UniProtKB - P14735 (IDE_HUMAN)
Insulin-degrading enzyme
IDE
Functioni
Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:2293021, PubMed:10684867, PubMed:26968463, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:29596046, PubMed:21098034).
Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed:23922390, PubMed:26394692, PubMed:29596046).
Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity).
Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (PubMed:9830016, PubMed:26394692) (Probable).
Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (PubMed:21098034).
Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (PubMed:21098034).
Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I.
By similarity1 Publication14 Publications(Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV).
2 PublicationsMiscellaneous
Catalytic activityi
- Degradation of insulin, glucagon and other polypeptides. No action on proteins.11 Publications EC:3.4.24.56
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 108 | ZincPROSITE-ProRule annotationCombined sources4 Publications | 1 | |
Active sitei | 111 | Proton acceptorPROSITE-ProRule annotation4 Publications | 1 | |
Metal bindingi | 112 | ZincPROSITE-ProRule annotationCombined sources4 Publications | 1 | |
Metal bindingi | 189 | ZincPROSITE-ProRule annotationCombined sources4 Publications | 1 | |
Binding sitei | 429 | ATPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 895 – 901 | ATPBy similarity | 7 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- endopeptidase activity Source: UniProtKB
- identical protein binding Source: IntAct
- insulin binding Source: UniProtKB
- metalloendopeptidase activity Source: UniProtKB
- peptide binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- ubiquitin-dependent protein binding Source: UniProtKB
- virus receptor activity Source: UniProtKB-KW
- zinc ion binding Source: UniProtKB
GO - Biological processi
- amyloid-beta clearance Source: ARUK-UCL
- amyloid-beta clearance by cellular catabolic process Source: ARUK-UCL
- amyloid-beta metabolic process Source: UniProtKB
- antigen processing and presentation of endogenous peptide antigen via MHC class I Source: UniProtKB
- bradykinin catabolic process Source: UniProtKB
- cellular protein catabolic process Source: UniProtKB
- determination of adult lifespan Source: UniProtKB
- hormone catabolic process Source: UniProtKB
- insulin catabolic process Source: UniProtKB
- insulin metabolic process Source: UniProtKB
- insulin receptor signaling pathway Source: UniProtKB
- peptide catabolic process Source: UniProtKB
- positive regulation of protein binding Source: UniProtKB
- positive regulation of protein catabolic process Source: ARUK-UCL
- protein catabolic process Source: ARUK-UCL
- proteolysis Source: UniProtKB
- proteolysis involved in cellular protein catabolic process Source: UniProtKB
- regulation of aerobic respiration Source: ARUK-UCL
- ubiquitin recycling Source: UniProtKB
Keywordsi
Molecular function | Allosteric enzyme, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor |
Biological process | Host-virus interaction |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.24.56, 2681 |
PathwayCommonsi | P14735 |
Reactomei | R-HSA-5689880, Ub-specific processing proteases R-HSA-9033241, Peroxisomal protein import |
SignaLinki | P14735 |
SIGNORi | P14735 |
Protein family/group databases
MEROPSi | M16.002 |
Names & Taxonomyi
Protein namesi | Recommended name: Insulin-degrading enzyme1 Publication (EC:3.4.24.564 Publications)Alternative name(s): Abeta-degrading protease Insulin protease1 Publication Short name: Insulinase1 Publication Insulysin1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5381, IDE |
MIMi | 146680, gene |
neXtProti | NX_P14735 |
VEuPathDBi | HostDB:ENSG00000119912 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity
Extracellular region or secreted
- Secreted 1 Publication
Cytoplasm and Cytosol
- cytosol 2 Publications
Note: Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: ARUK-UCL
- extracellular space Source: UniProtKB
Mitochondrion
- mitochondrion Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB
Peroxisome
- peroxisomal matrix Source: GO_Central
- peroxisome Source: UniProtKB
Plasma Membrane
- basolateral plasma membrane Source: ARUK-UCL
- external side of plasma membrane Source: ARUK-UCL
Other locations
- cell surface Source: UniProtKB
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 111 | E → Q: Loss of catalytic activity. 4 Publications | 1 | |
Mutagenesisi | 132 | S → C: Increases catalytic rate towards INS and amyloid; when associated with C-817. 1 Publication | 1 | |
Mutagenesisi | 184 | N → C: Increases catalytic rate towards INS and amyloid; when associated with C-828. 1 Publication | 1 | |
Mutagenesisi | 286 | P → G: Reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 366 – 369 | GARG → AARA: Reduced enzyme activity. 1 Publication | 4 | |
Mutagenesisi | 426 | D → C: Increases catalytic rate towards INS and amyloid; when associated with C-899. 2 Publications | 1 | |
Mutagenesisi | 496 | Y → A: Strongly reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 530 | F → A: Strongly increased enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 767 | R → A: Decreases dimerization. No effect on degradation of ANP. Retains the ability to degrade an aberrant form of ANP, when in the presence of both ANP and the aberrant ANP. 1 Publication | 1 | |
Mutagenesisi | 817 | E → C: Increases catalytic rate towards INS and amyloid; when associated with C-132. 1 Publication | 1 | |
Mutagenesisi | 828 | Q → C: Increases catalytic rate towards INS and amyloid; when associated with C-184. 1 Publication | 1 | |
Mutagenesisi | 831 | Y → F: No effect on catalytic activity. | 1 | |
Mutagenesisi | 899 | K → C: Increases catalytic rate towards INS and amyloid; when associated with C-426. 2 Publications | 1 |
Organism-specific databases
DisGeNETi | 3416 |
OpenTargetsi | ENSG00000119912 |
PharmGKBi | PA29629 |
Miscellaneous databases
Pharosi | P14735, Tchem |
Chemistry databases
ChEMBLi | CHEMBL1293287 |
DrugBanki | DB00626, Bacitracin DB00030, Insulin human DB00071, Insulin pork DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
DrugCentrali | P14735 |
GuidetoPHARMACOLOGYi | 2371 |
Genetic variation databases
BioMutai | IDE |
DMDMi | 215274252 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000074404 | 1 – 1019 | Insulin-degrading enzymeAdd BLAST | 1019 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 192 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 697 | N6-succinyllysineBy similarity | 1 |
Post-translational modificationi
Proteomic databases
EPDi | P14735 |
jPOSTi | P14735 |
MassIVEi | P14735 |
MaxQBi | P14735 |
PaxDbi | P14735 |
PeptideAtlasi | P14735 |
PRIDEi | P14735 |
ProteomicsDBi | 53079 [P14735-1] 7086 |
PTM databases
GlyGeni | P14735, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P14735 |
MetOSitei | P14735 |
PhosphoSitePlusi | P14735 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000119912, Expressed in hair follicle and 232 other tissues |
ExpressionAtlasi | P14735, baseline and differential |
Genevisiblei | P14735, HS |
Organism-specific databases
HPAi | ENSG00000119912, Low tissue specificity |
Interactioni
Subunit structurei
Binary interactionsi
P14735
With | #Exp. | IntAct |
---|---|---|
APP [P05067] | 3 | EBI-2556886,EBI-77613 |
CCL3 [P10147] | 3 | EBI-2556886,EBI-8459634 |
IDE - isoform 1 [P14735-1]
GO - Molecular functioni
- identical protein binding Source: IntAct
- insulin binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- ubiquitin-dependent protein binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 109642, 147 interactors |
DIPi | DIP-55771N |
IntActi | P14735, 68 interactors |
MINTi | P14735 |
STRINGi | 9606.ENSP00000265986 |
Chemistry databases
BindingDBi | P14735 |
Miscellaneous databases
RNActi | P14735, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P14735 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14735 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 336 – 342 | Substrate binding exosite | 7 | |
Regioni | 359 – 363 | Substrate binding1 Publication | 5 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 853 – 858 | SlyX motifBy similarity | 6 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0959, Eukaryota |
GeneTreei | ENSGT00940000155780 |
HOGENOMi | CLU_004639_1_1_1 |
InParanoidi | P14735 |
OMAi | WIFDEMK |
OrthoDBi | 1008844at2759 |
PhylomeDBi | P14735 |
TreeFami | TF106275 |
Family and domain databases
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 |
Pfami | View protein in Pfam PF00675, Peptidase_M16, 1 hit PF05193, Peptidase_M16_C, 2 hits PF16187, Peptidase_M16_M, 1 hit |
SUPFAMi | SSF63411, SSF63411, 4 hits |
PROSITEi | View protein in PROSITE PS00143, INSULINASE, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 15 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 15 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3ISG5 | A0A3B3ISG5_HUMAN | Insulin-degrading enzyme | IDE | 1,019 | Annotation score: | ||
A0A7I2V2P6 | A0A7I2V2P6_HUMAN | Insulin-degrading enzyme | IDE | 978 | Annotation score: | ||
A0A7I2V2S1 | A0A7I2V2S1_HUMAN | Insulin-degrading enzyme | IDE | 872 | Annotation score: | ||
A0A7I2V373 | A0A7I2V373_HUMAN | Insulin-degrading enzyme | IDE | 633 | Annotation score: | ||
A0A7I2V3E3 | A0A7I2V3E3_HUMAN | Insulin-degrading enzyme | IDE | 972 | Annotation score: | ||
A0A7I2V4Q3 | A0A7I2V4Q3_HUMAN | Insulin-degrading enzyme | IDE | 928 | Annotation score: | ||
A0A7I2V610 | A0A7I2V610_HUMAN | Insulin-degrading enzyme | IDE | 961 | Annotation score: | ||
A0A7I2V612 | A0A7I2V612_HUMAN | Insulin-degrading enzyme | IDE | 609 | Annotation score: | ||
A0A7I2V634 | A0A7I2V634_HUMAN | Insulin-degrading enzyme | IDE | 384 | Annotation score: | ||
A0A7I2YQS6 | A0A7I2YQS6_HUMAN | Insulin-degrading enzyme | IDE | 582 | Annotation score: | ||
There are more potential isoformsShow all |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 78 | I → M in AAA52712 (PubMed:2293021).Curated | 1 | |
Sequence conflicti | 472 | R → G in BAG35668 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 555 | A → V in AAA52712 (PubMed:2293021).Curated | 1 | |
Sequence conflicti | 567 – 569 | FFL → KKK in AAA52712 (PubMed:2293021).Curated | 3 | |
Sequence conflicti | 586 | D → G in BAG35668 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 845 | G → S in AAA52712 (PubMed:2293021).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_044303 | 1 – 555 | Missing in isoform 2. 1 PublicationAdd BLAST | 555 |
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 |
CCDSi | CCDS53554.1 [P14735-2] CCDS7421.1 [P14735-1] |
PIRi | A40119, SNHUIN |
RefSeqi | NP_001159418.1, NM_001165946.1 [P14735-2] NP_004960.2, NM_004969.3 [P14735-1] |
Genome annotation databases
Ensembli | ENST00000265986; ENSP00000265986; ENSG00000119912 ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2] |
GeneIDi | 3416 |
KEGGi | hsa:3416 |
MANE-Selecti | ENST00000265986.11; ENSP00000265986.6; NM_004969.4; NP_004960.2 |
UCSCi | uc001kia.4, human [P14735-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
CCDSi | CCDS53554.1 [P14735-2] CCDS7421.1 [P14735-1] |
PIRi | A40119, SNHUIN |
RefSeqi | NP_001159418.1, NM_001165946.1 [P14735-2] NP_004960.2, NM_004969.3 [P14735-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2G47 | X-ray | 2.10 | A/B | 42-1019 | [»] | |
2G48 | X-ray | 2.60 | A/B | 42-1019 | [»] | |
2G49 | X-ray | 2.50 | A/B | 42-1019 | [»] | |
2G54 | X-ray | 2.25 | A/B | 42-1019 | [»] | |
2G56 | X-ray | 2.20 | A/B | 42-1019 | [»] | |
2JBU | X-ray | 3.00 | A/B | 42-1019 | [»] | |
2JG4 | X-ray | 2.80 | A/B | 43-1019 | [»] | |
2WBY | X-ray | 2.60 | A/B | 42-1019 | [»] | |
2WC0 | X-ray | 2.80 | A/B | 42-1019 | [»] | |
2WK3 | X-ray | 2.59 | A/B | 1-1019 | [»] | |
2YPU | X-ray | 2.80 | A/B | 42-1019 | [»] | |
3CWW | X-ray | 1.96 | A/B | 42-1019 | [»] | |
3E4A | X-ray | 2.60 | A/B | 1-1019 | [»] | |
3E4Z | X-ray | 2.28 | A/B | 42-1019 | [»] | |
3E50 | X-ray | 2.30 | A/B | 42-1019 | [»] | |
3H44 | X-ray | 3.00 | A/B | 42-1019 | [»] | |
3HGZ | X-ray | 2.91 | A/B | 43-1011 | [»] | |
3N56 | X-ray | 3.10 | A/B | 42-1019 | [»] | |
3N57 | X-ray | 3.03 | A/B | 42-1019 | [»] | |
3OFI | X-ray | 2.35 | A/B | 42-1019 | [»] | |
3QZ2 | X-ray | 3.20 | A/B | 42-1019 | [»] | |
4DTT | X-ray | 3.22 | A/B | 42-1019 | [»] | |
4DWK | X-ray | 3.00 | A/B | 42-1019 | [»] | |
4GS8 | X-ray | 2.99 | A/B | 42-1019 | [»] | |
4GSC | X-ray | 2.81 | A/B | 42-1019 | [»] | |
4GSF | X-ray | 2.70 | A/B | 42-1019 | [»] | |
4IFH | X-ray | 3.29 | A/B | 42-1019 | [»] | |
4IOF | X-ray | 3.35 | A/B | 42-1019 | [»] | |
4LTE | X-ray | 2.70 | A/B | 42-1019 | [»] | |
4M1C | X-ray | 3.50 | A/B | 42-1019 | [»] | |
4NXO | X-ray | 2.73 | A/B | 42-1019 | [»] | |
4PES | X-ray | 2.21 | A/B | 42-1019 | [»] | |
4PF7 | X-ray | 2.33 | A/B | 42-1019 | [»] | |
4PF9 | X-ray | 2.50 | A/B | 42-1019 | [»] | |
4PFC | X-ray | 2.21 | A/B | 42-1019 | [»] | |
4QIA | X-ray | 3.20 | A/B | 42-1019 | [»] | |
4RAL | X-ray | 3.15 | A/B | 42-1019 | [»] | |
4RE9 | X-ray | 2.91 | A/B | 42-1019 | [»] | |
5CJO | X-ray | 3.29 | A | 42-1019 | [»] | |
5UOE | X-ray | 3.80 | A/B/C/D/E | 42-1019 | [»] | |
5WOB | X-ray | 3.95 | A/B/C/D/E/F/G/H | 42-1019 | [»] | |
6B3Q | electron microscopy | 3.70 | A/B | 42-1019 | [»] | |
6B70 | electron microscopy | 3.70 | A/B | 46-1011 | [»] | |
6B7Y | electron microscopy | 6.50 | A/B | 46-1011 | [»] | |
6B7Z | electron microscopy | 6.50 | A/B | 46-1011 | [»] | |
6BF6 | electron microscopy | 6.50 | A/B | 46-1011 | [»] | |
6BF7 | electron microscopy | 6.50 | A/B | 46-1011 | [»] | |
6BF8 | electron microscopy | 4.20 | A/B | 46-1011 | [»] | |
6BF9 | electron microscopy | 7.20 | A/B | 46-1011 | [»] | |
6BFC | electron microscopy | 3.70 | A/B | 46-1011 | [»] | |
6BYZ | X-ray | 2.96 | A/B | 1-1019 | [»] | |
6EDS | X-ray | 3.18 | A/B | 42-1019 | [»] | |
6MQ3 | X-ray | 3.57 | A/B | 42-1019 | [»] | |
7K1D | X-ray | 3.00 | A/B | 42-1019 | [»] | |
7K1E | X-ray | 2.80 | A/B | 42-1019 | [»] | |
7K1F | X-ray | 2.60 | A/B | 42-1019 | [»] | |
SMRi | P14735 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109642, 147 interactors |
DIPi | DIP-55771N |
IntActi | P14735, 68 interactors |
MINTi | P14735 |
STRINGi | 9606.ENSP00000265986 |
Chemistry databases
BindingDBi | P14735 |
ChEMBLi | CHEMBL1293287 |
DrugBanki | DB00626, Bacitracin DB00030, Insulin human DB00071, Insulin pork DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form |
DrugCentrali | P14735 |
GuidetoPHARMACOLOGYi | 2371 |
Protein family/group databases
MEROPSi | M16.002 |
PTM databases
GlyGeni | P14735, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P14735 |
MetOSitei | P14735 |
PhosphoSitePlusi | P14735 |
Genetic variation databases
BioMutai | IDE |
DMDMi | 215274252 |
Proteomic databases
EPDi | P14735 |
jPOSTi | P14735 |
MassIVEi | P14735 |
MaxQBi | P14735 |
PaxDbi | P14735 |
PeptideAtlasi | P14735 |
PRIDEi | P14735 |
ProteomicsDBi | 53079 [P14735-1] 7086 |
Protocols and materials databases
ABCDi | P14735, 3 sequenced antibodies |
Antibodypediai | 3227, 522 antibodies from 46 providers |
DNASUi | 3416 |
Genome annotation databases
Ensembli | ENST00000265986; ENSP00000265986; ENSG00000119912 ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2] |
GeneIDi | 3416 |
KEGGi | hsa:3416 |
MANE-Selecti | ENST00000265986.11; ENSP00000265986.6; NM_004969.4; NP_004960.2 |
UCSCi | uc001kia.4, human [P14735-1] |
Organism-specific databases
CTDi | 3416 |
DisGeNETi | 3416 |
GeneCardsi | IDE |
HGNCi | HGNC:5381, IDE |
HPAi | ENSG00000119912, Low tissue specificity |
MIMi | 146680, gene |
neXtProti | NX_P14735 |
OpenTargetsi | ENSG00000119912 |
PharmGKBi | PA29629 |
VEuPathDBi | HostDB:ENSG00000119912 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0959, Eukaryota |
GeneTreei | ENSGT00940000155780 |
HOGENOMi | CLU_004639_1_1_1 |
InParanoidi | P14735 |
OMAi | WIFDEMK |
OrthoDBi | 1008844at2759 |
PhylomeDBi | P14735 |
TreeFami | TF106275 |
Enzyme and pathway databases
BRENDAi | 3.4.24.56, 2681 |
PathwayCommonsi | P14735 |
Reactomei | R-HSA-5689880, Ub-specific processing proteases R-HSA-9033241, Peroxisomal protein import |
SignaLinki | P14735 |
SIGNORi | P14735 |
Miscellaneous databases
BioGRID-ORCSi | 3416, 7 hits in 1056 CRISPR screens |
ChiTaRSi | IDE, human |
EvolutionaryTracei | P14735 |
GeneWikii | Insulin-degrading_enzyme |
GenomeRNAii | 3416 |
Pharosi | P14735, Tchem |
PROi | PR:P14735 |
RNActi | P14735, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000119912, Expressed in hair follicle and 232 other tissues |
ExpressionAtlasi | P14735, baseline and differential |
Genevisiblei | P14735, HS |
Family and domain databases
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 |
Pfami | View protein in Pfam PF00675, Peptidase_M16, 1 hit PF05193, Peptidase_M16_C, 2 hits PF16187, Peptidase_M16_M, 1 hit |
SUPFAMi | SSF63411, SSF63411, 4 hits |
PROSITEi | View protein in PROSITE PS00143, INSULINASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | IDE_HUMAN | |
Accessioni | P14735Primary (citable) accession number: P14735 Secondary accession number(s): B2R721 Q5T5N2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | November 25, 2008 | |
Last modified: | February 23, 2022 | |
This is version 215 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families