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P14735 (IDE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-degrading enzyme

EC=3.4.24.56
Alternative name(s):
Abeta-degrading protease
Insulin protease
Short name=Insulinase
Insulysin
Gene names
Name:IDE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1019 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia. Ref.7 Ref.14 Ref.15

Catalytic activity

Degradation of insulin, glucagon and other polypeptides. No action on proteins. Ref.14

Cofactor

Binds 1 zinc ion per subunit. Ref.13

Enzyme regulation

Activated by small peptides By similarity. Activated by ATP and GTP, and to a lesser extent by CTP, TTP and PPPi. Inhibited by bacitracin. Inhibited by S-nitrosylation and oxidation agents. Ref.14 Ref.15

Subunit structure

Homodimer. Can form higher oligomers. Interacts (via N-terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform mayfunction as an entry receptor for this virus. Ref.8 Ref.9 Ref.13 Ref.14

Subcellular location

Cytoplasm. Cell membrane. Secreted By similarity. Note: Present at the cell surface of neuron cells. The membrane-associated isoform isapproximately 5 kDa larger than the known cytosolic isoform. Ref.7 Ref.8

Domain

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

Post-translational modification

The N-terminus is blocked.

Miscellaneous

ATP-binding induces a conformation change.

Sequence similarities

Belongs to the peptidase M16 family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Cytoplasm
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbeta-amyloid metabolic process

Inferred from direct assay Ref.14PubMed 9830016. Source: UniProtKB

bradykinin catabolic process

Inferred from direct assay Ref.14PubMed 21185309. Source: UniProtKB

determination of adult lifespan

Inferred from direct assay PubMed 18448515. Source: UniProtKB

hormone catabolic process

Inferred from electronic annotation. Source: Ensembl

insulin catabolic process

Inferred from direct assay PubMed 9231799PubMed 9830016. Source: UniProtKB

insulin metabolic process

Inferred from direct assay PubMed 18448515. Source: UniProtKB

insulin receptor signaling pathway

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein oligomerization

Inferred from direct assay PubMed 9830016. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay Ref.13. Source: UniProtKB

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 20082125PubMed 21185309. Source: UniProtKB

proteolysis involved in cellular protein catabolic process

Inferred from direct assay PubMed 9830016. Source: UniProtKB

ubiquitin homeostasis

Inferred from direct assay PubMed 21185309. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell surface

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18226493PubMed 9231799PubMed 9830016. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15285718PubMed 9830016. Source: UniProtKB

cytosolic proteasome complex

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 9830016. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 15285718. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15285718PubMed 9231799. Source: UniProtKB

peroxisomal matrix

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 9231799. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.14. Source: UniProtKB

ATPase activity

Inferred from electronic annotation. Source: Ensembl

beta-amyloid binding

Inferred from electronic annotation. Source: Ensembl

beta-endorphin binding

Inferred from electronic annotation. Source: Ensembl

glycoprotein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

insulin binding

Inferred from direct assay Ref.13. Source: UniProtKB

metalloendopeptidase activity

Inferred from direct assay Ref.13Ref.14. Source: UniProtKB

peptide binding

Inferred from physical interaction PubMed 20082125. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17715127. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.14. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

ubiquitin binding

Inferred from physical interaction PubMed 21185309. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCL3P101473EBI-2556886,EBI-8459634

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14735-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P14735-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10191019Insulin-degrading enzyme
PRO_0000074404

Regions

Nucleotide binding895 – 9017ATP By similarity
Region336 – 3427Substrate binding exosite
Region359 – 3635Substrate binding
Motif853 – 8586SlyX motif

Sites

Active site1111Proton acceptor By similarity
Metal binding1081Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1891Zinc By similarity
Binding site4291ATP By similarity

Amino acid modifications

Modified residue1921N6-succinyllysine By similarity
Modified residue6971N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 555555Missing in isoform 2.
VSP_044303
Natural variant6121E → K.
Corresponds to variant rs2229708 [ dbSNP | Ensembl ].
VAR_051571

Experimental info

Mutagenesis1111E → Q: Loss of catalytic activity. Ref.13
Mutagenesis1321S → C: Increases catalytic rate towards INS and amyloid; when associated with C-817. Ref.13
Mutagenesis1841N → C: Increases catalytic rate towards INS and amyloid; when associated with C-828. Ref.13
Mutagenesis4261D → C: Increases catalytic rate towards INS and amyloid; when associated with C-899. Ref.13 Ref.14
Mutagenesis8171E → C: Increases catalytic rate towards INS and amyloid; when associated with C-132. Ref.13
Mutagenesis8281Q → C: Increases catalytic rate towards INS and amyloid; when associated with C-184. Ref.13
Mutagenesis8311Y → F: No effect on catalytic activity.
Mutagenesis8991K → C: Increases catalytic rate towards INS and amyloid; when associated with C-426. Ref.13 Ref.14
Sequence conflict781I → M in AAA52712. Ref.2
Sequence conflict4721R → G in BAG35668. Ref.3
Sequence conflict5551A → V in AAA52712. Ref.2
Sequence conflict567 – 5693FFL → KKK in AAA52712. Ref.2
Sequence conflict5861D → G in BAG35668. Ref.3
Sequence conflict8451G → S in AAA52712. Ref.2

Secondary structure

...................................................................................................................................................... 1019
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 8A28AEF75EDA0EDA

FASTA1,019117,968
        10         20         30         40         50         60 
MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED 

        70         80         90        100        110        120 
KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK 

       130        140        150        160        170        180 
YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD 

       190        200        210        220        230        240 
REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE 

       250        260        270        280        290        300 
LLKFHSAYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ 

       310        320        330        340        350        360 
LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV 

       370        380        390        400        410        420 
GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV 

       430        440        450        460        470        480 
AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI 

       490        500        510        520        530        540 
VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL 

       550        560        570        580        590        600 
EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL 

       610        620        630        640        650        660 
KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE 

       670        680        690        700        710        720 
IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL 

       730        740        750        760        770        780 
SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ 

       790        800        810        820        830        840 
QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA 

       850        860        870        880        890        900 
NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL 

       910        920        930        940        950        960 
SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR RHKVSVHVLA 

       970        980        990       1000       1010 
REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR GLPLFPLVKP HINFMAAKL 

« Hide

Isoform 2 [UniParc].

Checksum: D51C435A02BA4932
Show »

FASTA46454,240

References

« Hide 'large scale' references
[1]"Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III."
Affholter J.A., Fried V.A., Roth R.A.
Science 242:1415-1418(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[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.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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.
[8]"Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread."
Li Q., Ali M.A., Cohen J.I.
Cell 127:305-316(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VZV GLYCOPROTEIN E.
[9]"The amino terminus of varicella-zoster virus (VZV) glycoprotein E is required for binding to insulin-degrading enzyme, a VZV receptor."
Li Q., Krogmann T., Ali M.A., Tang W.-J., Cohen J.I.
J. Virol. 81:8525-8532(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VZV GLYCOPROTEIN E.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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, COFACTOR, SUBUNIT, ACTIVE SITE.
[14]"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, ENZYME REGULATION, ATP-BINDING, SUBUNIT, MUTAGENESIS OF ASP-426 AND LYS-899, FUNCTION.
[15]"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, FUNCTION, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21188 mRNA. Translation: AAA52712.1.
AK312810 mRNA. Translation: BAG35668.1.
AK316407 mRNA. Translation: BAH14778.1.
AL356128 Genomic DNA. Translation: CAI13670.1.
CH471066 Genomic DNA. Translation: EAW50090.1.
CH471066 Genomic DNA. Translation: EAW50091.1.
BC096336 mRNA. Translation: AAH96336.1.
BC096337 mRNA. Translation: AAH96337.1.
BC096339 mRNA. Translation: AAH96339.1.
CCDSCCDS53554.1. [P14735-2]
CCDS7421.1. [P14735-1]
PIRSNHUIN. A40119.
RefSeqNP_001159418.1. NM_001165946.1. [P14735-2]
NP_004960.2. NM_004969.3. [P14735-1]
UniGeneHs.500546.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G47X-ray2.10A/B42-1019[»]
2G48X-ray2.60A/B42-1019[»]
2G49X-ray2.50A/B42-1019[»]
2G54X-ray2.25A/B42-1019[»]
2G56X-ray2.20A/B42-1019[»]
2JBUX-ray3.00A/B42-1019[»]
2JG4X-ray2.80A/B43-1019[»]
2WBYX-ray2.60A/B42-1019[»]
2WC0X-ray2.80A/B42-1019[»]
2WK3X-ray2.59A/B1-1019[»]
2YPUX-ray2.80A/B42-1019[»]
3CWWX-ray1.96A/B42-1019[»]
3E4AX-ray2.60A/B1-1019[»]
3E4ZX-ray2.28A/B42-1019[»]
3E50X-ray2.30A/B42-1019[»]
3H44X-ray3.00A/B42-1019[»]
3HGZX-ray2.91A/B43-1011[»]
3N56X-ray3.10A/B42-1019[»]
3N57X-ray3.03A/B42-1019[»]
3OFIX-ray2.35A/B42-1019[»]
3QZ2X-ray3.20A/B42-1019[»]
4DTTX-ray3.22A/B42-1019[»]
4DWKX-ray3.00A/B42-1019[»]
4GS8X-ray2.99A/B42-1019[»]
4GSCX-ray2.81A/B42-1019[»]
4GSFX-ray2.70A/B42-1019[»]
4IFHX-ray3.29A/B42-1019[»]
4IOFX-ray3.35A/B42-1019[»]
4LTEX-ray2.70A/B42-1019[»]
ProteinModelPortalP14735.
SMRP14735. Positions 43-1016.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109642. 24 interactions.
DIPDIP-55771N.
IntActP14735. 5 interactions.
MINTMINT-2801173.
STRING9606.ENSP00000265986.

Chemistry

BindingDBP14735.
ChEMBLCHEMBL1293287.
DrugBankDB00626. Bacitracin.
DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.

Protein family/group databases

MEROPSM16.002.

PTM databases

PhosphoSiteP14735.

Polymorphism databases

DMDM215274252.

Proteomic databases

MaxQBP14735.
PaxDbP14735.
PRIDEP14735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265986; ENSP00000265986; ENSG00000119912. [P14735-1]
ENST00000371581; ENSP00000360637; ENSG00000119912. [P14735-2]
GeneID3416.
KEGGhsa:3416.
UCSCuc001kia.3. human. [P14735-1]
uc010qnp.2. human. [P14735-2]

Organism-specific databases

CTD3416.
GeneCardsGC10M094211.
H-InvDBHIX0009042.
HGNCHGNC:5381. IDE.
HPACAB012303.
MIM146680. gene.
neXtProtNX_P14735.
PharmGKBPA29629.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1025.
HOGENOMHOG000161331.
HOVERGENHBG106799.
InParanoidP14735.
KOK01408.
OMASIFHIIK.
OrthoDBEOG7HHWRD.
PhylomeDBP14735.
TreeFamTF106275.

Enzyme and pathway databases

SignaLinkP14735.

Gene expression databases

ArrayExpressP14735.
BgeeP14735.
CleanExHS_IDE.
GenevestigatorP14735.

Family and domain databases

Gene3D3.30.830.10. 4 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
SUPFAMSSF63411. SSF63411. 4 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14735.
GeneWikiInsulin-degrading_enzyme.
GenomeRNAi3416.
NextBio13466.
PROP14735.
SOURCESearch...

Entry information

Entry nameIDE_HUMAN
AccessionPrimary (citable) accession number: P14735
Secondary accession number(s): B2R721 expand/collapse secondary AC list , B7ZAU2, D3DR35, Q5T5N2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM