UniProtKB - P27487 (DPP4_HUMAN)
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- BLAST>sp|P27487|DPP4_HUMAN Dipeptidyl peptidase 4 OS=Homo sapiens OX=9606 GN=DPP4 PE=1 SV=2 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
- Align
Dipeptidyl peptidase 4
DPP4
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.12"Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides."
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I.
Eur. J. Biochem. 267:5608-5613(2000) [PubMed] [Europe PMC] [Abstract] - Ref.13"The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26."
Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.
Proteomics 7:2300-2310(2007) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 659-669, FUNCTION, ENZYME REGULATION, INTERACTION WITH GPC3, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.19"Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity."
Abbott C.A., McCaughan G.W., Gorrell M.D.
FEBS Lett. 458:278-284(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF GLU-205 AND GLU-206. - Ref.20"Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts."
Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J., Rettig W.J.
J. Biol. Chem. 274:36505-36512(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.23"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. - Ref.24"Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.29"N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding."
Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E., Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.
Protein Sci. 13:145-154(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ADA, MUTAGENESIS OF ASN-85; ASN-92; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321; ASN-520 AND ASN-685. - Ref.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION. - Ref.33"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION, INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-750. - Ref.34"Lymphatic-specific expression of dipeptidyl peptidase IV and its dual role in lymphatic endothelial function."
Shin J.W., Jurisic G., Detmar M.
Exp. Cell Res. 314:3048-3056(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
Miscellaneous
<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>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 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.20"Fibroblast activation protein, a dual specificity serine protease expressed in reactive human tumor stromal fibroblasts."
Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J., Rettig W.J.
J. Biol. Chem. 274:36505-36512(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
<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.13"The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26."
Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.
Proteomics 7:2300-2310(2007) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 659-669, FUNCTION, ENZYME REGULATION, INTERACTION WITH GPC3, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.34"Lymphatic-specific expression of dipeptidyl peptidase IV and its dual role in lymphatic endothelial function."
Shin J.W., Jurisic G., Detmar M.
Exp. Cell Res. 314:3048-3056(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, 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 | 630 | 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 | 708 | 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 | 740 | 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
- dipeptidyl-peptidase 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protease 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 homodimerization activity 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: ReactomeInferred from experimenti
- serine-type peptidase 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
- signaling 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
- virus receptor activity Source: CACAO <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
- behavioral fear response Source: Ensembl
- cell adhesion Source: UniProtKB-KW
- endothelial cell migration 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
- locomotory exploration behavior Source: Ensembl
- negative regulation of extracellular matrix disassembly 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
- positive regulation of cell proliferation 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
- proteolysis Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- psychomotor behavior Source: Ensembl
- regulation of cell-cell adhesion mediated by integrin 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
- regulation of insulin secretion Source: Reactome
- response to hypoxia 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
- T cell activation 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
- T cell costimulation 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 | Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease |
| Biological process | Cell adhesion |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.14.5 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) R-HSA-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P27487 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P27487 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-DPP4 DPP4N_Peptidase_S9 |
MEROPS protease database More...MEROPSi | S09.003 |
MoonProt database of moonlighting proteins More...MoonProti | P27487 |
<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: Dipeptidyl peptidase 4 (EC:3.4.14.51 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
Alternative name(s): ADABP Adenosine deaminase complexing protein 2 Short name: ADCP-2 Dipeptidyl peptidase IV Short name: DPP IV T-cell activation antigen CD26 TP103 CD_antigen: CD26 Cleaved into the following 2 chains: Alternative name(s): Dipeptidyl peptidase IV membrane form Alternative name(s): Dipeptidyl peptidase IV soluble form |
| <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:DPP4 Synonyms:ADCP2, CD26 |
| <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:ENSG00000197635.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3009 DPP4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 102720 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P27487 |
<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.12"Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides."
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I.
Eur. J. Biochem. 267:5608-5613(2000) [PubMed] [Europe PMC] [Abstract]
Note: Detected in the serum and the seminal fluid.- Secreted 1 Publication
Plasma membrane
- Cell membrane 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.15"Direct association of adenosine deaminase with a T cell activation antigen, CD26."
Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.
Science 261:466-469(1993) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADA, SUBCELLULAR LOCATION.
<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"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. - Ref.24"Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Apical cell membrane 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.25"Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains."
Alfalah M., Jacob R., Naim H.Y.
J. Biol. Chem. 277:10683-10690(2002) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
- invadopodium membrane 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.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION.
- lamellipodium membrane 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.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION.
- Cell membrane 1 Publication
Other locations
- Cell junction 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.24"Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- 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.33"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION, INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-750.
Note: Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids (PubMed:11773049). Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation (PubMed:12676959). Its interaction with CAV1 is necessary for its translocation to membrane rafts (PubMed:17287217). Colocalized with PTPRC in membrane rafts (PubMed:12676959). Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma (PubMed:16651416). Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion (PubMed:11772392). Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (PubMed:10900005).6 Publications- Cell junction 1 Publication
- Ref.23"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. - Ref.24"Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.25"Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains."
Alfalah M., Jacob R., Naim H.Y.
J. Biol. Chem. 277:10683-10690(2002) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION. - Ref.26"A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPRC, INDUCTION, SUBCELLULAR LOCATION. - Ref.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION. - Ref.33"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION, INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-750.
<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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular region Source: Reactome
Lysosome
- lysosomal membrane Source: UniProtKBInferred from high throughput direct assayi
Plasma Membrane
- apical 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
- invadopodium 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
- lamellipodium membrane Source: UniProtKB-SubCell
- 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
Other locations
- cell surface 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
- endocytic vesicle 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
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- integral component of membrane Source: UniProtKB-KW
- intercellular canaliculus Source: Ensembl
- lamellipodium 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 Source: UniProtKBInferred from high throughput direct assayi
- membrane raft Source: UniProtKB-SubCell
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 6 | CytoplasmicSequence analysis | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 7 – 28 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 29 – 766 | ExtracellularSequence analysisAdd BLAST | 738 |
<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 junction, Cell membrane, Cell projection, 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
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 | 85 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 92 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 150 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 205 | E → K: Inhibits dipeptidyl peptidase 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 | 206 | E → L: Inhibits dipeptidyl peptidase 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 | 219 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 229 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 281 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 321 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 520 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 685 | N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 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 | 750 | H → A: Inhibits weakly homodimerization and dipeptidyl peptidase 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 | 750 | H → E: Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 1803 |
Open Targets More...OpenTargetsi | ENSG00000197635 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27467 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL284 |
Drug and drug target database More...DrugBanki | DB07482 (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE DB03253 (2s)-Pyrrolidin-2-Ylmethylamine DB04577 1-(1-phenylcyclopentyl)methylamine DB08024 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE DB07412 1-biphenyl-2-ylmethanamine DB08588 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE DB01884 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One DB08672 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE DB03660 4-Iodo-L-phenylalanine DB07239 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile DB06203 Alogliptin DB01076 Atorvastatin DB04491 Diisopropylphosphono Group DB06127 KRP-104 DB08882 Linagliptin DB06655 Liraglutide DB07779 N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE DB08429 N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide DB05065 PHX1149 DB05001 PSN9301 DB06335 Saxagliptin DB01261 Sitagliptin DB04876 Vildagliptin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1612 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DPP4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1352311 |
<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027213 | 1 – 766 | Dipeptidyl peptidase 4 membrane formAdd BLAST | 766 | |
| <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_0000027214 | 39 – 766 | Dipeptidyl peptidase 4 soluble formAdd BLAST | 728 |
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 | 85 | N-linked (GlcNAc...) asparagine4 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/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 | 92 | N-linked (GlcNAc...) asparagine2 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/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 | 150 | N-linked (GlcNAc...) asparagine4 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/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 | 219 | N-linked (GlcNAc...) asparagine3 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/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 | 229 | N-linked (GlcNAc...) asparagine4 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/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 | 281 | N-linked (GlcNAc...) asparagine3 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/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 | 321 | N-linked (GlcNAc...) asparagine2 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 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 | 328 ↔ 339 | |||
| <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 | 385 ↔ 394 | |||
| <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 | 444 ↔ 447 | |||
| <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 | 454 ↔ 472 | |||
| <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 | 520 | N-linked (GlcNAc...) asparagine4 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 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 | 649 ↔ 762 | |||
| <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 | 685 | N-linked (GlcNAc...) asparagine2 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/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<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"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. - Ref.25"Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains."
Alfalah M., Jacob R., Naim H.Y.
J. Biol. Chem. 277:10683-10690(2002) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION. - Ref.30"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685. - Ref.36"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-92; ASN-150; ASN-520 AND ASN-685. - Ref.41"The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold."
Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H., Sugiyama S., Inaka K., Yamamoto A., Shimizu R.
Biochem. Biophys. Res. Commun. 302:849-854(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, DISULFIDE BONDS. - Ref.42"Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog."
Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.
Nat. Struct. Biol. 10:19-25(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND ASN-520, DISULFIDE BONDS. - Ref.43"Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV."
Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.
Structure 11:947-959(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, DISULFIDE BONDS. - Ref.44"Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors."
Meng W., Brigance R.P., Chao H.J., Fura A., Harrity T., Marcinkeviciene J., O'Connor S.P., Tamura J.K., Xie D., Zhang Y., Klei H.E., Kish K., Weigelt C.A., Turdi H., Wang A., Zahler R., Kirby M.S., Hamann L.G.
J. Med. Chem. 53:5620-5628(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; ASN-92; ASN-150; ASN-219; ASN-229 AND ASN-520.
<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"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
<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
MaxQB - The MaxQuant DataBase More...MaxQBi | P27487 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P27487 |
PeptideAtlas More...PeptideAtlasi | P27487 |
PRoteomics IDEntifications database More...PRIDEi | P27487 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54396 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P27487 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P27487 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<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.11"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon."
Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.
Gastroenterology 101:618-625(1991) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 1-22, TISSUE SPECIFICITY. - Ref.34"Lymphatic-specific expression of dipeptidyl peptidase IV and its dual role in lymphatic endothelial function."
Shin J.W., Jurisic G., Detmar M.
Exp. Cell Res. 314:3048-3056(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION, 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.18"Interleukin-12 enhances CD26 expression and dipeptidyl peptidase IV function on human activated lymphocytes."
Cordero O.J., Salgado F.J., Vinuela J.E., Nogueira M.
Immunobiology 197:522-533(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION. - Ref.22"Mechanisms of CD26/dipeptidyl peptidase IV cytokine-dependent regulation on human activated lymphocytes."
Salgado F.J., Vela E., Martin M., Franco R., Nogueira M., Cordero O.J.
Cytokine 12:1136-1141(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION. - Ref.26"A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPRC, INDUCTION, SUBCELLULAR LOCATION. - Ref.31"Endothelial catabolism of extracellular adenosine during hypoxia: the role of surface adenosine deaminase and CD26."
Eltzschig H.K., Faigle M., Knapp S., Karhausen J., Ibla J., Rosenberger P., Odegard K.C., Laussen P.C., Thompson L.F., Colgan S.P.
Blood 108:1602-1610(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY HYPOXIA. - Ref.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000197635 |
CleanEx database of gene expression profiles More...CleanExi | HS_DPP4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P27487 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P27487 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB045970 |
<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.12"Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides."
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I.
Eur. J. Biochem. 267:5608-5613(2000) [PubMed] [Europe PMC] [Abstract] - Ref.13"The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26."
Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.
Proteomics 7:2300-2310(2007) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 659-669, FUNCTION, ENZYME REGULATION, INTERACTION WITH GPC3, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.15"Direct association of adenosine deaminase with a T cell activation antigen, CD26."
Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.
Science 261:466-469(1993) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADA, SUBCELLULAR LOCATION. - Ref.16"Binding of adenosine deaminase to the lymphocyte surface via CD26."
De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E., Gigase P., Scharpe S.
Eur. J. Immunol. 24:566-570(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADA. - Ref.17"The cysteine-rich region of dipeptidyl peptidase IV (CD 26) is the collagen-binding site."
Loster K., Zeilinger K., Schuppan D., Reutter W.
Biochem. Biophys. Res. Commun. 217:341-348(1995) [PubMed] [Europe PMC] [Abstract]Cited for: ASSOCIATION WITH COLLAGEN. - Ref.23"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH IGF2R, GLYCOSYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION. - Ref.26"A role for interleukin-12 in the regulation of T cell plasma membrane compartmentation."
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R., Cordero O.J., Nogueira M.
J. Biol. Chem. 278:24849-24857(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPRC, INDUCTION, SUBCELLULAR LOCATION. - Ref.27"Cell surface adenosine deaminase binds and stimulates plasminogen activation on 1-LN human prostate cancer cells."
Gonzalez-Gronow M., Hershfield M.S., Arredondo-Vega F.X., Pizzo S.V.
J. Biol. Chem. 279:20993-20998(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ADA. - Ref.28"One site mutation disrupts dimer formation in human DPP-IV proteins."
Chien C.H., Huang L.H., Chou C.Y., Chen Y.S., Han Y.S., Chang G.G., Liang P.H., Chen X.
J. Biol. Chem. 279:52338-52345(2004) [PubMed] [Europe PMC] [Abstract]Cited for: HOMODIMERIZATION, MUTAGENESIS OF HIS-750. - Ref.29"N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding."
Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E., Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.
Protein Sci. 13:145-154(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ADA, MUTAGENESIS OF ASN-85; ASN-92; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321; ASN-520 AND ASN-685. - Ref.32"The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices."
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.
Cancer Res. 66:4652-4661(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, HETERODIMERIZATION, INDUCTION, SUBCELLULAR LOCATION. - Ref.33"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, HOMODIMERIZATION, INTERACTION WITH CARD11 AND CAV1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-750. - Ref.38"Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC."
Raj V.S., Mou H., Smits S.L., Dekkers D.H., Muller M.A., Dijkman R., Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C., Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L.
Nature 495:251-254(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HUMAN CORONAVIRUS-EMC SPIKE PROTEIN. - Ref.40"High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine."
Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R., Dale G.E.
Acta Crystallogr. D 59:1206-1212(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH INHIBITOR, HOMODIMERIZATION. - Ref.41"The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold."
Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H., Sugiyama S., Inaka K., Yamamoto A., Shimizu R.
Biochem. Biophys. Res. Commun. 302:849-854(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, DISULFIDE BONDS. - Ref.42"Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog."
Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N.
Nat. Struct. Biol. 10:19-25(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND ASN-520, DISULFIDE BONDS. - Ref.43"Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV."
Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M.
Structure 11:947-959(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, DISULFIDE BONDS.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 12 | EBI-2871277,EBI-2871277 | ||
| ADA | P56658 | 5 | EBI-2871277,EBI-7475530 | From Bos taurus. |
| CCL11 | P51671 | 2 | EBI-2871277,EBI-727357 | |
| CXCL10 | P02778 | 2 | EBI-2871277,EBI-7815386 | |
| CXCL11 | O14625 | 2 | EBI-2871277,EBI-2871971 | |
| CXCL2 | P19875 | 2 | EBI-2871277,EBI-2114901 | |
| CXCL9 | Q07325 | 2 | EBI-2871277,EBI-3911467 | |
| GCG | P01275 | 4 | EBI-2871277,EBI-7629173 | |
| S | K0BRG7 | 5 | EBI-2871277,EBI-16040613 | From Human betacoronavirus 2c EMC/2012. |
| VIP | P01282 | 2 | EBI-2871277,EBI-751454 |
<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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protease 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 homodimerization activity 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
- signaling 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 | 108137, 8 interactors |
Database of interacting proteins More...DIPi | DIP-351N |
Protein interaction database and analysis system More...IntActi | P27487, 23 interactors |
Molecular INTeraction database More...MINTi | P27487 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353731 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P27487 |
<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 | 40 – 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 | 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 | 45 – 50 | 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 | 60 – 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 | 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 | 64 – 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 | 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 | 75 – 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 | 6 | |
| <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 | 81 – 83 | 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 | 86 – 90 | 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 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 | 92 – 97 | 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 – 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 | 104 – 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 | 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 | 111 – 122 | 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 | 12 | |
| <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 | 124 – 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 | 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 | 128 – 136 | 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 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 | 137 – 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 | 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 | 141 – 143 | 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 | 152 – 157 | 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 | 159 – 162 | 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 | 164 – 168 | 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 | 171 – 177 | 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 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 | 191 – 193 | 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 | 194 – 198 | 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 | 201 – 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 | 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 | 208 – 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 | 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 | 214 – 216 | 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 | 220 – 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 | 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 | 235 – 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 | 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 | 250 – 255 | 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 | 265 – 272 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 273 – 275 | 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 | 278 – 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 | 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 | 284 – 287 | 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 | 291 – 294 | 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 | 298 – 307 | 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 | 310 – 319 | 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 | 322 – 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 | 9 | |
| <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 | 332 – 334 | 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 | 337 – 339 | 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 – 343 | 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 | 345 – 348 | 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 | 350 – 352 | 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 | 354 – 358 | 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 | 362 – 364 | 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 | 368 – 376 | 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 | 378 – 380 | 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 | 382 – 388 | 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 | 391 – 393 | 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 | 395 – 397 | 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 | 400 – 402 | 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 | 404 – 410 | 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 | 412 – 420 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 422 – 424 | 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 | 429 – 435 | 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 | 438 – 446 | 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 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 | 447 – 449 | 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 | 451 – 453 | 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 | 456 – 461 | 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 | 465 – 472 | 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 | 474 – 477 | 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 | 479 – 484 | 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 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 | 485 – 488 | 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 | 489 – 495 | 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 | 498 – 504 | 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 | 506 – 508 | 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 | 511 – 519 | 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 | 522 – 530 | 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 | 536 – 538 | 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 | 540 – 545 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 563 – 569 | 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 | 574 – 578 | 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 | 584 – 586 | 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 | 588 – 591 | 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 | 592 – 594 | 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 | 598 – 600 | 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 | 601 – 614 | 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 | 14 | |
| <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 | 615 – 617 | 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 | 619 – 629 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 631 – 640 | 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 DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 641 – 643 | 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 | 648 – 654 | 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 | 659 – 661 | 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 | 664 – 671 | 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 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 | 676 – 679 | 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 | 680 – 685 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 689 – 697 | 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 | 698 – 705 | 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 | 709 – 711 | 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 | 714 – 725 | 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 | 12 | |
| <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 | 731 – 735 | 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 | 745 – 762 | 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 | 18 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P27487 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P27487 |
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 | P27487 |
<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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2100 Eukaryota COG1506 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119233 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231875 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG005527 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P27487 |
KEGG Orthology (KO) More...KOi | K01278 |
Identification of Orthologs from Complete Genome Data More...OMAi | QFILLEY |
Database of Orthologous Groups More...OrthoDBi | EOG091G0BU5 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P27487 |
TreeFam database of animal gene trees More...TreeFami | TF313309 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.140.10.30, 1 hit 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058 AB_hydrolase IPR002471 Pept_S9_AS IPR001375 Peptidase_S9 IPR002469 Peptidase_S9B_N IPR038554 Peptidase_S9B_N_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00930 DPPIV_N, 1 hit PF00326 Peptidase_S9, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474 SSF53474, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00708 PRO_ENDOPEP_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
MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK
60 70 80 90 100
NTYRLKLYSL RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH
110 120 130 140 150
SINDYSISPD GQFILLEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN
160 170 180 190 200
NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL PSYRITWTGK EDIIYNGITD
210 220 230 240 250
WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK
260 270 280 290 300
TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL
310 320 330 340 350
CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST
360 370 380 390 400
TGWVGRFRPS EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG
410 420 430 440 450
TWEVIGIEAL TSDYLYYISN EYKGMPGGRN LYKIQLSDYT KVTCLSCELN
460 470 480 490 500
PERCQYYSVS FSKEAKYYQL RCSGPGLPLY TLHSSVNDKG LRVLEDNSAL
510 520 530 540 550
DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY PLLLDVYAGP
560 570 580 590 600
CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
610 620 630 640 650
FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG
660 670 680 690 700
IAVAPVSRWE YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY
710 720 730 740 750
LLIHGTADDN VHFQQSAQIS KALVDVGVDF QAMWYTDEDH GIASSTAHQH
760
IYTHMSHFIK QCFSLP
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 | 6 | K → R in AAA52308 (PubMed:1347043).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 | 7 | V → I in CAA43118 (PubMed:1352704).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 | 437 | S → I in CAA43118 (PubMed:1352704).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 | 557 | T → I in AAA52308 (PubMed:1347043).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 | 663 | D → E in AAA52308 (PubMed:1347043).Curated | 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 | X60708 mRNA Translation: CAA43118.1 M80536 mRNA Translation: AAA52308.1 M74777 mRNA Translation: AAA51943.1 U13735 , U13710, U13711, U13712, U13713, U13714, U13715, U13716, U13717, U13718, U13719, U13720, U13721, U13722, U13723, U13724, U13725, U13726, U13727, U13728, U13729, U13730, U13731, U13732, U13733, U13734 Genomic DNA Translation: AAB60646.1 AB451339 mRNA Translation: BAG70153.1 AB451488 mRNA Translation: BAG70302.1 AC008063 Genomic DNA Translation: AAX93179.1 CH471058 Genomic DNA Translation: EAX11361.1 BC013329 mRNA Translation: AAH13329.2 BC065265 mRNA Translation: AAH65265.1 S79876 Genomic DNA Translation: AAB35614.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2216.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S24313 CDHU26 |
NCBI Reference Sequences More...RefSeqi | NP_001926.2, NM_001935.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.368912 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000360534; ENSP00000353731; ENSG00000197635 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1803 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1803 |
UCSC genome browser More...UCSCi | uc002ubz.4 human |
<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 | |
|---|---|---|---|---|---|
| P27487 | UPI00004C7FC2 | 738 | |||
| UPI000BB68842 | 804 | ||||
| dipeptidyl peptidase 4 isoform X1 | 804 | ||||
| UPI0005768155 | 776 | ||||
| UPI00057B90CB | 767 | ||||
| +59 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P27487 | UPI00004C7FC2 | 738 | |||
| dipeptidyl peptidase 4 isoform X1 | 804 | ||||
| UPI000BB68842 | 804 | ||||
| UPI0005768155 | 776 | ||||
| UPI00057B90CB | 767 | ||||
| +325 | |||||
<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 Dipeptidyl peptidase-4 entry |
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
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 | X60708 mRNA Translation: CAA43118.1 M80536 mRNA Translation: AAA52308.1 M74777 mRNA Translation: AAA51943.1 U13735 , U13710, U13711, U13712, U13713, U13714, U13715, U13716, U13717, U13718, U13719, U13720, U13721, U13722, U13723, U13724, U13725, U13726, U13727, U13728, U13729, U13730, U13731, U13732, U13733, U13734 Genomic DNA Translation: AAB60646.1 AB451339 mRNA Translation: BAG70153.1 AB451488 mRNA Translation: BAG70302.1 AC008063 Genomic DNA Translation: AAX93179.1 CH471058 Genomic DNA Translation: EAX11361.1 BC013329 mRNA Translation: AAH13329.2 BC065265 mRNA Translation: AAH65265.1 S79876 Genomic DNA Translation: AAB35614.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2216.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S24313 CDHU26 |
NCBI Reference Sequences More...RefSeqi | NP_001926.2, NM_001935.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.368912 |
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 |
| 1J2E | X-ray | 2.60 | A/B | 33-766 | [»] | |
| 1N1M | X-ray | 2.50 | A/B | 39-766 | [»] | |
| 1NU6 | X-ray | 2.10 | A/B | 39-766 | [»] | |
| 1NU8 | X-ray | 2.50 | A/B | 39-766 | [»] | |
| 1PFQ | X-ray | 1.90 | A/B | 36-766 | [»] | |
| 1R9M | X-ray | 2.10 | A/B/C/D | 39-766 | [»] | |
| 1R9N | X-ray | 2.30 | A/B/C/D | 39-766 | [»] | |
| 1RWQ | X-ray | 2.20 | A/B | 39-766 | [»] | |
| 1TK3 | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 1TKR | X-ray | 2.70 | A/B | 39-766 | [»] | |
| 1U8E | X-ray | 2.20 | A/B | 39-766 | [»] | |
| 1W1I | X-ray | 3.03 | A/B/C/D | 39-766 | [»] | |
| 1WCY | X-ray | 2.20 | A/B | 33-766 | [»] | |
| 1X70 | X-ray | 2.10 | A/B | 39-766 | [»] | |
| 2AJL | X-ray | 2.50 | I/J | 39-766 | [»] | |
| 2BGN | X-ray | 3.15 | A/B/C/D | 39-766 | [»] | |
| 2BGR | X-ray | 2.00 | A/B | 29-766 | [»] | |
| 2BUB | X-ray | 2.66 | A/B | 39-766 | [»] | |
| 2FJP | X-ray | 2.40 | A/B | 39-766 | [»] | |
| 2G5P | X-ray | 2.40 | A/B | 39-764 | [»] | |
| 2G5T | X-ray | 2.30 | A/B | 39-764 | [»] | |
| 2G63 | X-ray | 2.00 | A/B/C/D | 39-764 | [»] | |
| 2HHA | X-ray | 2.35 | A/B | 40-766 | [»] | |
| 2I03 | X-ray | 2.40 | A/B/C/D | 39-764 | [»] | |
| 2I78 | X-ray | 2.50 | A/B/C/D | 39-764 | [»] | |
| 2IIT | X-ray | 2.35 | A/B | 39-766 | [»] | |
| 2IIV | X-ray | 2.15 | A/B | 39-766 | [»] | |
| 2JID | X-ray | 2.80 | A/B | 31-766 | [»] | |
| 2OAG | X-ray | 2.30 | A/B/C/D | 39-764 | [»] | |
| 2OGZ | X-ray | 2.10 | A/B | 39-766 | [»] | |
| 2OLE | X-ray | 2.40 | A/B | 39-766 | [»] | |
| 2ONC | X-ray | 2.55 | A/B/C/D | 41-766 | [»] | |
| 2OPH | X-ray | 2.40 | A/B | 39-766 | [»] | |
| 2OQI | X-ray | 2.80 | A/B/C/D | 39-766 | [»] | |
| 2OQV | X-ray | 2.80 | A/B | 39-764 | [»] | |
| 2P8S | X-ray | 2.20 | A/B | 40-766 | [»] | |
| 2QJR | X-ray | 2.20 | A/B | 31-766 | [»] | |
| 2QKY | X-ray | 3.10 | A/B/C/D | 40-766 | [»] | |
| 2QOE | X-ray | 2.30 | A/B | 39-766 | [»] | |
| 2QT9 | X-ray | 2.10 | A/B | 1-766 | [»] | |
| 2QTB | X-ray | 2.25 | A/B | 1-766 | [»] | |
| 2RGU | X-ray | 2.60 | A/B | 39-766 | [»] | |
| 2RIP | X-ray | 2.90 | A | 38-766 | [»] | |
| 3BJM | X-ray | 2.35 | A/B | 39-766 | [»] | |
| 3C43 | X-ray | 2.30 | A/B | 39-766 | [»] | |
| 3C45 | X-ray | 2.05 | A/B | 39-766 | [»] | |
| 3CCB | X-ray | 2.49 | A/B/C/D | 39-766 | [»] | |
| 3CCC | X-ray | 2.71 | A/B/C/D | 39-766 | [»] | |
| 3D4L | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 3EIO | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 3F8S | X-ray | 2.43 | A/B | 31-766 | [»] | |
| 3G0B | X-ray | 2.25 | A/B/C/D | 39-766 | [»] | |
| 3G0C | X-ray | 2.69 | A/B/C/D | 39-766 | [»] | |
| 3G0D | X-ray | 2.39 | A/B/C/D | 39-766 | [»] | |
| 3G0G | X-ray | 2.45 | A/B/C/D | 39-766 | [»] | |
| 3H0C | X-ray | 2.66 | A/B | 39-766 | [»] | |
| 3HAB | X-ray | 2.10 | A/B | 39-766 | [»] | |
| 3HAC | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 3KWF | X-ray | 2.40 | A/B | 39-766 | [»] | |
| 3KWJ | X-ray | 2.80 | A/B | 39-766 | [»] | |
| 3NOX | X-ray | 2.34 | A/B | 39-766 | [»] | |
| 3O95 | X-ray | 2.85 | A/B/C/D | 39-766 | [»] | |
| 3O9V | X-ray | 2.75 | A/B/C/D | 39-766 | [»] | |
| 3OC0 | X-ray | 2.70 | A/B | 39-766 | [»] | |
| 3OPM | X-ray | 2.72 | A/B/C/D | 39-766 | [»] | |
| 3Q0T | X-ray | 2.40 | A/B | 39-766 | [»] | |
| 3Q8W | X-ray | 3.64 | A/B | 39-764 | [»] | |
| 3QBJ | X-ray | 2.21 | A/B | 31-766 | [»] | |
| 3SWW | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 3SX4 | X-ray | 2.60 | A/B | 39-766 | [»] | |
| 3VJK | X-ray | 2.49 | A/B | 33-766 | [»] | |
| 3VJL | X-ray | 2.39 | A/B | 33-766 | [»] | |
| 3VJM | X-ray | 2.10 | A/B | 33-766 | [»] | |
| 3W2T | X-ray | 2.36 | A/B | 33-766 | [»] | |
| 3WQH | X-ray | 2.85 | A/B | 39-766 | [»] | |
| 4A5S | X-ray | 1.62 | A/B | 39-766 | [»] | |
| 4DSA | X-ray | 3.25 | A/B | 39-766 | [»] | |
| 4DSZ | X-ray | 3.20 | A/B | 39-766 | [»] | |
| 4DTC | X-ray | 3.00 | A/B | 39-766 | [»] | |
| 4G1F | X-ray | 2.90 | A/B/C/D | 39-766 | [»] | |
| 4J3J | X-ray | 3.20 | A/B | 39-766 | [»] | |
| 4JH0 | X-ray | 2.35 | A/B | 39-766 | [»] | |
| 4KR0 | X-ray | 2.70 | A | 39-766 | [»] | |
| 4L72 | X-ray | 3.00 | A | 39-766 | [»] | |
| 4LKO | X-ray | 2.43 | A/B | 39-766 | [»] | |
| 4N8D | X-ray | 1.65 | A/B | 39-766 | [»] | |
| 4N8E | X-ray | 2.30 | A/B | 39-766 | [»] | |
| 4PNZ | X-ray | 1.90 | A/B | 39-766 | [»] | |
| 4PV7 | X-ray | 3.24 | A/B | 39-766 | [»] | |
| 4QZV | X-ray | 2.59 | A/C | 39-766 | [»] | |
| 5I7U | X-ray | 1.95 | A/B | 39-766 | [»] | |
| 5ISM | X-ray | 2.00 | A/B | 39-766 | [»] | |
| 5J3J | X-ray | 2.75 | A/B | 40-766 | [»] | |
| 5KBY | X-ray | 2.24 | A/B/C/D | 39-766 | [»] | |
| 5T4B | X-ray | 1.76 | A/B | 40-766 | [»] | |
| 5T4E | X-ray | 1.77 | A/B | 40-766 | [»] | |
| 5T4F | X-ray | 1.90 | A/B | 40-766 | [»] | |
| 5T4H | X-ray | 2.61 | A/B | 40-766 | [»] | |
| 6B1E | X-ray | 1.77 | A/B | 39-766 | [»] | |
| 6B1O | X-ray | 1.91 | A/B | 39-766 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P27487 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P27487 | |||||
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 | 108137, 8 interactors |
Database of interacting proteins More...DIPi | DIP-351N |
Protein interaction database and analysis system More...IntActi | P27487, 23 interactors |
Molecular INTeraction database More...MINTi | P27487 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353731 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P27487 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL284 |
Drug and drug target database More...DrugBanki | DB07482 (2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE DB03253 (2s)-Pyrrolidin-2-Ylmethylamine DB04577 1-(1-phenylcyclopentyl)methylamine DB08024 1-[2-(S)-AMINO-3-BIPHENYL-4-YL-PROPIONYL]-PYRROLIDINE-2-(S)-CARBONITRILE DB07412 1-biphenyl-2-ylmethanamine DB08588 2-({2-[(3R)-3-AMINOPIPERIDIN-1-YL]-4-OXOQUINAZOLIN-3(4H)-YL}METHYL)BENZONITRILE DB01884 2-Amino-3-Methyl-1-Pyrrolidin-1-Yl-Butan-1-One DB08672 4-[(3R)-3-{[2-(4-FLUOROPHENYL)-2-OXOETHYL]AMINO}BUTYL]BENZAMIDE DB03660 4-Iodo-L-phenylalanine DB07239 7-(aminomethyl)-6-(2-chlorophenyl)-1-methyl-1H-benzimidazole-5-carbonitrile DB06203 Alogliptin DB01076 Atorvastatin DB04491 Diisopropylphosphono Group DB06127 KRP-104 DB08882 Linagliptin DB06655 Liraglutide DB07779 N-({(2S)-1-[(3R)-3-AMINO-4-(2-FLUOROPHENYL)BUTANOYL]PYRROLIDIN-2-YL}METHYL)BENZAMIDE DB08429 N-({(2S)-1-[(3R)-3-amino-4-(3-chlorophenyl)butanoyl]pyrrolidin-2-yl}methyl)-3-(methylsulfonyl)benzamide DB05065 PHX1149 DB05001 PSN9301 DB06335 Saxagliptin DB01261 Sitagliptin DB04876 Vildagliptin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1612 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-DPP4 DPP4N_Peptidase_S9 |
MEROPS protease database More...MEROPSi | S09.003 |
MoonProt database of moonlighting proteins More...MoonProti | P27487 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P27487 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P27487 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DPP4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1352311 |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | P27487 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P27487 |
PeptideAtlas More...PeptideAtlasi | P27487 |
PRoteomics IDEntifications database More...PRIDEi | P27487 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54396 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1803 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000360534; ENSP00000353731; ENSG00000197635 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1803 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1803 |
UCSC genome browser More...UCSCi | uc002ubz.4 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1803 |
DisGeNET More...DisGeNETi | 1803 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000197635.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | DPP4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3009 DPP4 |
Human Protein Atlas More...HPAi | CAB045970 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 102720 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P27487 |
Open Targets More...OpenTargetsi | ENSG00000197635 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27467 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2100 Eukaryota COG1506 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119233 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231875 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG005527 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P27487 |
KEGG Orthology (KO) More...KOi | K01278 |
Identification of Orthologs from Complete Genome Data More...OMAi | QFILLEY |
Database of Orthologous Groups More...OrthoDBi | EOG091G0BU5 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P27487 |
TreeFam database of animal gene trees More...TreeFami | TF313309 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.14.5 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) R-HSA-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P27487 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P27487 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | DPP4 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P27487 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Dipeptidyl_peptidase-4 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1803 |
Protein Ontology More...PROi | PR:P27487 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000197635 |
CleanEx database of gene expression profiles More...CleanExi | HS_DPP4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P27487 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P27487 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.140.10.30, 1 hit 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058 AB_hydrolase IPR002471 Pept_S9_AS IPR001375 Peptidase_S9 IPR002469 Peptidase_S9B_N IPR038554 Peptidase_S9B_N_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00930 DPPIV_N, 1 hit PF00326 Peptidase_S9, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474 SSF53474, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00708 PRO_ENDOPEP_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 | DPP4_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 | P27487Primary (citable) accession number: P27487 Secondary accession number(s): Q53TN1 | |
| <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: | August 1, 1992 |
| Last sequence update: | February 1, 1996 | |
| Last modified: | June 20, 2018 | |
| This is version 206 of the entry and version 2 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, Direct protein sequencing, Reference proteomeDocuments
- Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries - Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - 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 - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
