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 Publications

Miscellaneous

ATP-binding induces a conformation change.1 Publication

Catalytic activityⁱ

Degradation of insulin, glucagon and other polypeptides. No action on proteins.
11 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes."
  Affholter J.A., Hsieh C.L., Francke U., Roth R.A.
  Mol. Endocrinol. 4:1125-1135(1990) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, FUNCTION, CATALYTIC ACTIVITY.
- Ref.8
  "Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme."
  Vekrellis K., Ye Z., Qiu W.Q., Walsh D., Hartley D., Chesneau V., Rosner M.R., Selkoe D.J.
  J. Neurosci. 20:1657-1665(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-111, ACTIVE SITE.
- Ref.14
  "Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism."
  Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.
  Nature 443:870-874(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-1019 OF MUTANT GLN-111 IN COMPLEXES WITH ZINC IONS; IAPP; INSULIN; AMYLOID AND GLUCAGON, MUTAGENESIS OF GLU-111; SER-132; ASN-184; ASP-426; GLU-817; GLN-828 AND LYS-899, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, SUBUNIT.
- Ref.15
  "Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE."
  Im H., Manolopoulou M., Malito E., Shen Y., Zhao J., Neant-Fery M., Sun C.-Y., Meredith S.C., Sisodia S.S., Leissring M.A., Tang W.-J.
  J. Biol. Chem. 282:25453-25463(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 43-1018 OF MUTANT PHE-831 IN COMPLEX WITH ZINC IONS AND SUBSTRATE PEPTIDE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ATP-BINDING, SUBUNIT, MUTAGENESIS OF ASP-426 AND LYS-899, FUNCTION.
- Ref.16
  "Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme."
  Malito E., Ralat L.A., Manolopoulou M., Tsay J.L., Wadlington N.L., Tang W.-J.
  Biochemistry 47:12822-12834(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 42-1019 OF MUTANT GLN-111 IN COMPLEX WITH BRADYKININ AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.17
  "Molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme."
  Manolopoulou M., Guo Q., Malito E., Schilling A.B., Tang W.J.
  J. Biol. Chem. 284:14177-14188(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 42-1019 IN COMPLEX WITH INSULIN AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF GLU-111, ACTIVE SITE.
- Ref.18
  "Insulin-degrading enzyme modulates the natriuretic peptide-mediated signaling response."
  Ralat L.A., Guo Q., Ren M., Funke T., Dickey D.M., Potter L.R., Tang W.J.
  J. Biol. Chem. 286:4670-4679(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 42-1019 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ARG-767.
- Ref.19
  "Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme."
  McCord L.A., Liang W.G., Dowdell E., Kalas V., Hoey R.J., Koide A., Koide S., Tang W.J.
  Proc. Natl. Acad. Sci. U.S.A. 110:13827-13832(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 42-1019 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PRO-286; 366-GLY--GLY-369; TYR-496; PHE-530 AND ARG-767, ACTIVE SITE.
- Ref.20
  "Anti-diabetic activity of insulin-degrading enzyme inhibitors mediated by multiple hormones."
  Maianti J.P., McFedries A., Foda Z.H., Kleiner R.E., Du X.Q., Leissring M.A., Tang W.J., Charron M.J., Seeliger M.A., Saghatelian A., Liu D.R.
  Nature 511:94-98(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 42-1019 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION.
- Ref.21
  "Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice."
  Deprez-Poulain R., Hennuyer N., Bosc D., Liang W.G., Enee E., Marechal X., Charton J., Totobenazara J., Berte G., Jahklal J., Verdelet T., Dumont J., Dassonneville S., Woitrain E., Gauriot M., Paquet C., Duplan I., Hermant P.
  Deprez B.
  Nat. Commun. 6:8250-8250(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 42-1019 IN COMPLEX WITH ZINC AND SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
- Ref.22
  "Ensemble cryoEM elucidates the mechanism of insulin capture and degradation by human insulin degrading enzyme."
  Zhang Z., Liang W.G., Bailey L.J., Tan Y.Z., Wei H., Wang A., Farcasanu M., Woods V.A., McCord L.A., Lee D., Shang W., Deprez-Poulain R., Deprez B., Liu D.R., Koide A., Koide S., Kossiakoff A.A., Li S.
  , Carragher B., Potter C.S., Tang W.J.
  Elife 7:0-0(2018) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 42-1019 IN COMPLEX WITH INSULIN, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
EC:3.4.24.56

Cofactorⁱ

Zn²⁺6 PublicationsNote: Binds 1 zinc ion per subunit.6 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	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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

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

MEROPS protease database More...MEROPSⁱ	M16.002

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	Name:IDE1 PublicationImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:5381, IDE
MIMⁱ	146680, gene
neXtProtⁱ	NX_P14735
VEuPathDBⁱ	HostDB:ENSG00000119912.15

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

DisGeNET More...DisGeNETⁱ	3416
Open Targets More...OpenTargetsⁱ	ENSG00000119912
PharmGKBⁱ	PA29629

Miscellaneous databases

Pharosⁱ	P14735, Tchem

Pharosⁱ

P14735, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL1293287
Drug and drug target database More...DrugBankⁱ	DB00626, Bacitracin DB00030, Insulin human DB00071, Insulin pork DB14487, Zinc acetate DB14533, Zinc chloride DB14548, Zinc sulfate, unspecified form
DrugCentral More...DrugCentralⁱ	P14735
IUPHAR/BPS Guide to PHARMACOLOGY More...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

The N-terminus is blocked.

Proteomic databases

EPDⁱ	P14735
jPOSTⁱ	P14735
MassIVEⁱ	P14735
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P14735
PaxDbⁱ	P14735
PeptideAtlas More...PeptideAtlasⁱ	P14735
PRIDEⁱ	P14735
ProteomicsDBⁱ	53079 [P14735-1] 7086

PTM databases

iPTMnetⁱ	P14735
MetOSiteⁱ	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 hair follicle and 231 other tissues
ExpressionAtlasⁱ	P14735, baseline and differential
Genevisibleⁱ	P14735, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000119912, Low tissue specificity

HPAⁱ

ENSG00000119912, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:17051221, PubMed:19321446, PubMed:23922390, PubMed:26394692, PubMed:29596046) (Probable). Can also form homotetramers (By similarity).

By similarity1 Publication5 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

Hide details

P14735

With	#Exp.	IntAct
APP [P05067]	3	EBI-2556886,EBI-77613
CCL3 [P10147]	3	EBI-2556886,EBI-8459634

IDE - isoform 1 [P14735-1]

With	#Exp.	IntAct
Amyloid-beta protein 40 (PRO_0000000093)	3	EBI-15607031,EBI-2431589
GCG [P01275]	3	EBI-15607031,EBI-7629173
IAPP [P10997]	3	EBI-15607031,EBI-8526679
itself	2	EBI-15607031,EBI-15607031
INS [P01308]	3	EBI-15607031,EBI-7090529
gE [Q9J3M8] from Varicella-zoster virus (strain Oka vaccine).	2	EBI-15607031,EBI-2532305

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	109642, 111 interactors
Database of interacting proteins More...DIPⁱ	DIP-55771N
IntActⁱ	P14735, 68 interactors
Molecular INTeraction database More...MINTⁱ	P14735
STRINGⁱ	9606.ENSP00000265986

Chemistry databases

BindingDBⁱ

P14735

Miscellaneous databases

RNActⁱ	P14735, protein

RNActⁱ

P14735, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	47 – 50	Combined sources	4
Beta strandⁱ	63 – 69	Combined sources	7
Beta strandⁱ	74 – 79	Combined sources	6
Beta strandⁱ	84 – 93	Combined sources	10
Helixⁱ	96 – 98	Combined sources	3
Beta strandⁱ	101 – 103	Combined sources	3
Helixⁱ	106 – 113	Combined sources	8
Helixⁱ	114 – 116	Combined sources	3
Beta strandⁱ	118 – 121	Combined sources	4
Helixⁱ	126 – 132	Combined sources	7
Turnⁱ	133 – 135	Combined sources	3
Beta strandⁱ	137 – 142	Combined sources	6
Beta strandⁱ	147 – 154	Combined sources	8
Helixⁱ	155 – 157	Combined sources	3
Helixⁱ	158 – 166	Combined sources	9
Helixⁱ	167 – 169	Combined sources	3
Helixⁱ	176 – 194	Combined sources	19
Helixⁱ	197 – 207	Combined sources	11
Helixⁱ	214 – 216	Combined sources	3
Helixⁱ	223 – 226	Combined sources	4
Helixⁱ	228 – 232	Combined sources	5
Helixⁱ	237 – 248	Combined sources	12
Helixⁱ	251 – 253	Combined sources	3
Beta strandⁱ	254 – 262	Combined sources	9
Helixⁱ	264 – 275	Combined sources	12
Beta strandⁱ	276 – 278	Combined sources	3
Helixⁱ	295 – 297	Combined sources	3
Beta strandⁱ	298 – 304	Combined sources	7
Beta strandⁱ	307 – 309	Combined sources	3
Beta strandⁱ	312 – 319	Combined sources	8
Helixⁱ	323 – 325	Combined sources	3
Turnⁱ	326 – 328	Combined sources	3
Helixⁱ	330 – 338	Combined sources	9
Helixⁱ	346 – 352	Combined sources	7
Beta strandⁱ	359 – 367	Combined sources	9
Beta strandⁱ	370 – 378	Combined sources	9
Helixⁱ	381 – 385	Combined sources	5
Helixⁱ	387 – 404	Combined sources	18
Helixⁱ	408 – 423	Combined sources	16
Helixⁱ	430 – 440	Combined sources	11
Turnⁱ	441 – 443	Combined sources	3
Helixⁱ	446 – 448	Combined sources	3
Turnⁱ	449 – 454	Combined sources	6
Helixⁱ	461 – 468	Combined sources	8
Helixⁱ	473 – 475	Combined sources	3
Beta strandⁱ	477 – 481	Combined sources	5
Helixⁱ	483 – 485	Combined sources	3
Turnⁱ	486 – 488	Combined sources	3
Turnⁱ	494 – 496	Combined sources	3
Beta strandⁱ	499 – 504	Combined sources	6
Helixⁱ	507 – 514	Combined sources	8
Beta strandⁱ	549 – 553	Combined sources	5
Beta strandⁱ	555 – 563	Combined sources	9
Beta strandⁱ	565 – 567	Combined sources	3
Beta strandⁱ	570 – 579	Combined sources	10
Helixⁱ	581 – 583	Combined sources	3
Beta strandⁱ	584 – 586	Combined sources	3
Helixⁱ	587 – 613	Combined sources	27
Beta strandⁱ	616 – 623	Combined sources	8
Beta strandⁱ	626 – 635	Combined sources	10
Helixⁱ	638 – 650	Combined sources	13
Helixⁱ	656 – 672	Combined sources	17
Helixⁱ	673 – 675	Combined sources	3
Helixⁱ	678 – 690	Combined sources	13
Beta strandⁱ	691 – 693	Combined sources	3
Helixⁱ	697 – 704	Combined sources	8
Helixⁱ	709 – 721	Combined sources	13
Beta strandⁱ	722 – 732	Combined sources	11
Helixⁱ	735 – 753	Combined sources	19
Helixⁱ	760 – 762	Combined sources	3
Beta strandⁱ	775 – 782	Combined sources	8
Beta strandⁱ	787 – 799	Combined sources	13
Helixⁱ	802 – 823	Combined sources	22
Turnⁱ	824 – 827	Combined sources	4
Beta strandⁱ	831 – 840	Combined sources	10
Beta strandⁱ	843 – 854	Combined sources	12
Helixⁱ	856 – 876	Combined sources	21
Helixⁱ	879 – 894	Combined sources	16
Helixⁱ	900 – 912	Combined sources	13
Helixⁱ	920 – 928	Combined sources	9
Helixⁱ	933 – 943	Combined sources	11
Beta strandⁱ	952 – 959	Combined sources	8
Beta strandⁱ	990 – 992	Combined sources	3
Helixⁱ	995 – 1000	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P14735
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P14735

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
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155780
HOGENOMⁱ	CLU_004639_1_1_1
InParanoidⁱ	P14735
OMAⁱ	HGNLYKE
Database of Orthologous Groups More...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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00675, Peptidase_M16, 1 hit PF05193, Peptidase_M16_C, 2 hits PF16187, Peptidase_M16_M, 1 hit
SUPFAMⁱ	SSF63411, SSF63411, 4 hits
PROSITEⁱ	View protein in PROSITE PS00143, INSULINASE, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 2 described isoforms and 15 potential isoforms that are computationally mapped.Show all Align All

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

This isoform has been chosen as the canonicalⁱ 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MSKLWFKQDD KFFLPKACLN FEFFSPFAYV DPLHCNMAYL YLELLKDSLN 
        60         70         80         90        100
EYAYAAELAG LSYDLQNTIY GMYLSVKGYN DKQPILLKKI IEKMATFEID 
       110        120        130        140        150
EKRFEIIKEA YMRSLNNFRA EQPHQHAMYY LRLLMTEVAW TKDELKEALD 
       160        170        180        190        200
DVTLPRLKAF IPQLLSRLHI EALLHGNITK QAALGIMQMV EDTLIEHAHT 
       210        220        230        240        250
KPLLPSQLVR YREVQLPDRG WFVYQQRNEV HNNCGIEIYY QTDMQSTSEN 
       260        270        280        290        300
MFLELFCQII SEPCFNTLRT KEQLGYIVFS GPRRANGIQG LRFIIQSEKP 
       310        320        330        340        350
PHYLESRVEA FLITMEKSIE DMTEEAFQKH IQALAIRRLD KPKKLSAECA 
       360        370        380        390        400
KYWGEIISQQ YNFDRDNTEV AYLKTLTKED IIKFYKEMLA VDAPRRHKVS 
       410        420        430        440        450
VHVLAREMDS CPVVGEFPCQ NDINLSQAPA LPQPEVIQNM TEFKRGLPLF 
       460 
PLVKPHINFM AAKL

Show »

Length:464

Mass (Da):54,240

Checksum:ⁱD51C435A02BA4932

GO

Computationally mapped potential isoform sequencesⁱ

There are 15 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	A0A3B3ISG5	A0A3B3ISG5_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	1,019	Annotation score:
	B3KSB8	B3KSB8_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme (cDNA FLJ35968 fis, clone TESTI2013053, highly similar to INSULIN-DEGRADING ENZYME)	IDE	464	Annotation score:
	R4GN65	R4GN65_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	61	Annotation score:
	A0A7I2V2P6	A0A7I2V2P6_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	978	Annotation score:
	A0A7I2V2S1	A0A7I2V2S1_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	872	Annotation score:
	A0A7I2V373	A0A7I2V373_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	633	Annotation score:
	A0A7I2V3E3	A0A7I2V3E3_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	972	Annotation score:
	A0A7I2V3K9	A0A7I2V3K9_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	428	Annotation score:
	A0A7I2V4A4	A0A7I2V4A4_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	447	Annotation score:
	A0A7I2V4Q3	A0A7I2V4Q3_HUMAN	Insulin-degrading enzyme Insulin-degrading enzyme	IDE	928	Annotation score:
There are more potential isoformsShow all

Experimental Info

Feature key	Position(s)	DescriptionActions	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS53554.1 [P14735-2] CCDS7421.1 [P14735-1]
PIRⁱ	A40119, SNHUIN
NCBI Reference Sequences More...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
UCSC genome browser More...UCSCⁱ	uc001kia.4, human [P14735-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P14735	Insulin-degrading enzyme		HUMAN		384	UniRef100_P14735
+1
P14735-2	Insulin-degrading enzyme		HUMAN		428	UniRef100_A0A7I2V3K9
Uncharacterized protein		FELCA		1219
insulin-degrading enzyme isoform X1		ACIJB		1019
Uncharacterized protein		LYNCA		1019
Insulin-degrading enzyme (Fragment)		CANLF		150
+9

Protein	Similar proteins		Species	Score	Length	Source
P14735	Insulin-degrading enzyme		MOUSE		1019	UniRef90_P14735
Insulin-degrading enzyme	)	RAT		1019
Insulin-degrading enzyme		BOVIN		1019
Insulin-degrading enzyme		HUMAN		384
Uncharacterized protein		FELCA		1156
+548

Protein	Similar proteins		Species	Score	Length	Source
P14735	Insulin-degrading enzyme	)	RAT		1019	UniRef50_P14735
Insulin-degrading enzyme		BOVIN		1019
Insulin-degrading enzyme		MOUSE		1019
Insulin-degrading enzyme		HUMAN		384
Uncharacterized protein		FELCA		1156
+1329

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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, 111 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

MEROPSⁱ

M16.002

PTM databases

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, 505 antibodies

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	ENSG00000119912, Low tissue specificity
MIMⁱ	146680, gene
neXtProtⁱ	NX_P14735
OpenTargetsⁱ	ENSG00000119912
PharmGKBⁱ	PA29629
VEuPathDBⁱ	HostDB:ENSG00000119912.15
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0959, Eukaryota
GeneTreeⁱ	ENSGT00940000155780
HOGENOMⁱ	CLU_004639_1_1_1
InParanoidⁱ	P14735
OMAⁱ	HGNLYKE
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, 6 hits in 1005 CRISPR screens
ChiTaRSⁱ	IDE, human
EvolutionaryTraceⁱ	P14735
GeneWikiⁱ	Insulin-degrading_enzyme
GenomeRNAiⁱ	3416
Pharosⁱ	P14735, Tchem
Protein Ontology More...PROⁱ	PR:P14735
RNActⁱ	P14735, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000119912, Expressed in hair follicle and 231 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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	IDE_HUMAN
Accessionⁱ	P14735Primary (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:	April 7, 2021
	This is version 212 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 proteome

Documents

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

UniProtKB

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UniProtKB - P14735 (IDE_HUMAN)

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Insulin-degrading enzyme

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Plasma membrane

Cytoplasm and Cytosol

Cytosol

Extracellular region or secreted

Mitochondrion

Nucleus

Peroxisome

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P14735

IDE - isoform 1 [P14735-1]

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ