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Protein

Insulin-degrading enzyme

Gene

IDE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Degradation of insulin, glucagon and other polypeptides. No action on proteins.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme 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
Metal bindingi108ZincPROSITE-ProRule annotation1
Active sitei111Proton acceptorPROSITE-ProRule annotation1
Metal bindingi112ZincPROSITE-ProRule annotation1
Metal bindingi189ZincPROSITE-ProRule annotation1
Binding sitei429ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi895 – 901ATPBy similarity7

GO - Molecular functioni

  • ATPase activity Source: Ensembl
  • ATP binding Source: UniProtKB
  • beta-amyloid binding Source: Ensembl
  • beta-endorphin binding Source: Ensembl
  • glycoprotein binding Source: UniProtKB
  • insulin binding Source: UniProtKB
  • metalloendopeptidase activity Source: UniProtKB
  • peptide binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • beta-amyloid metabolic process Source: UniProtKB
  • bradykinin catabolic process Source: UniProtKB
  • determination of adult lifespan Source: UniProtKB
  • hormone catabolic process Source: Ensembl
  • insulin catabolic process Source: UniProtKB
  • insulin metabolic process Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • negative regulation of proteolysis Source: Ensembl
  • positive regulation of protein oligomerization Source: UniProtKB
  • protein heterooligomerization Source: Ensembl
  • protein homooligomerization Source: UniProtKB
  • protein homotetramerization Source: Ensembl
  • protein processing Source: GO_Central
  • proteolysis Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: UniProtKB
  • ubiquitin homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS04345-MONOMER.
BRENDAi3.4.24.56. 2681.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
SignaLinkiP14735.

Protein family/group databases

MEROPSiM16.982.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-degrading enzyme (EC:3.4.24.56)
Alternative name(s):
Abeta-degrading protease
Insulin protease
Short name:
Insulinase
Insulysin
Gene namesi
Name:IDE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:5381. IDE.

Subcellular locationi

  • Cytoplasm
  • Cell membrane
  • Secreted By similarity

  • Note: Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • cytosolic proteasome complex Source: Ensembl
  • extracellular space Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • peroxisomal matrix Source: GO_Central
  • peroxisome Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi3416.
OpenTargetsiENSG00000119912.
PharmGKBiPA29629.

Chemistry databases

ChEMBLiCHEMBL1293287.
DrugBankiDB00626. Bacitracin.
DB00030. Insulin Regular.
GuidetoPHARMACOLOGYi2371.

Polymorphism and mutation databases

BioMutaiIDE.
DMDMi215274252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000744041 – 1019Insulin-degrading enzymeAdd BLAST1019

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei192N6-succinyllysineBy similarity1
Modified residuei697N6-succinyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

EPDiP14735.
MaxQBiP14735.
PaxDbiP14735.
PeptideAtlasiP14735.
PRIDEiP14735.

PTM databases

iPTMnetiP14735.
PhosphoSitePlusiP14735.

Expressioni

Gene expression databases

BgeeiENSG00000119912.
CleanExiHS_IDE.
ExpressionAtlasiP14735. baseline and differential.
GenevisibleiP14735. HS.

Organism-specific databases

HPAiHPA063478.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CCL3P101473EBI-2556886,EBI-8459634

GO - Molecular functioni

  • insulin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109642. 80 interactors.
DIPiDIP-55771N.
IntActiP14735. 8 interactors.
MINTiMINT-2801173.
STRINGi9606.ENSP00000265986.

Chemistry databases

BindingDBiP14735.

Structurei

Secondary structure

11019
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 50Combined sources4
Beta strandi63 – 69Combined sources7
Beta strandi74 – 79Combined sources6
Beta strandi84 – 93Combined sources10
Helixi96 – 98Combined sources3
Beta strandi101 – 103Combined sources3
Helixi106 – 113Combined sources8
Helixi114 – 116Combined sources3
Beta strandi118 – 121Combined sources4
Helixi126 – 132Combined sources7
Turni133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Beta strandi147 – 154Combined sources8
Helixi155 – 157Combined sources3
Helixi158 – 166Combined sources9
Helixi167 – 169Combined sources3
Helixi176 – 194Combined sources19
Helixi197 – 207Combined sources11
Helixi214 – 216Combined sources3
Helixi223 – 226Combined sources4
Helixi228 – 232Combined sources5
Helixi237 – 248Combined sources12
Helixi251 – 253Combined sources3
Beta strandi254 – 262Combined sources9
Helixi264 – 275Combined sources12
Beta strandi276 – 278Combined sources3
Helixi295 – 297Combined sources3
Beta strandi298 – 304Combined sources7
Beta strandi307 – 309Combined sources3
Beta strandi312 – 319Combined sources8
Helixi323 – 325Combined sources3
Turni326 – 328Combined sources3
Helixi330 – 338Combined sources9
Helixi346 – 352Combined sources7
Beta strandi359 – 367Combined sources9
Beta strandi370 – 378Combined sources9
Helixi381 – 385Combined sources5
Helixi387 – 404Combined sources18
Helixi408 – 423Combined sources16
Helixi430 – 440Combined sources11
Turni441 – 443Combined sources3
Helixi446 – 448Combined sources3
Turni449 – 454Combined sources6
Helixi461 – 468Combined sources8
Helixi473 – 475Combined sources3
Beta strandi477 – 481Combined sources5
Helixi483 – 485Combined sources3
Turni486 – 488Combined sources3
Turni494 – 496Combined sources3
Beta strandi499 – 504Combined sources6
Helixi507 – 514Combined sources8
Beta strandi549 – 553Combined sources5
Beta strandi555 – 563Combined sources9
Beta strandi565 – 567Combined sources3
Beta strandi570 – 579Combined sources10
Helixi581 – 583Combined sources3
Beta strandi584 – 586Combined sources3
Helixi587 – 613Combined sources27
Beta strandi616 – 623Combined sources8
Beta strandi626 – 635Combined sources10
Helixi638 – 650Combined sources13
Helixi656 – 672Combined sources17
Helixi673 – 675Combined sources3
Helixi678 – 690Combined sources13
Beta strandi691 – 693Combined sources3
Helixi697 – 704Combined sources8
Helixi709 – 721Combined sources13
Beta strandi722 – 732Combined sources11
Helixi735 – 753Combined sources19
Helixi760 – 762Combined sources3
Beta strandi775 – 782Combined sources8
Beta strandi787 – 799Combined sources13
Helixi802 – 823Combined sources22
Turni824 – 827Combined sources4
Beta strandi831 – 840Combined sources10
Beta strandi843 – 854Combined sources12
Helixi856 – 876Combined sources21
Helixi879 – 894Combined sources16
Helixi900 – 912Combined sources13
Helixi920 – 928Combined sources9
Helixi933 – 943Combined sources11
Beta strandi952 – 959Combined sources8
Beta strandi990 – 992Combined sources3
Helixi995 – 1000Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
4Q5ZX-ray3.93A/B/C/D/E/F/G/H42-1019[»]
4QIAX-ray3.20A/B42-1019[»]
4RALX-ray3.15A/B42-1019[»]
4RE9X-ray2.91A/B42-1019[»]
5CJOX-ray3.29A42-1019[»]
ProteinModelPortaliP14735.
SMRiP14735.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14735.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni336 – 342Substrate binding exosite7
Regioni359 – 363Substrate binding5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi853 – 858SlyX motif6

Domaini

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

Sequence similaritiesi

Belongs to the peptidase M16 family.Curated

Phylogenomic databases

eggNOGiKOG0959. Eukaryota.
COG1025. LUCA.
GeneTreeiENSGT00530000063327.
HOGENOMiHOG000161331.
HOVERGENiHBG106799.
InParanoidiP14735.
KOiK01408.
OMAiLINQVME.
OrthoDBiEOG091G0255.
PhylomeDBiP14735.
TreeFamiTF106275.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
IPR032632. Peptidase_M16_M.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
PF16187. Peptidase_M16_M. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051571612E → K.Corresponds to variant rs2229708dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0443031 – 555Missing in isoform 2. 1 PublicationAdd BLAST555

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. Translation: CAI13670.1.
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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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. Translation: CAI13670.1.
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:
PDBei
RCSB PDBi
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[»]
4Q5ZX-ray3.93A/B/C/D/E/F/G/H42-1019[»]
4QIAX-ray3.20A/B42-1019[»]
4RALX-ray3.15A/B42-1019[»]
4RE9X-ray2.91A/B42-1019[»]
5CJOX-ray3.29A42-1019[»]
ProteinModelPortaliP14735.
SMRiP14735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109642. 80 interactors.
DIPiDIP-55771N.
IntActiP14735. 8 interactors.
MINTiMINT-2801173.
STRINGi9606.ENSP00000265986.

Chemistry databases

BindingDBiP14735.
ChEMBLiCHEMBL1293287.
DrugBankiDB00626. Bacitracin.
DB00030. Insulin Regular.
GuidetoPHARMACOLOGYi2371.

Protein family/group databases

MEROPSiM16.982.

PTM databases

iPTMnetiP14735.
PhosphoSitePlusiP14735.

Polymorphism and mutation databases

BioMutaiIDE.
DMDMi215274252.

Proteomic databases

EPDiP14735.
MaxQBiP14735.
PaxDbiP14735.
PeptideAtlasiP14735.
PRIDEiP14735.

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

CTDi3416.
DisGeNETi3416.
GeneCardsiIDE.
H-InvDBHIX0009042.
HGNCiHGNC:5381. IDE.
HPAiHPA063478.
MIMi146680. gene.
neXtProtiNX_P14735.
OpenTargetsiENSG00000119912.
PharmGKBiPA29629.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0959. Eukaryota.
COG1025. LUCA.
GeneTreeiENSGT00530000063327.
HOGENOMiHOG000161331.
HOVERGENiHBG106799.
InParanoidiP14735.
KOiK01408.
OMAiLINQVME.
OrthoDBiEOG091G0255.
PhylomeDBiP14735.
TreeFamiTF106275.

Enzyme and pathway databases

BioCyciZFISH:HS04345-MONOMER.
BRENDAi3.4.24.56. 2681.
ReactomeiR-HSA-5689880. Ub-specific processing proteases.
SignaLinkiP14735.

Miscellaneous databases

EvolutionaryTraceiP14735.
GeneWikiiInsulin-degrading_enzyme.
GenomeRNAii3416.
PROiP14735.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119912.
CleanExiHS_IDE.
ExpressionAtlasiP14735. baseline and differential.
GenevisibleiP14735. HS.

Family and domain databases

Gene3Di3.30.830.10. 4 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
IPR032632. Peptidase_M16_M.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
PF16187. Peptidase_M16_M. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIDE_HUMAN
AccessioniPrimary (citable) accession number: P14735
Secondary accession number(s): B2R721
, B7ZAU2, D3DR35, Q5T5N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 173 of the entry and version 4 of the sequence. [Complete history]
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.

Miscellaneousi

Miscellaneous

ATP-binding induces a conformation change.

Keywords - Technical termi

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

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.