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UniProtKB - P27487 (DPP4_HUMAN)

Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.10 Publications

Miscellaneous

Level of plasma concentrations of the soluble form (SDPP) can be managed as a colon carcinoma diagnostic and prognostic marker.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by GPC3 and diprotin A.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei630Charge relay systemPROSITE-ProRule annotation1
Active sitei708Charge relay systemPROSITE-ProRule annotation1
Active sitei740Charge relay systemPROSITE-ProRule annotation1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionAminopeptidase, Hydrolase, Protease, Receptor, Serine protease
Biological processCell 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)
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:
Dipeptidyl peptidase 4 membrane form
Alternative name(s):
Dipeptidyl peptidase IV membrane form
Dipeptidyl peptidase 4 soluble 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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 domaini1 – 6CytoplasmicSequence analysis6
<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>Transmembranei7 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST22
Topological domaini29 – 766ExtracellularSequence analysisAdd BLAST738

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi85N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi92N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi150N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi205E → K: Inhibits dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi206E → L: Inhibits dipeptidyl peptidase activity. 1 Publication1
Mutagenesisi219N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi229N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi281N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi321N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi520N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi685N → A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation. 1 Publication1
Mutagenesisi750H → A: Inhibits weakly homodimerization and dipeptidyl peptidase activity. 2 Publications1
Mutagenesisi750H → E: Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation activity. 2 Publications1

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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_00000272131 – 766Dipeptidyl peptidase 4 membrane formAdd BLAST766
ChainiPRO_000002721439 – 766Dipeptidyl peptidase 4 soluble formAdd BLAST728

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi85N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi92N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi150N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi219N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi229N-linked (GlcNAc...) asparagine4 Publications1
Glycosylationi281N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi321N-linked (GlcNAc...) asparagine2 Publications1
<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 bondi328 ↔ 339
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Glycosylationi520N-linked (GlcNAc...) asparagine4 Publications1
Disulfide bondi649 ↔ 762
Glycosylationi685N-linked (GlcNAc...) asparagine2 Publications1

<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

The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.
N- and O-Glycosylated.8 Publications
Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

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

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1177

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

Expressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon.2 Publications

<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

Up-regulated by IL12/interleukin-12 on activated T-cells. IL12-activated cells expressed enhanced levels of DPP4 but not mRNAs. Down-regulated by TNF. Up-regulated in migratory endothelial cells and in the invasive endothelial cells in tumors. Induced by hypoxia (PubMed:16670267).5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000197635 Expressed in 171 organ(s), highest expression level in tendon of biceps brachii

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

Monomer. Homodimer (PubMed:12832764, PubMed:15448155, PubMed:17287217, PubMed:12646248, PubMed:12483204, PubMed:12906826). Heterodimer with Seprase (FAP) (PubMed:16651416). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Associates with collagen (PubMed:8526932). Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes (PubMed:12676959). Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity (PubMed:15016824, PubMed:10951221, PubMed:14691230, PubMed:7907293, PubMed:8101391). Interacts with CAV1 (via the N-terminus); the interaction is direct (PubMed:17287217). Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11 (PubMed:17287217). Interacts with IGF2R; the interaction is direct (PubMed:10900005). Interacts with GPC3 (PubMed:17549790). Interacts with human coronavirus-EMC spike protein and acts as a receptor for this virus (PubMed:23486063).17 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108137, 8 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P27487

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

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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

The extracellular cysteine-rich region is necessary for association with collagen, dimer formation and optimal dipeptidyl peptidase activity.

<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

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2100 Eukaryota
COG1506 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161291

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		AYVWKND

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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P27487-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:766
Mass (Da):88,279
Last modified:February 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5FB4A2C6662D6117
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WBB6F8WBB6_HUMAN
Dipeptidyl peptidase 4
DPP4
118Annotation score:

Annotation score:1 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>
F8WE17F8WE17_HUMAN
Dipeptidyl peptidase 4
DPP4
170Annotation score:

Annotation score:1 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>
H7C1N5H7C1N5_HUMAN
Dipeptidyl peptidase 4
DPP4
86Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti6K → R in AAA52308 (PubMed:1347043).Curated1
Sequence conflicti7V → I in CAA43118 (PubMed:1352704).Curated1
Sequence conflicti437S → I in CAA43118 (PubMed:1352704).Curated1
Sequence conflicti557T → I in AAA52308 (PubMed:1347043).Curated1
Sequence conflicti663D → E in AAA52308 (PubMed:1347043).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links 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

<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:
EMBLi
GenBanki
DDBJi
Links 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
CCDSiCCDS2216.1
PIRiS24313 CDHU26
RefSeqiNP_001926.2, NM_001935.3
UniGeneiHs.368912

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2EX-ray2.60A/B33-766[»]
1N1MX-ray2.50A/B39-766[»]
1NU6X-ray2.10A/B39-766[»]
1NU8X-ray2.50A/B39-766[»]
1PFQX-ray1.90A/B36-766[»]
1R9MX-ray2.10A/B/C/D39-766[»]
1R9NX-ray2.30A/B/C/D39-766[»]
1RWQX-ray2.20A/B39-766[»]
1TK3X-ray2.00A/B39-766[»]
1TKRX-ray2.70A/B39-766[»]
1U8EX-ray2.20A/B39-766[»]
1W1IX-ray3.03A/B/C/D39-766[»]
1WCYX-ray2.20A/B33-766[»]
1X70X-ray2.10A/B39-766[»]
2AJLX-ray2.50I/J39-766[»]
2BGNX-ray3.15A/B/C/D39-766[»]
2BGRX-ray2.00A/B29-766[»]
2BUBX-ray2.66A/B39-766[»]
2FJPX-ray2.40A/B39-766[»]
2G5PX-ray2.40A/B39-764[»]
2G5TX-ray2.30A/B39-764[»]
2G63X-ray2.00A/B/C/D39-764[»]
2HHAX-ray2.35A/B40-766[»]
2I03X-ray2.40A/B/C/D39-764[»]
2I78X-ray2.50A/B/C/D39-764[»]
2IITX-ray2.35A/B39-766[»]
2IIVX-ray2.15A/B39-766[»]
2JIDX-ray2.80A/B31-766[»]
2OAGX-ray2.30A/B/C/D39-764[»]
2OGZX-ray2.10A/B39-766[»]
2OLEX-ray2.40A/B39-766[»]
2ONCX-ray2.55A/B/C/D41-766[»]
2OPHX-ray2.40A/B39-766[»]
2OQIX-ray2.80A/B/C/D39-766[»]
2OQVX-ray2.80A/B39-764[»]
2P8SX-ray2.20A/B40-766[»]
2QJRX-ray2.20A/B31-766[»]
2QKYX-ray3.10A/B/C/D40-766[»]
2QOEX-ray2.30A/B39-766[»]
2QT9X-ray2.10A/B1-766[»]
2QTBX-ray2.25A/B1-766[»]
2RGUX-ray2.60A/B39-766[»]
2RIPX-ray2.90A38-766[»]
3BJMX-ray2.35A/B39-766[»]
3C43X-ray2.30A/B39-766[»]
3C45X-ray2.05A/B39-766[»]
3CCBX-ray2.49A/B/C/D39-766[»]
3CCCX-ray2.71A/B/C/D39-766[»]
3D4LX-ray2.00A/B39-766[»]
3EIOX-ray2.00A/B39-766[»]
3F8SX-ray2.43A/B31-766[»]
3G0BX-ray2.25A/B/C/D39-766[»]
3G0CX-ray2.69A/B/C/D39-766[»]
3G0DX-ray2.39A/B/C/D39-766[»]
3G0GX-ray2.45A/B/C/D39-766[»]
3H0CX-ray2.66A/B39-766[»]
3HABX-ray2.10A/B39-766[»]
3HACX-ray2.00A/B39-766[»]
3KWFX-ray2.40A/B39-766[»]
3KWJX-ray2.80A/B39-766[»]
3NOXX-ray2.34A/B39-766[»]
3O95X-ray2.85A/B/C/D39-766[»]
3O9VX-ray2.75A/B/C/D39-766[»]
3OC0X-ray2.70A/B39-766[»]
3OPMX-ray2.72A/B/C/D39-766[»]
3Q0TX-ray2.40A/B39-766[»]
3Q8WX-ray3.64A/B39-764[»]
3QBJX-ray2.21A/B31-766[»]
3SWWX-ray2.00A/B39-766[»]
3SX4X-ray2.60A/B39-766[»]
3VJKX-ray2.49A/B33-766[»]
3VJLX-ray2.39A/B33-766[»]
3VJMX-ray2.10A/B33-766[»]
3W2TX-ray2.36A/B33-766[»]
3WQHX-ray2.85A/B39-766[»]
4A5SX-ray1.62A/B39-766[»]
4DSAX-ray3.25A/B39-766[»]
4DSZX-ray3.20A/B39-766[»]
4DTCX-ray3.00A/B39-766[»]
4G1FX-ray2.90A/B/C/D39-766[»]
4J3JX-ray3.20A/B39-766[»]
4JH0X-ray2.35A/B39-766[»]
4KR0X-ray2.70A39-766[»]
4L72X-ray3.00A39-766[»]
4LKOX-ray2.43A/B39-766[»]
4N8DX-ray1.65A/B39-766[»]
4N8EX-ray2.30A/B39-766[»]
4PNZX-ray1.90A/B39-766[»]
4PV7X-ray3.24A/B39-766[»]
4QZVX-ray2.59A/C39-766[»]
5I7UX-ray1.95A/B39-766[»]
5ISMX-ray2.00A/B39-766[»]
5J3JX-ray2.75A/B40-766[»]
5KBYX-ray2.24A/B/C/D39-766[»]
5T4BX-ray1.76A/B40-766[»]
5T4EX-ray1.77A/B40-766[»]
5T4FX-ray1.90A/B40-766[»]
5T4HX-ray2.61A/B40-766[»]
6B1EX-ray1.77A/B39-766[»]
6B1OX-ray1.91A/B39-766[»]
ProteinModelPortaliP27487
SMRiP27487
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108137, 8 interactors
CORUMiP27487
DIPiDIP-351N
IntActiP27487, 23 interactors
MINTiP27487
STRINGi9606.ENSP00000353731

Chemistry databases

BindingDBiP27487
ChEMBLiCHEMBL284
DrugBankiDB07482 (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
GuidetoPHARMACOLOGYi1612

Protein family/group databases

ESTHERihuman-DPP4 DPP4N_Peptidase_S9
MEROPSiS09.003
MoonProtiP27487

PTM databases

GlyConnecti1177
iPTMnetiP27487
PhosphoSitePlusiP27487

Polymorphism and mutation databases

BioMutaiDPP4
DMDMi1352311

Proteomic databases

MaxQBiP27487
PaxDbiP27487
PeptideAtlasiP27487
PRIDEiP27487
ProteomicsDBi54396

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1803
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360534; ENSP00000353731; ENSG00000197635
GeneIDi1803
KEGGihsa:1803
UCSCiuc002ubz.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1803
DisGeNETi1803
EuPathDBiHostDB:ENSG00000197635.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		DPP4
HGNCiHGNC:3009 DPP4
HPAiCAB045970
MIMi102720 gene
neXtProtiNX_P27487
OpenTargetsiENSG00000197635
PharmGKBiPA27467

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA
GeneTreeiENSGT00940000161291
HOGENOMiHOG000231875
HOVERGENiHBG005527
InParanoidiP27487
KOiK01278
OMAiAYVWKND
OrthoDBiEOG091G0BU5
PhylomeDBiP27487
TreeFamiTF313309

Enzyme and pathway databases

BRENDAi3.4.14.5 2681
ReactomeiR-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-RKiP27487
SIGNORiP27487

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DPP4 human
EvolutionaryTraceiP27487

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

BgeeiENSG00000197635 Expressed in 171 organ(s), highest expression level in tendon of biceps brachii
CleanExiHS_DPP4
ExpressionAtlasiP27487 baseline and differential
GenevisibleiP27487 HS

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView 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 nameiDPP4_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 210 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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