HUMAN:IDE

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	IDE
Protein Name(s)	Insulin-degrading enzyme Abeta-degrading protease Insulin protease Insulinase Insulysin
External Links
UniProt	P14735
EMBL	M21188 AK312810 AK316407 AL356128 CH471066 CH471066 BC096336 BC096337 BC096339
CCDS	CCDS53554.1 CCDS7421.1
PIR	A40119
RefSeq	NP_001159418.1 NP_004960.2
UniGene	Hs.500546
PDB	2G47 2G48 2G49 2G54 2G56 2JBU 2JG4 2WBY 2WC0 2WK3 2YPU 3CWW 3E4A 3E4Z 3E50 3H44 3HGZ 3N56 3N57 3OFI 3QZ2 4DTT 4DWK 4GS8 4GSC 4GSF 4IFH 4IOF 4LTE 4M1C 4QLD
PDBsum	2G47 2G48 2G49 2G54 2G56 2JBU 2JG4 2WBY 2WC0 2WK3 2YPU 3CWW 3E4A 3E4Z 3E50 3H44 3HGZ 3N56 3N57 3OFI 3QZ2 4DTT 4DWK 4GS8 4GSC 4GSF 4IFH 4IOF 4LTE 4M1C 4QLD
ProteinModelPortal	P14735
SMR	P14735
BioGrid	109642
DIP	DIP-55771N
IntAct	P14735
MINT	MINT-2801173
STRING	9606.ENSP00000265986
BindingDB	P14735
ChEMBL	CHEMBL1293287
DrugBank	DB00071 DB00626 DB00030
MEROPS	M16.002
PhosphoSite	P14735
DMDM	215274252
MaxQB	P14735
PaxDb	P14735
PRIDE	P14735
Ensembl	ENST00000265986 ENST00000371581
GeneID	3416
KEGG	hsa:3416
UCSC	uc001kia.3 uc010qnp.2
CTD	3416
GeneCards	GC10M094211
H-InvDB	HIX0009042
HGNC	HGNC:5381
HPA	CAB012303
MIM	146680
neXtProt	NX_P14735
PharmGKB	PA29629
eggNOG	COG1025
GeneTree	ENSGT00530000063327
HOGENOM	HOG000161331
HOVERGEN	HBG106799
InParanoid	P14735
KO	K01408
OMA	QPRKQLK
OrthoDB	EOG7HHWRD
PhylomeDB	P14735
TreeFam	TF106275
SignaLink	P14735
EvolutionaryTrace	P14735
GeneWiki	Insulin-degrading_enzyme
GenomeRNAi	3416
NextBio	13466
PRO	PR:P14735
Proteomes	UP000005640
Bgee	P14735
CleanEx	HS_IDE
ExpressionAtlas	P14735
Genevestigator	P14735
GO	GO:0009986 GO:0005737 GO:0005829 GO:0031597 GO:0005615 GO:0005739 GO:0005634 GO:0005782 GO:0005777 GO:0005886 GO:0005524 GO:0016887 GO:0001540 GO:0031626 GO:0001948 GO:0043559 GO:0004222 GO:0042277 GO:0042803 GO:0005102 GO:0043130 GO:0008270 GO:0050435 GO:0010815 GO:0008340 GO:0042447 GO:1901143 GO:1901142 GO:0008286 GO:0045861 GO:0032461 GO:0051291 GO:0051260 GO:0051289 GO:0006508 GO:0051603 GO:0010992 GO:0016032
Gene3D	3.30.830.10
InterPro	IPR011249 IPR011237 IPR011765 IPR001431 IPR007863
Pfam	PF00675 PF05193
SUPFAM	SSF63411
PROSITE	PS00143

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0070062	extracellular exosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHR7	C	produced_by:(CL:0000129)	Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHR7	P	has_agent:(CL:0000129) occurs_in:(GO:0005615) has_input:(UniProtKB:P05067:PRO_0000000092)	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9JHR7	P	has_agent:(CL:0000129) occurs_in:(GO:0005615) part_of:(GO:0097242) has_input:(UniProtKB:P05067:PRO_0000000093)	Seeded From UniProt	complete
involved_in	GO:1903715	regulation of aerobic respiration	PMID:23525105^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P05067	P	regulates_o_occurs_in:(GO:0005739)	Seeded From UniProt	complete
involved_in	GO:0150094	amyloid-beta clearance by cellular catabolic process	PMID:23525105^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P05067:PRO_0000000093) occurs_in:(GO:0005739)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:23525105^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23525105^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	PMID:16511862^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(CL:0002139) part_of:(CL:1001602) part_of:(GO:0009986)	Seeded From UniProt	complete
part_of	GO:0009897	external side of plasma membrane	PMID:16511862^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002139) part_of:(CL:1001602) part_of:(GO:0009986) part_of:(GO:0016323)	Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:16511862^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002139) part_of:(CL:1001602)	Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	PMID:16511862^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002139) occurs_in:(CL:1001602)	Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35559	C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35559	C	adjacent_to:(CL:0000129)	Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	PMID:10684867^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:26968463^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	PMID:19321446^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:19321446^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1901143	insulin catabolic process	PMID:19321446^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19321446^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0150094	amyloid-beta clearance by cellular catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35559	P	occurs_in:(CL:0000129)	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:18602473^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P05067:PRO_0000000093)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:20364150^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	PMID:20364150^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043171	peptide catabolic process	PMID:20364150^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019885	antigen processing and presentation of endogenous peptide antigen via MHC class I	PMID:20364150^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004175	endopeptidase activity	PMID:20364150^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35559	P	occurs_in:(UBERON:0001950) occurs_in:(GO:0005615)	Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P35559	P	has_start_location:(CL:0002609) has_target_end_location:(GO:0005576) has_target_start_location:(GO:0005576)	Seeded From UniProt	complete
involved_in	GO:1901143	insulin catabolic process	PMID:9231799^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901143	insulin catabolic process	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901142	insulin metabolic process	PMID:18448515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P05067)\|has_input:(UniProtKB:P01308)	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:17051221^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0000129)	Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043559	insulin binding	PMID:20082125^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
enables	GO:0043559	insulin binding	PMID:17051221^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0140036	ubiquitin-dependent protein binding	PMID:21185309^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0CG48	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:20082125^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P51460	F		Seeded From UniProt	complete
involved_in	GO:0032461	positive regulation of protein oligomerization	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P05067)	Seeded From UniProt	complete
involved_in	GO:0010992	ubiquitin recycling	PMID:21185309^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010815	bradykinin catabolic process	PMID:21185309^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010815	bradykinin catabolic process	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:17055432^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008340	determination of adult lifespan	PMID:18448515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008286	insulin receptor signaling pathway	PMID:3059494^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:21185309^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P0CG48)	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:20082125^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P51460)\|has_direct_input:(UniProtKB:P01308)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15285718^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005777	peroxisome	PMID:9231799^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15285718^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9231799^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:18226493^[18]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002609)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15285718^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9231799^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
NOT\|part_of	GO:0005634	nucleus	PMID:18226493^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:9830016^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000129)	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:20178365^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P50542	F		Seeded From UniProt	complete
enables	GO:0004222	metalloendopeptidase activity	PMID:17051221^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P01275)\|has_direct_input:(UniProtKB:P05067)	Seeded From UniProt	complete
enables	GO:0004222	metalloendopeptidase activity	PMID:17613531^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000220551 RGD:2861 UniProtKB:P14735	P		Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000932752 RGD:2861 UniProtKB:P14735	P		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000932752 RGD:2861	P		Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000220589 RGD:2861	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[20]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000220551 UniProtKB:P14735	C		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0001618	P		Seeded From UniProt	complete
involved_in	GO:0150094	amyloid-beta clearance by cellular catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0097242	amyloid-beta clearance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0045861	negative regulation of proteolysis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
involved_in	GO:0044257	cellular protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
enables	GO:0043559	insulin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	P		Seeded From UniProt	complete
enables	GO:0031626	beta-endorphin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
part_of	GO:0031597	cytosolic proteasome complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	C		Seeded From UniProt	complete
enables	GO:0017046	peptide hormone binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	C		Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
enables	GO:0004222	metalloendopeptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
enables	GO:0001540	amyloid-beta binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35559 ensembl:ENSRNOP00000023342	F		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011249	F		Seeded From UniProt	complete
enables	GO:0004222	metalloendopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001431	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001431	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011249	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24847884^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14735-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17051221^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14735-1	F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:10684867^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	adjacent_to:(CL:0000129)\|part_of(UBERON:0001359)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:10684867^[3] Reactome:R-HSA-9033236 Reactome:R-HSA-9033235	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005777	peroxisome	PMID:10684867^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004222	metalloendopeptidase activity	PMID:10684867^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(UniProtKB:P01308)\|has_input:(UniProtKB:P01275)\|has_input:(UniProtKB:P05067:PRO_0000000093)\|has_input:(UniProtKB:P05067:PRO_0000000092)	Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:22383525^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_agent:(CL:0000127) has_regulation_target:(UniProtKB:P05067:PRO_0000000092)	Seeded From UniProt	complete
involved_in	GO:0006625	protein targeting to peroxisome	Reactome:R-HSA-9033241	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	Reactome:R-HSA-9033235	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	F		Seeded From UniProt	complete
enables	GO:0001618	virus receptor activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1183	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0021	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0482	F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Leal, MC et al. (2013) Transcriptional regulation of insulin-degrading enzyme modulates mitochondrial amyloid β (Aβ) peptide catabolism and functionality. J. Biol. Chem. 288 12920-31 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Lynch, JA et al. (2006) Insulin degrading enzyme is localized predominantly at the cell surface of polarized and unpolarized human cerebrovascular endothelial cell cultures. J. Neurosci. Res. 83 1262-70 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Vekrellis, K et al. (2000) Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20 1657-65 PubMed GONUTS page
↑ Hubin, E et al. (2016) Characterization of insulin-degrading enzyme-mediated cleavage of Aβ in distinct aggregation states. Biochim. Biophys. Acta 1860 1281-90 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Manolopoulou, M et al. (2009) Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme. J. Biol. Chem. 284 14177-88 PubMed GONUTS page
↑ Betts, V et al. (2008) Aggregation and catabolism of disease-associated intra-Abeta mutations: reduced proteolysis of AbetaA21G by neprilysin. Neurobiol. Dis. 31 442-50 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Parmentier, N et al. (2010) Production of an antigenic peptide by insulin-degrading enzyme. Nat. Immunol. 11 449-54 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Chesneau, V et al. (1997) Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation. Endocrinology 138 3444-51 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Qiu, WQ et al. (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 273 32730-8 PubMed GONUTS page
↑ ^10.0 ^10.1 Hong, MG et al. (2008) Evidence that the gene encoding insulin degrading enzyme influences human lifespan. Hum. Mol. Genet. 17 2370-8 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Shen, Y et al. (2006) Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 443 870-4 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 Im, H et al. (2007) Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. J. Biol. Chem. 282 25453-63 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Zhang, WJ et al. (2010) In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme. Protein J. 29 93-8 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Ralat, LA et al. (2011) Ubiquitin is a novel substrate for human insulin-degrading enzyme. J. Mol. Biol. 406 454-66 PubMed GONUTS page
↑ Li, Q et al. (2006) Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread. Cell 127 305-16 PubMed GONUTS page
↑ Affholter, JA et al. (1988) Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242 1415-8 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Leissring, MA et al. (2004) Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem. J. 383 439-46 PubMed GONUTS page
↑ ^18.0 ^18.1 Bernstein, HG et al. (2008) Regional and cellular distribution patterns of insulin-degrading enzyme in the adult human brain and pituitary. J. Chem. Neuroanat. 35 216-24 PubMed GONUTS page
↑ Ghosh, D & Berg, JM (2010) A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities. J. Am. Chem. Soc. 132 3973-9 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Maianti, JP et al. (2014) Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones. Nature 511 94-8 PubMed GONUTS page
↑ Basak, JM et al. (2012) Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Aβ uptake and degradation by astrocytes. J. Biol. Chem. 287 13959-71 PubMed GONUTS page

[PMID:23525105-1] 1.0 ^1.1 ^1.2 ^1.3 Leal, MC et al. (2013) Transcriptional regulation of insulin-degrading enzyme modulates mitochondrial amyloid β (Aβ) peptide catabolism and functionality. J. Biol. Chem. 288 12920-31 PubMed GONUTS page

[PMID:16511862-2] 2.0 ^2.1 ^2.2 ^2.3 Lynch, JA et al. (2006) Insulin degrading enzyme is localized predominantly at the cell surface of polarized and unpolarized human cerebrovascular endothelial cell cultures. J. Neurosci. Res. 83 1262-70 PubMed GONUTS page

[PMID:10684867-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Vekrellis, K et al. (2000) Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20 1657-65 PubMed GONUTS page

[PMID:26968463-4] Hubin, E et al. (2016) Characterization of insulin-degrading enzyme-mediated cleavage of Aβ in distinct aggregation states. Biochim. Biophys. Acta 1860 1281-90 PubMed GONUTS page

[PMID:19321446-5] 5.0 ^5.1 ^5.2 ^5.3 Manolopoulou, M et al. (2009) Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme. J. Biol. Chem. 284 14177-88 PubMed GONUTS page

[PMID:18602473-6] Betts, V et al. (2008) Aggregation and catabolism of disease-associated intra-Abeta mutations: reduced proteolysis of AbetaA21G by neprilysin. Neurobiol. Dis. 31 442-50 PubMed GONUTS page

[PMID:20364150-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Parmentier, N et al. (2010) Production of an antigenic peptide by insulin-degrading enzyme. Nat. Immunol. 11 449-54 PubMed GONUTS page

[PMID:9231799-8] 8.0 ^8.1 ^8.2 ^8.3 Chesneau, V et al. (1997) Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation. Endocrinology 138 3444-51 PubMed GONUTS page

[PMID:9830016-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Qiu, WQ et al. (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 273 32730-8 PubMed GONUTS page

[PMID:18448515-10] 10.0 ^10.1 Hong, MG et al. (2008) Evidence that the gene encoding insulin degrading enzyme influences human lifespan. Hum. Mol. Genet. 17 2370-8 PubMed GONUTS page

[PMID:17051221-11] 11.0 ^11.1 ^11.2 ^11.3 Shen, Y et al. (2006) Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 443 870-4 PubMed GONUTS page

[PMID:17613531-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 Im, H et al. (2007) Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE. J. Biol. Chem. 282 25453-63 PubMed GONUTS page

[PMID:20082125-13] 13.0 ^13.1 ^13.2 Zhang, WJ et al. (2010) In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme. Protein J. 29 93-8 PubMed GONUTS page

[PMID:21185309-14] 14.0 ^14.1 ^14.2 ^14.3 Ralat, LA et al. (2011) Ubiquitin is a novel substrate for human insulin-degrading enzyme. J. Mol. Biol. 406 454-66 PubMed GONUTS page

[PMID:17055432-15] Li, Q et al. (2006) Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread. Cell 127 305-16 PubMed GONUTS page

[PMID:3059494-16] Affholter, JA et al. (1988) Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242 1415-8 PubMed GONUTS page

[PMID:15285718-17] 17.0 ^17.1 ^17.2 Leissring, MA et al. (2004) Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem. J. 383 439-46 PubMed GONUTS page

[PMID:18226493-18] 18.0 ^18.1 Bernstein, HG et al. (2008) Regional and cellular distribution patterns of insulin-degrading enzyme in the adult human brain and pituitary. J. Chem. Neuroanat. 35 216-24 PubMed GONUTS page

[PMID:20178365-19] Ghosh, D & Berg, JM (2010) A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities. J. Am. Chem. Soc. 132 3973-9 PubMed GONUTS page

[PMID:21873635-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:24847884-21] Maianti, JP et al. (2014) Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones. Nature 511 94-8 PubMed GONUTS page

[PMID:22383525-22] Basak, JM et al. (2012) Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of Aβ uptake and degradation by astrocytes. J. Biol. Chem. 287 13959-71 PubMed GONUTS page

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