UniProtKB - P14735 (IDE_HUMAN)
Protein
Insulin-degrading enzyme
Gene
IDE
Organism
Homo sapiens (Human)
Status
Functioni
Plays a role in the cellular breakdown of insulin, APP peptides, IAPP 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). 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). 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 Publication13 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.1 Publication
Catalytic activityi
- Degradation of insulin, glucagon and other polypeptides. No action on proteins.10 Publications EC:3.4.24.56
Cofactori
Zn2+5 PublicationsNote: Binds 1 zinc ion per subunit.5 Publications
Activity regulationi
Activated by small peptides (By similarity). Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi (PubMed:17613531). Inhibited by bacitracin (PubMed:17055432, PubMed:17613531). In vitro modification of Cys residues impairs enzyme activity (PubMed:18986166).By similarity3 Publications
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
- amyloid-beta binding Source: Ensembl
- ATPase activity Source: Ensembl
- ATP binding Source: UniProtKB
- beta-endorphin binding Source: Ensembl
- 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
- negative regulation of proteolysis Source: Ensembl
- peptide catabolic process Source: UniProtKB
- positive regulation of protein catabolic process Source: ARUK-UCL
- positive regulation of protein oligomerization Source: UniProtKB
- protein catabolic process Source: ARUK-UCL
- protein heterooligomerization Source: Ensembl
- protein homooligomerization Source: UniProtKB
- protein homotetramerization Source: Ensembl
- protein targeting to peroxisome Source: Reactome
- 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 |
Reactomei | R-HSA-5689880 Ub-specific processing proteases R-HSA-9033241 Peroxisomal protein import |
SignaLinki | P14735 |
Protein family/group databases
MEROPSi | M16.982 |
Names & Taxonomyi
Protein namesi | Recommended name: Insulin-degrading enzyme1 Publication (EC:3.4.24.563 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 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity
Extracellular region or secreted
- Secreted 1 Publication
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
- cytosolic proteasome complex Source: Ensembl
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 Source: GOC
- 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. 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 |
Chemistry databases
ChEMBLi | CHEMBL1293287 |
DrugBanki | DB00626 Bacitracin DB00030 Insulin Human DB00071 Insulin Pork DB01593 Zinc DB14487 Zinc acetate DB14533 Zinc chloride |
DrugCentrali | P14735 |
GuidetoPHARMACOLOGYi | 2371 |
Polymorphism and mutation 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
The N-terminus is blocked.
Proteomic databases
EPDi | P14735 |
jPOSTi | P14735 |
MassIVEi | P14735 |
MaxQBi | P14735 |
PaxDbi | P14735 |
PeptideAtlasi | P14735 |
PRIDEi | P14735 |
ProteomicsDBi | 53079 [P14735-1] 7086 |
PTM databases
iPTMneti | P14735 |
PhosphoSitePlusi | P14735 |
Expressioni
Tissue specificityi
Detected in brain and in cerebrospinal fluid (at protein level).1 Publication
Gene expression databases
Bgeei | ENSG00000119912 Expressed in 218 organ(s), highest expression level in hair follicle |
ExpressionAtlasi | P14735 baseline and differential |
Genevisiblei | P14735 HS |
Organism-specific databases
HPAi | HPA063478 |
Interactioni
Subunit structurei
Binary interactionsi
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, 92 interactors |
DIPi | DIP-55771N |
IntActi | P14735, 64 interactors |
MINTi | P14735 |
STRINGi | 9606.ENSP00000265986 |
Chemistry databases
BindingDBi | P14735 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D 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
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
eggNOGi | KOG0959 Eukaryota COG1025 LUCA |
GeneTreei | ENSGT00940000155780 |
HOGENOMi | HOG000161331 |
InParanoidi | P14735 |
KOi | K01408 |
OMAi | HGNLYKE |
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 3 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 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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3ISG5 | A0A3B3ISG5_HUMAN | Insulin-degrading enzyme | IDE | 1,019 | Annotation score: | ||
Q5T5N3 | Q5T5N3_HUMAN | Insulin-degrading enzyme | IDE | 257 | Annotation score: | ||
R4GN65 | R4GN65_HUMAN | Insulin-degrading enzyme | IDE | 61 | Annotation score: |
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 [P14735-1] ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2] |
GeneIDi | 3416 |
KEGGi | hsa:3416 |
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 | [»] | |
SMRi | P14735 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 109642, 92 interactors |
DIPi | DIP-55771N |
IntActi | P14735, 64 interactors |
MINTi | P14735 |
STRINGi | 9606.ENSP00000265986 |
Chemistry databases
BindingDBi | P14735 |
ChEMBLi | CHEMBL1293287 |
DrugBanki | DB00626 Bacitracin DB00030 Insulin Human DB00071 Insulin Pork DB01593 Zinc DB14487 Zinc acetate DB14533 Zinc chloride |
DrugCentrali | P14735 |
GuidetoPHARMACOLOGYi | 2371 |
Protein family/group databases
MEROPSi | M16.982 |
PTM databases
iPTMneti | P14735 |
PhosphoSitePlusi | P14735 |
Polymorphism and mutation 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 |
Genome annotation databases
Ensembli | ENST00000265986; ENSP00000265986; ENSG00000119912 [P14735-1] ENST00000371581; ENSP00000360637; ENSG00000119912 [P14735-2] |
GeneIDi | 3416 |
KEGGi | hsa:3416 |
UCSCi | uc001kia.4 human [P14735-1] |
Organism-specific databases
CTDi | 3416 |
DisGeNETi | 3416 |
GeneCardsi | IDE |
HGNCi | HGNC:5381 IDE |
HPAi | HPA063478 |
MIMi | 146680 gene |
neXtProti | NX_P14735 |
OpenTargetsi | ENSG00000119912 |
PharmGKBi | PA29629 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0959 Eukaryota COG1025 LUCA |
GeneTreei | ENSGT00940000155780 |
HOGENOMi | HOG000161331 |
InParanoidi | P14735 |
KOi | K01408 |
OMAi | HGNLYKE |
OrthoDBi | 1008844at2759 |
PhylomeDBi | P14735 |
TreeFami | TF106275 |
Enzyme and pathway databases
BRENDAi | 3.4.24.56 2681 |
Reactomei | R-HSA-5689880 Ub-specific processing proteases R-HSA-9033241 Peroxisomal protein import |
SignaLinki | P14735 |
Miscellaneous databases
ChiTaRSi | IDE human |
EvolutionaryTracei | P14735 |
GeneWikii | Insulin-degrading_enzyme |
GenomeRNAii | 3416 |
Pharosi | P14735 |
PROi | PR:P14735 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000119912 Expressed in 218 organ(s), highest expression level in hair follicle |
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 |
ProtoNeti | Search... |
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: | November 13, 2019 | |
This is version 203 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, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families - 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