: Lowers activity by approximately 30%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 160 | S → A: Reduces activity by about 50%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 160 | S → G: Reduces activity by 96%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 201 | E → D: Reduces activity by about 98%. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 201 | E → L or Q: Abolishes activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 207 | W → L: Greatly lowers activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 248 | D → A: Reduces activity by 99%. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 248 | D → Q: Abolishes activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 304 | Q → L: Lowers activity by approximately 35%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 305 | D → A, E or L: Abolishes activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 305 | D → N: Reduces activity by 99%. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 319 | H → L: Reduces activity by 87%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 325 | F → A: Greatly lowers activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 329 | W → A: Abolishes activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 25797 |
Open Targets More...OpenTargetsi | ENSG00000115828 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34095 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4508 |
Drug and drug target database More...DrugBanki | DB04581 1-benzylimidazole DB04636 Glutamine t-butyl ester DB04622 N-ACETYLHISTAMINE |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2411 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | QPCT |
Domain mapping of disease mutations (DMDM) More...DMDMi | 2498824 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
| <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_0000022195 | 29 – 361 | Glutaminyl-peptide cyclotransferaseAdd BLAST | 333 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 49 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 139 ↔ 164 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 296 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<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>Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q16769 |
PeptideAtlas More...PeptideAtlasi | Q16769 |
PRoteomics IDEntifications database More...PRIDEi | Q16769 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 61056 61057 [Q16769-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q16769-2 [Q16769-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q16769 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q16769 |
<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 More...Bgeei | ENSG00000115828 |
CleanEx database of gene expression profiles More...CleanExi | HS_QPCT |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q16769 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q16769 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA008406 |
<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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117329, 19 interactors |
Protein interaction database and analysis system More...IntActi | Q16769, 3 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000344829 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q16769 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 38 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 39 – 42 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 50 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 62 – 68 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 71 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 82 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 98 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 103 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 116 – 128 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 131 – 140 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 149 – 151 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 157 – 160 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 161 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 175 – 179 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 180 – 182 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 191 – 199 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 204 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 209 – 212 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 214 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 226 – 229 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 237 – 240 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 241 – 247 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 252 – 254 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 257 – 259 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 262 – 264 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 265 – 280 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 284 – 286 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 293 – 295 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 308 – 311 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 312 – 314 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 317 – 320 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 327 – 330 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 338 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 341 – 359 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q16769 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q16769 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q16769 |
<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
<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>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3946 Eukaryota ENOG410YIYE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000003107 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000189291 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG009812 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q16769 |
KEGG Orthology (KO) More...KOi | K00683 |
Identification of Orthologs from Complete Genome Data More...OMAi | TMRRWNL |
Database of Orthologous Groups More...OrthoDBi | EOG091G09N2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q16769 |
TreeFam database of animal gene trees More...TreeFami | TF315071 |
Family and domain databases
Conserved Domains Database More...CDDi | cd03880 M28_QC_like, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037457 M28_QC_like IPR007484 Peptidase_M28 |
Pfam protein domain database More...Pfami | View protein in Pfam PF04389 Peptidase_M28, 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 (2)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.
<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <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 basketAdded 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.
10 20 30 40 50
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK NYHQPAILNS
60 70 80 90 100
SALRQIAEGT SISEMWQNDL QPLLIERYPG SPGSYAARQH IMQRIQRLQA
110 120 130 140 150
DWVLEIDTFL SQTPYGYRSF SNIISTLNPT AKRHLVLACH YDSKYFSHWN
160 170 180 190 200
NRVFVGATDS AVPCAMMLEL ARALDKKLLS LKTVSDSKPD LSLQLIFFDG
210 220 230 240 250
EEAFLHWSPQ DSLYGSRHLA AKMASTPHPP GARGTSQLHG MDLLVLLDLI
260 270 280 290 300
GAPNPTFPNF FPNSARWFER LQAIEHELHE LGLLKDHSLE GRYFQNYSYG
310 320 330 340 350
GVIQDDHIPF LRRGVPVLHL IPSPFPEVWH TMDDNEENLD ESTIDNLNKI
360
LQVFVLEYLH L
The sequence of this isoform differs from the canonical sequence as follows:
41-89: Missing.
10 20 30 40 50
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK HIMQRIQRLQ
60 70 80 90 100
ADWVLEIDTF LSQTPYGYRS FSNIISTLNP TAKRHLVLAC HYDSKYFSHW
110 120 130 140 150
NNRVFVGATD SAVPCAMMLE LARALDKKLL SLKTVSDSKP DLSLQLIFFD
160 170 180 190 200
GEEAFLHWSP QDSLYGSRHL AAKMASTPHP PGARGTSQLH GMDLLVLLDL
210 220 230 240 250
IGAPNPTFPN FFPNSARWFE RLQAIEHELH ELGLLKDHSL EGRYFQNYSY
260 270 280 290 300
GGVIQDDHIP FLRRGVPVLH LIPSPFPEVW HTMDDNEENL DESTIDNLNK
310
ILQVFVLEYL HL
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_053956 | 54 | R → W Lowers activity by approximately 30%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_005569 | 71 | Q → R. Corresponds to variant dbSNP:rs895245310Ensembl. | 1 | |
| <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_053957 | 360 | H → P1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_038487 | 41 – 89 | Missing in isoform 2. CuratedAdd BLAST | 49 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1790.1 [Q16769-1] |
Protein sequence database of the Protein Information Resource More...PIRi | I37421 |
NCBI Reference Sequences More...RefSeqi | NP_036545.1, NM_012413.3 [Q16769-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.79033 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 25797 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:25797 |
UCSC genome browser More...UCSCi | uc002rqg.4 human [Q16769-1] |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q16769 | Glutaminyl-peptide cyclotransferase | 361 | |||
| UPI000059CF34 | 329 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q16769 | Glutaminyl-peptide cyclotransferase | 361 | |||
| UPI000059CF34 | 329 | ||||
| UPI0006438292 | 402 | ||||
| UPI000C2A5729 | 361 | ||||
| UPI0002147325 | 330 | ||||
| +12 | |||||
| Q16769-2 | Glutaminyl-peptide cyclotransferase (Fragment) | 284 | |||
| UPI0005F36E7B | 312 | ||||
| UPI00062A9487 | 312 | ||||
| QPCT isoform 4 (Fragment) | 284 | ||||
| QPCT isoform 2 (Fragment) | 284 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q16769 | Glutaminyl-peptide cyclotransferase | 361 | |||
| UPI000059CF34 | 329 | ||||
| UPI0006438292 | 402 | ||||
| UPI000C2A5729 | 361 | ||||
| UPI0003F06487 | 496 | ||||
| +81 | |||||
| Q16769-2 | Glutaminyl-peptide cyclotransferase (Fragment) | 284 | |||
| UPI0005F36E7B | 312 | ||||
| UPI00062A9487 | 312 | ||||
| QPCT isoform 4 (Fragment) | 284 | ||||
| QPCT isoform 2 (Fragment) | 284 | ||||
| +4 | |||||
<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
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1790.1 [Q16769-1] |
Protein sequence database of the Protein Information Resource More...PIRi | I37421 |
NCBI Reference Sequences More...RefSeqi | NP_036545.1, NM_012413.3 [Q16769-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.79033 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1MOI | model | - | A | 1-361 | [»] | |
| 2AFM | X-ray | 1.66 | A/B | 33-361 | [»] | |
| 2AFO | X-ray | 2.35 | A/B | 33-361 | [»] | |
| 2AFS | X-ray | 2.22 | A/B | 33-361 | [»] | |
| 2AFU | X-ray | 2.22 | A/B | 33-361 | [»] | |
| 2AFW | X-ray | 1.56 | A/B | 33-361 | [»] | |
| 2AFX | X-ray | 1.64 | A/B | 33-361 | [»] | |
| 2AFZ | X-ray | 1.68 | A/B | 33-361 | [»] | |
| 2ZED | X-ray | 1.70 | A/B | 33-361 | [»] | |
| 2ZEE | X-ray | 1.99 | A/B | 33-361 | [»] | |
| 2ZEF | X-ray | 1.67 | A/B | 33-361 | [»] | |
| 2ZEG | X-ray | 2.08 | A/B | 33-361 | [»] | |
| 2ZEH | X-ray | 1.80 | A/B | 33-361 | [»] | |
| 2ZEL | X-ray | 1.97 | A/B | 33-361 | [»] | |
| 2ZEM | X-ray | 2.18 | A/B | 33-361 | [»] | |
| 2ZEN | X-ray | 1.78 | A/B | 33-361 | [»] | |
| 2ZEO | X-ray | 1.66 | A/B | 33-361 | [»] | |
| 2ZEP | X-ray | 2.10 | A/B | 33-361 | [»] | |
| 3PBB | X-ray | 1.95 | A/B | 33-361 | [»] | |
| 3PBE | X-ray | 1.95 | A/B | 33-361 | [»] | |
| 3SI0 | X-ray | 2.10 | A | 38-361 | [»] | |
| 4YU9 | X-ray | 2.10 | A/B/C | 33-361 | [»] | |
| 4YWY | X-ray | 1.95 | A/B/C | 1-361 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q16769 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q16769 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117329, 19 interactors |
Protein interaction database and analysis system More...IntActi | Q16769, 3 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000344829 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q16769 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4508 |
Drug and drug target database More...DrugBanki | DB04581 1-benzylimidazole DB04636 Glutamine t-butyl ester DB04622 N-ACETYLHISTAMINE |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2411 |
Protein family/group databases
MEROPS protease database More...MEROPSi | M28.974 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q16769 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q16769 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | QPCT |
Domain mapping of disease mutations (DMDM) More...DMDMi | 2498824 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q16769 |
PeptideAtlas More...PeptideAtlasi | Q16769 |
PRoteomics IDEntifications database More...PRIDEi | Q16769 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 61056 61057 [Q16769-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q16769-2 [Q16769-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 25797 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 25797 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:25797 |
UCSC genome browser More...UCSCi | uc002rqg.4 human [Q16769-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 25797 |
DisGeNET More...DisGeNETi | 25797 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000115828.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | QPCT |
Human Gene Nomenclature Database More...HGNCi | HGNC:9753 QPCT |
Human Protein Atlas More...HPAi | HPA008406 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607065 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q16769 |
Open Targets More...OpenTargetsi | ENSG00000115828 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34095 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3946 Eukaryota ENOG410YIYE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000003107 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000189291 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG009812 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q16769 |
KEGG Orthology (KO) More...KOi | K00683 |
Identification of Orthologs from Complete Genome Data More...OMAi | TMRRWNL |
Database of Orthologous Groups More...OrthoDBi | EOG091G09N2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q16769 |
TreeFam database of animal gene trees More...TreeFami | TF315071 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS03941-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.2.5 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6798695 Neutrophil degranulation |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | QPCT human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q16769 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | QPCT |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 25797 |
Protein Ontology More...PROi | PR:Q16769 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000115828 |
CleanEx database of gene expression profiles More...CleanExi | HS_QPCT |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q16769 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q16769 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd03880 M28_QC_like, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037457 M28_QC_like IPR007484 Peptidase_M28 |
Pfam protein domain database More...Pfami | View protein in Pfam PF04389 Peptidase_M28, 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 namei | QPCT_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>Accessioni | Q16769Primary (citable) accession number: Q16769 Secondary accession number(s): Q16770, Q3KRG6, Q53TR4 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1997 | |
| Last modified: | June 20, 2018 | |
| This is version 150 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
