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Protein

Insulin-degrading enzyme

Gene

IDE

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

Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.3 Publications
(Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV).2 Publications

Miscellaneous

ATP-binding induces a conformation change.

<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 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+1 PublicationNote: Binds 1 zinc ion per subunit.1 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

Activated by small peptides (By similarity). Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi. Inhibited by bacitracin. Inhibited by S-nitrosylation and oxidation agents.By similarity2 Publications

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 bindingi108ZincPROSITE-ProRule annotation1
<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 sitei111Proton acceptorPROSITE-ProRule annotation1
Metal bindingi112ZincPROSITE-ProRule annotation1
Metal bindingi189ZincPROSITE-ProRule annotation1
<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 sitei429ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi895 – 901ATPBy similarity7

<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

GO - Biological processi

<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 functionAllosteric enzyme, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
Biological processHost-virus interaction
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.56 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5689880 Ub-specific processing proteases
R-HSA-9033241 Peroxisomal protein import

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P14735

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M16.982

<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:
Insulin-degrading enzyme (EC:3.4.24.56)
Alternative name(s):
Abeta-degrading protease
Insulin protease
Short name:
Insulinase
Insulysin
<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:IDE
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000119912.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:5381 IDE

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
146680 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P14735

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, 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>Mutagenesisi111E → Q: Loss of catalytic activity. 1 Publication1
Mutagenesisi132S → C: Increases catalytic rate towards INS and amyloid; when associated with C-817. 1 Publication1
Mutagenesisi184N → C: Increases catalytic rate towards INS and amyloid; when associated with C-828. 1 Publication1
Mutagenesisi426D → C: Increases catalytic rate towards INS and amyloid; when associated with C-899. 2 Publications1
Mutagenesisi817E → C: Increases catalytic rate towards INS and amyloid; when associated with C-132. 1 Publication1
Mutagenesisi828Q → C: Increases catalytic rate towards INS and amyloid; when associated with C-184. 1 Publication1
Mutagenesisi831Y → F: No effect on catalytic activity. 1
Mutagenesisi899K → C: Increases catalytic rate towards INS and amyloid; when associated with C-426. 2 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
3416

Open Targets

More...
OpenTargetsi
ENSG00000119912

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA29629

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1293287

Drug and drug target database

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DrugBanki
DB00626 Bacitracin
DB00030 Insulin Human
DB00071 Insulin Pork

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2371

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
IDE

Domain mapping of disease mutations (DMDM)

More...
DMDMi
215274252

<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_00000744041 – 1019Insulin-degrading enzymeAdd BLAST1019

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei192N6-succinyllysineBy similarity1
Modified residuei697N6-succinyllysineBy similarity1

<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 N-terminus is blocked.

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P14735

MaxQB - The MaxQuant DataBase

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MaxQBi
P14735

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

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PaxDbi
P14735

PeptideAtlas

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PeptideAtlasi
P14735

PRoteomics IDEntifications database

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PRIDEi
P14735

ProteomicsDB human proteome resource

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ProteomicsDBi
53079

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P14735

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

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PhosphoSitePlusi
P14735

<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

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Bgeei
ENSG00000119912 Expressed in 218 organ(s), highest expression level in hair follicle

CleanEx database of gene expression profiles

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CleanExi
HS_IDE

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P14735 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P14735 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA063478

<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. Can form higher oligomers.3 Publications
(Microbial infection) Interacts (via N-terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform may function as an entry receptor for this virus (PubMed:17055432, PubMed:17553876).2 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109642, 90 interactors

Database of interacting proteins

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DIPi
DIP-55771N

Protein interaction database and analysis system

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IntActi
P14735, 32 interactors

Molecular INTeraction database

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MINTi
P14735

STRING: functional protein association networks

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STRINGi
9606.ENSP00000265986

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P14735

<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

11019
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P14735

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

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SMRi
P14735

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P14735

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni336 – 342Substrate binding exosite7
Regioni359 – 363Substrate binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi853 – 858SlyX motif6

<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 SlyX motif may be involved in the non-conventional secretion of the protein.By similarity

<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 M16 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0959 Eukaryota
COG1025 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155780

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000161331

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG106799

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P14735

KEGG Orthology (KO)

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KOi
K01408

Identification of Orthologs from Complete Genome Data

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OMAi
GIRIIVQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0255

Database for complete collections of gene phylogenies

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PhylomeDBi
P14735

TreeFam database of animal gene trees

More...
TreeFami
TF106275

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011249 Metalloenz_LuxS/M16
IPR011765 Pept_M16_N
IPR001431 Pept_M16_Zn_BS
IPR007863 Peptidase_M16_C
IPR032632 Peptidase_M16_M

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00675 Peptidase_M16, 1 hit
PF05193 Peptidase_M16_C, 2 hits
PF16187 Peptidase_M16_M, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF63411 SSF63411, 4 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00143 INSULINASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P14735-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI
60 70 80 90 100
GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP
110 120 130 140 150
PNIAGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY
160 170 180 190 200
FDVSHEHLEG ALDRFAQFFL CPLFDESCKD REVNAVDSEH EKNVMNDAWR
210 220 230 240 250
LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE LLKFHSAYYS
260 270 280 290 300
SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ
310 320 330 340 350
LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL
360 370 380 390 400
KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK
410 420 430 440 450
LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGI LHYYPLEEVL
460 470 480 490 500
TAEYLLEEFR PDLIEMVLDK LRPENVRVAI VSKSFEGKTD RTEEWYGTQY
510 520 530 540 550
KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL EKEATPYPAL
560 570 580 590 600
IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL
610 620 630 640 650
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA
660 670 680 690 700
TFEIDEKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL
710 720 730 740 750
KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG IMQMVEDTLI
760 770 780 790 800
EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ
810 820 830 840 850
STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII
860 870 880 890 900
QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL
910 920 930 940 950
SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR
960 970 980 990 1000
RHKVSVHVLA REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR
1010
GLPLFPLVKP HINFMAAKL
Length:1,019
Mass (Da):117,968
Last modified:November 25, 2008 - v4
<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:i8A28AEF75EDA0EDA
GO
Isoform 2 (identifier: P14735-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-555: Missing.

Show »
Length:464
Mass (Da):54,240
Checksum:iD51C435A02BA4932
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
Q5T5N3Q5T5N3_HUMAN
Insulin-degrading enzyme
IDE
257Annotation 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>
R4GN65R4GN65_HUMAN
Insulin-degrading enzyme
IDE
61Annotation 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 conflicti78I → M in AAA52712 (PubMed:2293021).Curated1
Sequence conflicti472R → G in BAG35668 (PubMed:14702039).Curated1
Sequence conflicti555A → V in AAA52712 (PubMed:2293021).Curated1
Sequence conflicti567 – 569FFL → KKK in AAA52712 (PubMed:2293021).Curated3
Sequence conflicti586D → G in BAG35668 (PubMed:14702039).Curated1
Sequence conflicti845G → S in AAA52712 (PubMed:2293021).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0443031 – 555Missing in isoform 2. 1 PublicationAdd BLAST555

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M21188 mRNA Translation: AAA52712.1
AK312810 mRNA Translation: BAG35668.1
AK316407 mRNA Translation: BAH14778.1
AL356128 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50090.1
CH471066 Genomic DNA Translation: EAW50091.1
BC096336 mRNA Translation: AAH96336.1
BC096337 mRNA Translation: AAH96337.1
BC096339 mRNA Translation: AAH96339.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS53554.1 [P14735-2]
CCDS7421.1 [P14735-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40119 SNHUIN

NCBI Reference Sequences

More...
RefSeqi
NP_001159418.1, NM_001165946.1 [P14735-2]
NP_004960.2, NM_004969.3 [P14735-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.500546

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265986; ENSP00000265986; ENSG00000119912 [P14735-1]
ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
3416

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3416

UCSC genome browser

More...
UCSCi
uc001kia.4 human [P14735-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
M21188 mRNA Translation: AAA52712.1
AK312810 mRNA Translation: BAG35668.1
AK316407 mRNA Translation: BAH14778.1
AL356128 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50090.1
CH471066 Genomic DNA Translation: EAW50091.1
BC096336 mRNA Translation: AAH96336.1
BC096337 mRNA Translation: AAH96337.1
BC096339 mRNA Translation: AAH96339.1
CCDSiCCDS53554.1 [P14735-2]
CCDS7421.1 [P14735-1]
PIRiA40119 SNHUIN
RefSeqiNP_001159418.1, NM_001165946.1 [P14735-2]
NP_004960.2, NM_004969.3 [P14735-1]
UniGeneiHs.500546

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G47X-ray2.10A/B42-1019[»]
2G48X-ray2.60A/B42-1019[»]
2G49X-ray2.50A/B42-1019[»]
2G54X-ray2.25A/B42-1019[»]
2G56X-ray2.20A/B42-1019[»]
2JBUX-ray3.00A/B42-1019[»]
2JG4X-ray2.80A/B43-1019[»]
2WBYX-ray2.60A/B42-1019[»]
2WC0X-ray2.80A/B42-1019[»]
2WK3X-ray2.59A/B1-1019[»]
2YPUX-ray2.80A/B42-1019[»]
3CWWX-ray1.96A/B42-1019[»]
3E4AX-ray2.60A/B1-1019[»]
3E4ZX-ray2.28A/B42-1019[»]
3E50X-ray2.30A/B42-1019[»]
3H44X-ray3.00A/B42-1019[»]
3HGZX-ray2.91A/B43-1011[»]
3N56X-ray3.10A/B42-1019[»]
3N57X-ray3.03A/B42-1019[»]
3OFIX-ray2.35A/B42-1019[»]
3QZ2X-ray3.20A/B42-1019[»]
4DTTX-ray3.22A/B42-1019[»]
4DWKX-ray3.00A/B42-1019[»]
4GS8X-ray2.99A/B42-1019[»]
4GSCX-ray2.81A/B42-1019[»]
4GSFX-ray2.70A/B42-1019[»]
4IFHX-ray3.29A/B42-1019[»]
4IOFX-ray3.35A/B42-1019[»]
4LTEX-ray2.70A/B42-1019[»]
4M1CX-ray3.50A/B42-1019[»]
4NXOX-ray2.73A/B42-1019[»]
4PESX-ray2.21A/B42-1019[»]
4PF7X-ray2.33A/B42-1019[»]
4PF9X-ray2.50A/B42-1019[»]
4PFCX-ray2.21A/B42-1019[»]
4QIAX-ray3.20A/B42-1019[»]
4RALX-ray3.15A/B42-1019[»]
4RE9X-ray2.91A/B42-1019[»]
5CJOX-ray3.29A42-1019[»]
5UOEX-ray3.80A/B/C/D/E42-1019[»]
5WOBX-ray3.95A/B/C/D/E/F/G/H42-1019[»]
6B3Qelectron microscopy3.70A/B42-1019[»]
6B70electron microscopy3.70A/B46-1011[»]
6B7Yelectron microscopy6.50A/B46-1011[»]
6B7Zelectron microscopy6.50A/B46-1011[»]
6BF6electron microscopy6.50A/B46-1011[»]
6BF7electron microscopy6.50A/B46-1011[»]
6BF8electron microscopy4.20A/B46-1011[»]
6BF9electron microscopy7.20A/B46-1011[»]
6BFCelectron microscopy3.70A/B46-1011[»]
ProteinModelPortaliP14735
SMRiP14735
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109642, 90 interactors
DIPiDIP-55771N
IntActiP14735, 32 interactors
MINTiP14735
STRINGi9606.ENSP00000265986

Chemistry databases

BindingDBiP14735
ChEMBLiCHEMBL1293287
DrugBankiDB00626 Bacitracin
DB00030 Insulin Human
DB00071 Insulin Pork
GuidetoPHARMACOLOGYi2371

Protein family/group databases

MEROPSiM16.982

PTM databases

iPTMnetiP14735
PhosphoSitePlusiP14735

Polymorphism and mutation databases

BioMutaiIDE
DMDMi215274252

Proteomic databases

EPDiP14735
MaxQBiP14735
PaxDbiP14735
PeptideAtlasiP14735
PRIDEiP14735
ProteomicsDBi53079

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265986; ENSP00000265986; ENSG00000119912 [P14735-1]
ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2]
GeneIDi3416
KEGGihsa:3416
UCSCiuc001kia.4 human [P14735-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3416
DisGeNETi3416
EuPathDBiHostDB:ENSG00000119912.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
IDE

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0009042
HGNCiHGNC:5381 IDE
HPAiHPA063478
MIMi146680 gene
neXtProtiNX_P14735
OpenTargetsiENSG00000119912
PharmGKBiPA29629

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0959 Eukaryota
COG1025 LUCA
GeneTreeiENSGT00940000155780
HOGENOMiHOG000161331
HOVERGENiHBG106799
InParanoidiP14735
KOiK01408
OMAiGIRIIVQ
OrthoDBiEOG091G0255
PhylomeDBiP14735
TreeFamiTF106275

Enzyme and pathway databases

BRENDAi3.4.24.56 2681
ReactomeiR-HSA-5689880 Ub-specific processing proteases
R-HSA-9033241 Peroxisomal protein import
SignaLinkiP14735

Miscellaneous databases

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

More...
ChiTaRSi
IDE human
EvolutionaryTraceiP14735

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Insulin-degrading_enzyme

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

More...
GenomeRNAii
3416

Protein Ontology

More...
PROi
PR:P14735

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000119912 Expressed in 218 organ(s), highest expression level in hair follicle
CleanExiHS_IDE
ExpressionAtlasiP14735 baseline and differential
GenevisibleiP14735 HS

Family and domain databases

InterProiView protein in InterPro
IPR011249 Metalloenz_LuxS/M16
IPR011765 Pept_M16_N
IPR001431 Pept_M16_Zn_BS
IPR007863 Peptidase_M16_C
IPR032632 Peptidase_M16_M
PfamiView protein in Pfam
PF00675 Peptidase_M16, 1 hit
PF05193 Peptidase_M16_C, 2 hits
PF16187 Peptidase_M16_M, 1 hit
SUPFAMiSSF63411 SSF63411, 4 hits
PROSITEiView protein in PROSITE
PS00143 INSULINASE, 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 nameiIDE_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: P14735
Secondary accession number(s): B2R721
, B7ZAU2, D3DR35, Q5T5N2
<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: April 1, 1990
Last sequence update: November 25, 2008
Last modified: December 5, 2018
This is version 194 of the entry and version 4 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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