UniProtKB - P24158 (PRTN3_HUMAN)
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- BLAST>sp|P24158|PRTN3_HUMAN Myeloblastin OS=Homo sapiens OX=9606 GN=PRTN3 PE=1 SV=3 MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTL IHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVL LIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTF FCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYV DWIRSTLRRVEAKGRP
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Myeloblastin
PRTN3
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<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.12"Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract] - Ref.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.28"Neutrophil proteinase 3 acts on protease-activated receptor-2 to enhance vascular endothelial cell barrier function."
Kuckleburg C.J., Newman P.J.
Arterioscler. Thromb. Vasc. Biol. 33:275-284(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.12"Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract] - Ref.18"Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.28"Neutrophil proteinase 3 acts on protease-activated receptor-2 to enhance vascular endothelial cell barrier function."
Kuckleburg C.J., Newman P.J.
Arterioscler. Thromb. Vasc. Biol. 33:275-284(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei
<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.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 | 71 | Charge relay systemPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | 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 | 118 | Charge relay systemPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | 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 | 203 | Charge relay systemPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi | 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
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- serine-type endopeptidase 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
- serine-type peptidase activity 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
<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
- antimicrobial humoral response Source: Reactome
- blood coagulation Source: Reactome
- cell-cell junction maintenance Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- collagen catabolic process Source: UniProtKB-KW
- cytokine-mediated signaling pathway Source: Reactome
- mature conventional dendritic cell differentiation 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
- membrane protein ectodomain proteolysis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of phagocytosis 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
- neutrophil degranulation Source: Reactome
- neutrophil extravasation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cell proliferation 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
- positive regulation of GTPase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- proteolysis 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 | Hydrolase, Protease, Serine protease |
| Biological process | Collagen degradation |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.21.76. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-140875. Common Pathway of Fibrin Clot Formation. R-HSA-449836. Other interleukin signaling. R-HSA-6798695. Neutrophil degranulation. R-HSA-6803157. Antimicrobial peptides. |
Protein family/group databases
MEROPS protease database More...MEROPSi | S01.134. |
<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: Myeloblastin (EC:3.4.21.766 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
Alternative name(s): AGP7 C-ANCA antigen Leukocyte proteinase 3 Short name: PR-3 Short name: PR3 Neutrophil proteinase 4 Short name: NP-4 P29 Wegener autoantigen |
| <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:PRTN3 Synonyms:MBN |
| <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 <span class="caps">NCBI</span> 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:ENSG00000196415.9. |
Human Gene Nomenclature Database More...HGNCi | HGNC:9495. PRTN3. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 177020. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P24158. |
<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 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
- Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Secreted 2 Publications
Plasma membrane
- Cell membrane 4 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
- Ref.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Cell membrane 4 Publications
Other locations
- Cytoplasmic granule 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
- Ref.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.12"Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract] - Ref.18"Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
- Membrane raft 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.26"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA neutrophil activation."
Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F., Kettritz R.
J. Biol. Chem. 286:7070-7081(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.26"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA neutrophil activation."
Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F., Kettritz R.
J. Biol. Chem. 286:7070-7081(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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.26"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA neutrophil activation."
Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F., Kettritz R.
J. Biol. Chem. 286:7070-7081(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Note: Localizes predominantly to azurophil granules (primary secretory granules) in neutrophils (PubMed:2033050, PubMed:3198760, PubMed:7897245, PubMed:18462208). Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration (PubMed:22266279, PubMed:28240246). Following secretion tethered to the cell membrane by CD177 (PubMed:18462208, PubMed:22266279).6 Publications- Cytoplasmic granule 1 Publication
- Ref.12"Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract] - Ref.18"Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<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
Cytosol
- cytosol 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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: Reactome
- extracellular space Source: UniProtKBInferred from high throughput direct assayi
Lysosome
- azurophil granule lumen 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
Plasma Membrane
- plasma membrane 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
- plasma membrane raft 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>Keywords - Cellular componenti
Cell membrane, Membrane, 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
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim"><span class="caps">OMIM</span></a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
- Ref.11"Wegener's autoantigen decoded."
Jenne D.E., Tschopp J., Luedemann J., Utecht B., Gross W.L.
Nature 346:520-520(1990) [PubMed] [Europe PMC] [Abstract] - Ref.16"Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase."
Niles J.L., McCluskey R.T., Ahmad M.F., Arnaout M.A.
Blood 74:1888-1893(1989) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-47.
<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.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Organism-specific databases
DisGeNET More...DisGeNETi | 5657. |
MalaCards human disease database More...MalaCardsi | PRTN3. |
Open Targets More...OpenTargetsi | ENSG00000196415. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 900. Granulomatosis with polyangiitis. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33842. |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3900. |
Drug and drug target database More...DrugBanki | DB05161. Elafin. |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2401. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PRTN3. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 6174926. |
<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 – 25 | Add BLAST | 25 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000027707 | 26 – 27 | 2 | ||
| <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_0000027708 | 28 – 248 | Myeloblastin4 Publications <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
| 221 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000027709 | 249 – 256 | 8 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <span class="caps">PTM</span> / 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 | 56 ↔ 72 | 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 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"><span class="caps">PTM</span> / 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 | 129 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <span class="caps">PTM</span> / 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 | 152 ↔ 209 | 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 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"><span class="caps">PTM</span> / 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 | 174 | N-linked (GlcNAc...) asparagineCombined 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 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 <span class="caps">PTM</span> / 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 | 182 ↔ 188 | 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 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 <span class="caps">PTM</span> / 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 | 199 ↔ 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 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>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, Glycoprotein, ZymogenProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P24158. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P24158. |
PeptideAtlas More...PeptideAtlasi | P24158. |
PRoteomics IDEntifications database More...PRIDEi | P24158. |
<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"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<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.12"Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract] - Ref.18"Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.21"Proteinase 3. A distinct human polymorphonuclear leukocyte proteinase that produces emphysema in hamsters."
Kao R.C., Wehner N.G., Skubitz K.M., Gray B.H., Hoidal J.R.
J. Clin. Invest. 82:1963-1973(1988) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. - Ref.26"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-ANCA neutrophil activation."
Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A., Luft F., Kettritz R.
J. Biol. Chem. 286:7070-7081(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.27"Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils."
Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J.
J. Immunol. 188:2419-2426(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.24"Neutrophil surface presentation of the anti-neutrophil cytoplasmic antibody-antigen proteinase 3 depends on N-terminal processing."
von Vietinghoff S., Eulenberg C., Wellner M., Luft F.C., Kettritz R.
Clin. Exp. Immunol. 152:508-516(2008) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000196415. |
CleanEx database of gene expression profiles More...CleanExi | HS_PRTN3. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P24158. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P24158. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB017558. HPA005938. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>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.23"NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils."
von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cristina Cardoso M., Luft F.C., Kettritz R.
Blood 109:4487-4493(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD177, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.30"Characterization of the CD177 interaction with the ANCA antigen proteinase 3."
Jerke U., Marino S.F., Daumke O., Kettritz R.
Sci. Rep. 7:43328-43328(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD177, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| IL32 | P24001-4 | 3 | EBI-465028,EBI-15570379 | |
| SMAD3 | P84022 | 2 | EBI-465028,EBI-347161 |
<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
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111638. 15 interactors. |
Database of interacting proteins More...DIPi | DIP-31107N. |
Protein interaction database and analysis system More...IntActi | P24158. 4 interactors. |
Molecular INTeraction database More...MINTi | P24158. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000234347. |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P24158. |
<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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 42 – 47 | 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 | 6 | |
| <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 | 56 – 62 | 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 | 65 – 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 | 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 | 70 – 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 | 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 | 74 – 76 | 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 | 78 – 80 | 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 | 81 – 86 | 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 | 6 | |
| <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 – 107 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 112 – 115 | 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 | 120 – 126 | 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 | 151 – 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 | 10 | |
| <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 | 162 – 164 | 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 | 171 – 178 | 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 | 8 | |
| <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 | 186 – 190 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 192 – 195 | 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 | 206 – 209 | 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 | 212 – 219 | 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 | 8 | |
| <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 | 221 – 223 | 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 | 227 – 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 | 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 | 231 – 235 | 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 | 236 – 239 | 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 | 240 – 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 | 8 |
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 |
| 1FUJ | X-ray | 2.20 | A/B/C/D | 28-248 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P24158. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P24158. | |||||
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 | P24158. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 28 – 248 | Peptidase S1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 221 |
<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>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<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 | KOG3627. Eukaryota. COG5640. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144219. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG013304. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P24158. |
KEGG Orthology (KO) More...KOi | K01350. |
Identification of Orthologs from Complete Genome Data More...OMAi | PGSHFCG. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DF7. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P24158. |
TreeFam database of animal gene trees More...TreeFami | TF335284. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00190. Tryp_SPc. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR009003. Peptidase_S1_PA. IPR001314. Peptidase_S1A. IPR001254. Trypsin_dom. IPR018114. TRYPSIN_HIS. IPR033116. TRYPSIN_SER. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00089. Trypsin. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00722. CHYMOTRYPSIN. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00020. Tryp_SPc. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50494. SSF50494. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 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>Sequencei
<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.
10 20 30 40 50
MAHRPPSPAL ASVLLALLLS GAARAAEIVG GHEAQPHSRP YMASLQMRGN
60 70 80 90 100
PGSHFCGGTL IHPSFVLTAA HCLRDIPQRL VNVVLGAHNV RTQEPTQQHF
110 120 130 140 150
SVAQVFLNNY DAENKLNDVL LIQLSSPANL SASVATVQLP QQDQPVPHGT
160 170 180 190 200
QCLAMGWGRV GAHDPPAQVL QELNVTVVTF FCRPHNICTF VPRRKAGICF
210 220 230 240 250
GDSGGPLICD GIIQGIDSFV IWGCATRLFP DFFTRVALYV DWIRSTLRRV
EAKGRP
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 2 | A → R in CAA39203 (PubMed:2258701).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 38 | S → I AA sequence (PubMed:1688612).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 40 | P → PI AA sequence (PubMed:1688612).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 46 | Q → E AA sequence (PubMed:2404977).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 46 | Q → E AA sequence (PubMed:2501794).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 48 | R → A AA sequence (PubMed:2121162).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 64 | S → D AA sequence (PubMed:2033050).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 70 | A → P in AAA59558 (PubMed:1681549).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 255 | Missing in CAA39203 (PubMed:2258701).Curated | 1 |
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_011691 | 119 | V → I7 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011713 | 135 | A → T4 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 ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011714 | 136 | T → S4 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 |
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 | M75154 mRNA. Translation: AAA59558.1. AC004799 Genomic DNA. No translation available. CH471139 Genomic DNA. Translation: EAW69591.1. BC096183 mRNA. Translation: AAH96183.1. BC096184 mRNA. Translation: AAH96184.1. BC096185 mRNA. Translation: AAH96185.1. BC096186 mRNA. Translation: AAH96186.1. M96628 Genomic DNA. Translation: AAB59364.1. AH005293 Genomic DNA. Translation: AAB59493.1. M97911 Genomic DNA. No translation available. AH007523 Genomic DNA. Translation: AAD21524.1. X56606 mRNA. Translation: CAA39943.1. X55668 mRNA. Translation: CAA39203.1. M29142 mRNA. Translation: AAA36342.1. Frameshift. X56132 mRNA. Translation: CAA39597.1. X56132 mRNA. Translation: CAA39598.1. Different initiation. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS32860.1. |
Protein sequence database of the Protein Information Resource More...PIRi | A45080. PRHU3. |
NCBI Reference Sequences More...RefSeqi | NP_002768.3. NM_002777.3. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.928. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000234347; ENSP00000234347; ENSG00000196415. ENST00000612112; ENSP00000478977; ENSG00000277804. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5657. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5657. |
UCSC genome browser More...UCSCi | uc002lqa.2. human. |
<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
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 | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| P24158 | U3KPS2 UPI0005D02339 | Homo sapiens (Human) | 256 | UniRef100_P24158 | Cluster: Myeloblastin | 3 |
| Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| P24158 | U3KPS2 UPI0005D02339 H2NWR5 A0A2J8RA37 G3QER8 H2QES4 A0A2J8IKN8 UPI0004F09EFE A0A2J8IKN3 UPI000011179E +1 | Homo sapiens (Human) Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Gorilla gorilla gorilla (Western lowland gorilla) Pan troglodytes (Chimpanzee) Pan paniscus (Pygmy chimpanzee) (Bonobo) | 256 | UniRef90_P24158 | Cluster: Myeloblastin | 12 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Proteinase 3 entry |
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 | M75154 mRNA. Translation: AAA59558.1. AC004799 Genomic DNA. No translation available. CH471139 Genomic DNA. Translation: EAW69591.1. BC096183 mRNA. Translation: AAH96183.1. BC096184 mRNA. Translation: AAH96184.1. BC096185 mRNA. Translation: AAH96185.1. BC096186 mRNA. Translation: AAH96186.1. M96628 Genomic DNA. Translation: AAB59364.1. AH005293 Genomic DNA. Translation: AAB59493.1. M97911 Genomic DNA. No translation available. AH007523 Genomic DNA. Translation: AAD21524.1. X56606 mRNA. Translation: CAA39943.1. X55668 mRNA. Translation: CAA39203.1. M29142 mRNA. Translation: AAA36342.1. Frameshift. X56132 mRNA. Translation: CAA39597.1. X56132 mRNA. Translation: CAA39598.1. Different initiation. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS32860.1. |
Protein sequence database of the Protein Information Resource More...PIRi | A45080. PRHU3. |
NCBI Reference Sequences More...RefSeqi | NP_002768.3. NM_002777.3. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.928. |
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 |
| 1FUJ | X-ray | 2.20 | A/B/C/D | 28-248 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P24158. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P24158. | |||||
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 | 111638. 15 interactors. |
Database of interacting proteins More...DIPi | DIP-31107N. |
Protein interaction database and analysis system More...IntActi | P24158. 4 interactors. |
Molecular INTeraction database More...MINTi | P24158. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000234347. |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P24158. |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3900. |
Drug and drug target database More...DrugBanki | DB05161. Elafin. |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2401. |
Protein family/group databases
MEROPS protease database More...MEROPSi | S01.134. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PRTN3. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 6174926. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P24158. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P24158. |
PeptideAtlas More...PeptideAtlasi | P24158. |
PRoteomics IDEntifications database More...PRIDEi | P24158. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5657. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000234347; ENSP00000234347; ENSG00000196415. ENST00000612112; ENSP00000478977; ENSG00000277804. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5657. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5657. |
UCSC genome browser More...UCSCi | uc002lqa.2. human. |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5657. |
DisGeNET More...DisGeNETi | 5657. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000196415.9. |
GeneCards: human genes, protein and diseases More...GeneCardsi | PRTN3. |
Human Gene Nomenclature Database More...HGNCi | HGNC:9495. PRTN3. |
Human Protein Atlas More...HPAi | CAB017558. HPA005938. |
MalaCards human disease database More...MalaCardsi | PRTN3. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 177020. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P24158. |
Open Targets More...OpenTargetsi | ENSG00000196415. |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 900. Granulomatosis with polyangiitis. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33842. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3627. Eukaryota. COG5640. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144219. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG013304. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P24158. |
KEGG Orthology (KO) More...KOi | K01350. |
Identification of Orthologs from Complete Genome Data More...OMAi | PGSHFCG. |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DF7. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P24158. |
TreeFam database of animal gene trees More...TreeFami | TF335284. |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.21.76. 2681. |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-140875. Common Pathway of Fibrin Clot Formation. R-HSA-449836. Other interleukin signaling. R-HSA-6798695. Neutrophil degranulation. R-HSA-6803157. Antimicrobial peptides. |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P24158. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Proteinase_3. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5657. |
Protein Ontology More...PROi | PR:P24158. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000196415. |
CleanEx database of gene expression profiles More...CleanExi | HS_PRTN3. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P24158. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P24158. HS. |
Family and domain databases
Conserved Domains Database More...CDDi | cd00190. Tryp_SPc. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR009003. Peptidase_S1_PA. IPR001314. Peptidase_S1A. IPR001254. Trypsin_dom. IPR018114. TRYPSIN_HIS. IPR033116. TRYPSIN_SER. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00089. Trypsin. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00722. CHYMOTRYPSIN. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00020. Tryp_SPc. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50494. SSF50494. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 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 | PRTN3_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 | P24158Primary (citable) accession number: P24158 Secondary accession number(s): P15637 , P18078, Q4VB08, Q4VB09, Q6LBM7, Q6LBN2, Q9UD25, Q9UQD8 | |
| <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: | March 1, 1992 |
| Last sequence update: | December 15, 1998 | |
| Last modified: | March 28, 2018 | |
| This is version 195 of the entry and version 3 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. | |