Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P16444 (DPEP1_HUMAN)

Entry version 200 (10 Apr 2019)
Sequence version 3 (07 Mar 2006)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Dipeptidase 1

Gene

DPEP1

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

Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.

<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

  • Hydrolysis of dipeptides.PROSITE-ProRule annotation EC:3.4.13.19

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+PROSITE-ProRule annotation1 Publication

<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 L-penicillamine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi36Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi38Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi141Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi141Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei168Substrate1
Metal bindingi214Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi235Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei246Substrate1
Binding sitei304Substrate1

<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 functionDipeptidase, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS00367-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.13.19 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-5423646 Aflatoxin activation and detoxification

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P16444

Protein family/group databases

MEROPS protease database

More...MEROPSi		M19.001

<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:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Dehydropeptidase-I
Microsomal dipeptidase
Renal dipeptidase
Short name:
hRDP
<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:DPEP1
Synonyms:MDP, RDP
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000015413.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:3002 DPEP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		179780 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P16444

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

<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>Mutagenesisi141E → D or C: Complete loss of activity. 1
Mutagenesisi141E → Q: Partial loss of activity. 1

Organism-specific databases

DisGeNET

More...DisGeNETi		1800

Open Targets

More...OpenTargetsi		ENSG00000015413

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA144

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1989

Drug and drug target database

More...DrugBanki		DB01597 Cilastatin
DB06211 Doripenem

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DPEP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		92090943

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 163 PublicationsAdd BLAST16
<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_000001865217 – 385Dipeptidase 1Add BLAST369
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000018653386 – 411Removed in mature formAdd BLAST26

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>Glycosylationi57N-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 bondi87 ↔ 170PROSITE-ProRule annotation1 Publication
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation1 Publication
Glycosylationi279N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi332N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi358N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi377InterchainPROSITE-ProRule annotation1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi385GPI-anchor amidated serine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P16444

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P16444

MaxQB - The MaxQuant DataBase

More...MaxQBi		P16444

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P16444

PeptideAtlas

More...PeptideAtlasi		P16444

PRoteomics IDEntifications database

More...PRIDEi		P16444

ProteomicsDB human proteome resource

More...ProteomicsDBi		53362

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1174

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P16444

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P16444

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000015413 Expressed in 101 organ(s), highest expression level in small intestine Peyer's patch

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P16444 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P16444 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA009426
HPA012783

<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

Homodimer; disulfide-linked.PROSITE-ProRule annotation1 Publication

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108134, 62 interactors

Protein interaction database and analysis system

More...IntActi		P16444, 2 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000376807

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P16444

<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

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1ITQX-ray2.30A/B17-385[»]
1ITUX-ray2.00A/B17-385[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P16444

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P16444

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		P16444

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4127 Eukaryota
COG2355 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159615

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000072016

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG002339

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16444

KEGG Orthology (KO)

More...KOi		K01273

Identification of Orthologs from Complete Genome Data

More...OMAi		EGAHMLG

Database of Orthologous Groups

More...OrthoDBi		1272387at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16444

TreeFam database of animal gene trees

More...TreeFami		TF324523

Family and domain databases

Conserved Domains Database

More...CDDi		cd01301 rDP_like, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000180 Dipep_AS
IPR028536 Dpep1
IPR032466 Metal_Hydrolase
IPR008257 Pept_M19

The PANTHER Classification System

More...PANTHERi		PTHR10443 PTHR10443, 1 hit
PTHR10443:SF12 PTHR10443:SF12, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01244 Peptidase_M19, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51556 SSF51556, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00869 RENAL_DIPEPTIDASE_1, 1 hit
PS51365 RENAL_DIPEPTIDASE_2, 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 2 potential isoforms that are computationally mapped.Show allAlign All

P16444-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR 
        60         70         80         90        100
LQDERANLTT LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE 
       110        120        130        140        150
QMDVVHRMCR MYPETFLYVT SSAGIRQAFR EGKVASLIGV EGGHSIDSSL 
       160        170        180        190        200
GVLRALYQLG MRYLTLTHSC NTPWADNWLV DTGDSEPQSQ GLSPFGQRVV 
       210        220        230        240        250
KELNRLGVLI DLAHVSVATM KATLQLSRAP VIFSHSSAYS VCASRRNVPD 
       260        270        280        290        300
DVLRLVKQTD SLVMVNFYNN YISCTNKANL SQVADHLDHI KEVAGARAVG 
       310        320        330        340        350
FGGDFDGVPR VPEGLEDVSK YPDLIAELLR RNWTEAEVKG ALADNLLRVF 
       360        370        380        390        400
EAVEQASNLT QAPEEEPIPL DQLGGSCRTH YGYSSGASSL HRHWGLLLAS 
       410 
LAPLVLCLSL L
Length:411
Mass (Da):45,674
Last modified:March 7, 2006 - v3
<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:iC8C6474C3479D20D
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BQS5H3BQS5_HUMAN
Dipeptidase
DPEP1
107Annotation score:

Annotation score:2 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>
H3BP43H3BP43_HUMAN
Dipeptidase
DPEP1
111Annotation score:

Annotation score:2 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 conflicti9P → S (PubMed:8439558).Curated1
Sequence conflicti9P → S (PubMed:7764673).Curated1
Sequence conflicti102M → R (PubMed:2303490).Curated1
Sequence conflicti125I → R (PubMed:2303490).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_036496246R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1043397364Ensembl.1
Natural variantiVAR_061375351E → K. Corresponds to variant dbSNP:rs1126464Ensembl.1
Natural variantiVAR_061376351E → Q. Corresponds to variant dbSNP:rs1126464Ensembl.1

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
D13137 Genomic DNA Translation: BAA02430.1
J05257 mRNA Translation: AAB59410.1
D13138 mRNA Translation: BAA02431.1
S70330, S70329 Genomic DNA Translation: AAC60630.2
CH471184 Genomic DNA Translation: EAW66719.1
CH471184 Genomic DNA Translation: EAW66720.1
BC017023 mRNA Translation: AAH17023.1
BT006664 mRNA Translation: AAP35310.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10982.1

Protein sequence database of the Protein Information Resource

More...PIRi		S29848

NCBI Reference Sequences

More...RefSeqi		NP_001121613.1, NM_001128141.2
NP_004404.1, NM_004413.3
XP_005256342.1, XM_005256285.4
XP_005256343.1, XM_005256286.3
XP_011521227.1, XM_011522925.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.109

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000261615; ENSP00000261615; ENSG00000015413
ENST00000393092; ENSP00000376807; ENSG00000015413
ENST00000421184; ENSP00000397313; ENSG00000015413

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1800

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1800

UCSC genome browser

More...UCSCi		uc002fnr.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13137 Genomic DNA Translation: BAA02430.1
J05257 mRNA Translation: AAB59410.1
D13138 mRNA Translation: BAA02431.1
S70330, S70329 Genomic DNA Translation: AAC60630.2
CH471184 Genomic DNA Translation: EAW66719.1
CH471184 Genomic DNA Translation: EAW66720.1
BC017023 mRNA Translation: AAH17023.1
BT006664 mRNA Translation: AAP35310.1
CCDSiCCDS10982.1
PIRiS29848
RefSeqiNP_001121613.1, NM_001128141.2
NP_004404.1, NM_004413.3
XP_005256342.1, XM_005256285.4
XP_005256343.1, XM_005256286.3
XP_011521227.1, XM_011522925.2
UniGeneiHs.109

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ITQX-ray2.30A/B17-385[»]
1ITUX-ray2.00A/B17-385[»]
ProteinModelPortaliP16444
SMRiP16444
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108134, 62 interactors
IntActiP16444, 2 interactors
STRINGi9606.ENSP00000376807

Chemistry databases

BindingDBiP16444
ChEMBLiCHEMBL1989
DrugBankiDB01597 Cilastatin
DB06211 Doripenem

Protein family/group databases

MEROPSiM19.001

PTM databases

GlyConnecti1174
iPTMnetiP16444
PhosphoSitePlusiP16444

Polymorphism and mutation databases

BioMutaiDPEP1
DMDMi92090943

Proteomic databases

EPDiP16444
jPOSTiP16444
MaxQBiP16444
PaxDbiP16444
PeptideAtlasiP16444
PRIDEiP16444
ProteomicsDBi53362

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1800
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261615; ENSP00000261615; ENSG00000015413
ENST00000393092; ENSP00000376807; ENSG00000015413
ENST00000421184; ENSP00000397313; ENSG00000015413
GeneIDi1800
KEGGihsa:1800
UCSCiuc002fnr.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1800
DisGeNETi1800
EuPathDBiHostDB:ENSG00000015413.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		DPEP1
HGNCiHGNC:3002 DPEP1
HPAiHPA009426
HPA012783
MIMi179780 gene
neXtProtiNX_P16444
OpenTargetsiENSG00000015413
PharmGKBiPA144

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4127 Eukaryota
COG2355 LUCA
GeneTreeiENSGT00940000159615
HOGENOMiHOG000072016
HOVERGENiHBG002339
InParanoidiP16444
KOiK01273
OMAiEGAHMLG
OrthoDBi1272387at2759
PhylomeDBiP16444
TreeFamiTF324523

Enzyme and pathway databases

BioCyciMetaCyc:HS00367-MONOMER
BRENDAi3.4.13.19 2681
ReactomeiR-HSA-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-HSA-5423646 Aflatoxin activation and detoxification
SABIO-RKiP16444

Miscellaneous databases

EvolutionaryTraceiP16444

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Dipeptidase_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1800

Protein Ontology

More...PROi		PR:P16444

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000015413 Expressed in 101 organ(s), highest expression level in small intestine Peyer's patch
ExpressionAtlasiP16444 baseline and differential
GenevisibleiP16444 HS

Family and domain databases

CDDicd01301 rDP_like, 1 hit
InterProiView protein in InterPro
IPR000180 Dipep_AS
IPR028536 Dpep1
IPR032466 Metal_Hydrolase
IPR008257 Pept_M19
PANTHERiPTHR10443 PTHR10443, 1 hit
PTHR10443:SF12 PTHR10443:SF12, 1 hit
PfamiView protein in Pfam
PF01244 Peptidase_M19, 1 hit
SUPFAMiSSF51556 SSF51556, 1 hit
PROSITEiView protein in PROSITE
PS00869 RENAL_DIPEPTIDASE_1, 1 hit
PS51365 RENAL_DIPEPTIDASE_2, 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 nameiDPEP1_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: P16444
Secondary accession number(s): D3DX80, Q96AK2
<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, 1990
Last sequence update: March 7, 2006
Last modified: April 10, 2019
This is version 200 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again