P14735 (IDE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1019 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.13 Ref.14
Catalytic activity	Degradation of insulin, glucagon and other polypeptides. No action on proteins. Ref.13
Cofactor	Binds 1 zinc ion per subunit. Ref.12
Enzyme regulation	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.13 Ref.14
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 may function as an entry receptor for this virus. Ref.8 Ref.9 Ref.12 Ref.13
Subcellular location	Cytoplasm. Cell membrane. Secreted By similarity. Note: Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 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 process	Host-virus interaction
Cellular component	Cell membrane Cytoplasm Membrane Secreted
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	beta-amyloid metabolic process Inferred from direct assay Ref.13. Source: UniProtKB bradykinin catabolic process Inferred from direct assay Ref.13. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW sex differentiation Traceable author statement. Source: ProtInc
Cellular component	extracellular space Traceable author statement. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from direct assay Ref.13. Source: UniProtKB metalloendopeptidase activity Inferred from direct assay Ref.13. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.13. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 1019

1018

Insulin-degrading enzyme

PRO_0000074404

Regions

Region

336 – 342

7

Substrate binding exosite

Region

359 – 363

5

Substrate binding

Motif

853 – 858

6

SlyX motif

Sites

Active site

111

1

Proton acceptor By similarity

Metal binding

108

1

Zinc By similarity

Metal binding

112

1

Zinc By similarity

Metal binding

189

1

Zinc By similarity

Amino acid modifications

Modified residue

308

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

612

1

E → K.
Corresponds to variant rs2229708 [ dbSNP | Ensembl ].

VAR_051571

Experimental info

Mutagenesis

111

1

E → Q: Loss of catalytic activity. Ref.12

Mutagenesis

132

1

S → C: Increases catalytic rate towards INS and amyloid; when associated with C-817. Ref.12

Mutagenesis

184

1

N → C: Increases catalytic rate towards INS and amyloid; when associated with C-828. Ref.12

Mutagenesis

426

1

D → C: Increases catalytic rate towards INS and amyloid; when associated with C-899. Ref.12 Ref.13

Mutagenesis

817

1

E → C: Increases catalytic rate towards INS and amyloid; when associated with C-132. Ref.12

Mutagenesis

828

1

Q → C: Increases catalytic rate towards INS and amyloid; when associated with C-184. Ref.12

Mutagenesis

831

1

Y → F: No effect on catalytic activity.

Mutagenesis

899

1

K → C: Increases catalytic rate towards INS and amyloid; when associated with C-426. Ref.12 Ref.13

Sequence conflict

78

1

I → M in AAA52712. Ref.2

Sequence conflict

472

1

R → G in BAG35668. Ref.3

Sequence conflict

555

1

A → V in AAA52712. Ref.2

Sequence conflict

567 – 569

3

FFL → KKK in AAA52712. Ref.2

Sequence conflict

586

1

D → G in BAG35668. Ref.3

Sequence conflict

845

1

G → S in AAA52712. Ref.2

Secondary structure

1

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1019

Helix Strand Turn

Details...

Beta strand

47 – 50

4

Beta strand

63 – 69

7

Beta strand

74 – 79

6

Beta strand

84 – 93

10

Helix

96 – 98

3

Helix

106 – 113

8

Helix

114 – 116

3

Beta strand

118 – 121

4

Helix

126 – 132

7

Turn

133 – 135

3

Beta strand

137 – 142

6

Beta strand

147 – 154

8

Helix

155 – 157

3

Helix

158 – 166

9

Helix

167 – 169

3

Helix

176 – 193

18

Helix

197 – 208

12

Helix

214 – 216

3

Helix

223 – 226

4

Helix

228 – 232

5

Helix

237 – 248

12

Helix

251 – 253

3

Beta strand

254 – 262

9

Helix

264 – 275

12

Helix

295 – 297

3

Beta strand

298 – 304

7

Beta strand

307 – 309

3

Beta strand

312 – 319

8

Helix

323 – 325

3

Turn

326 – 328

3

Helix

330 – 338

9

Helix

346 – 352

7

Beta strand

355 – 367

13

Beta strand

370 – 379

10

Helix

381 – 384

4

Helix

387 – 404

18

Helix

408 – 423

16

Helix

430 – 440

11

Turn

441 – 443

3

Helix

446 – 448

3

Turn

449 – 454

6

Helix

461 – 468

8

Helix

473 – 475

3

Beta strand

477 – 481

5

Helix

483 – 485

3

Turn

486 – 488

3

Turn

494 – 496

3

Beta strand

499 – 504

6

Helix

507 – 514

8

Beta strand

549 – 553

5

Beta strand

555 – 563

9

Beta strand

570 – 579

10

Helix

581 – 583

3

Beta strand

584 – 586

3

Helix

587 – 613

27

Beta strand

616 – 623

8

Beta strand

626 – 635

10

Helix

638 – 650

13

Helix

656 – 671

16

Helix

672 – 675

4

Helix

678 – 690

13

Beta strand

691 – 693

3

Helix

697 – 703

7

Turn

704 – 706

3

Helix

709 – 721

13

Beta strand

722 – 732

11

Helix

735 – 753

19

Helix

760 – 762

3

Beta strand

775 – 782

8

Beta strand

787 – 799

13

Helix

802 – 823

22

Turn

824 – 827

4

Beta strand

831 – 840

10

Beta strand

843 – 854

12

Helix

856 – 876

21

Helix

879 – 894

16

Helix

900 – 912

13

Helix

920 – 928

9

Helix

933 – 943

11

Beta strand

952 – 959

8

Helix

995 – 1000

6

Sequences

	Sequence		Length	Mass (Da)
	P14735 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 8A28AEF75EDA0EDA	FASTA	1,019	117,968
	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

References

	« Hide 'large scale' referencesShow '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: 3059494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 2293021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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. , 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: 15164054] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 10684867] [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: 17055432] [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: 17553876] [Abstract] Cited for: INTERACTION WITH VZV GLYCOPROTEIN E.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-308, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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: 17051221] [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.
[13]	"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: 17613531] [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.
[14]	"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: 18986166] [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.
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.

IPI

IPI00220373.

PIR

SNHUIN. A40119.

RefSeq

NP_004960.2. NM_004969.3.

UniGene

Hs.500546.

3D structure databases

PDBe
RCSB PDB
PDBj

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	43-1018	[»]
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	[»]
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	[»]

ProteinModelPortal

P14735.

SMR

P14735. Positions 43-1016.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-55771N.

IntAct

P14735. 2 interactions.

STRING

P14735.

Protein family/group databases

MEROPS

M16.002.

PTM databases

PhosphoSite

P14735.

Polymorphism databases

DMDM

215274252.

Proteomic databases

PRIDE

P14735.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000265986; ENSP00000265986; ENSG00000119912.

GeneID

3416.

KEGG

hsa:3416.

Organism-specific databases

CTD

3416.

GeneCards

GC10M094201.

H-InvDB

HIX0009042.

HGNC

HGNC:5381. IDE.

HPA

CAB012303.

MIM

146680. gene.

neXtProt

NX_P14735.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG04724.

HOGENOM

HBG328356.

HOVERGEN

HBG106799.

InParanoid

P14735.

OMA

VMQITNE.

OrthoDB

EOG4H4630.

PhylomeDB

P14735.

Gene expression databases

ArrayExpress

P14735.

Bgee

P14735.

CleanEx

HS_IDE.

Genevestigator

P14735.

GermOnline

ENSG00000119912. Homo sapiens.

Family and domain databases

InterPro

IPR011249. Metalloenz_metal-bd.
IPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]

Gene3D

G3DSA:3.30.830.10. Pept_M16_core. 2 hits.

KO

K01408.

Pfam

PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]

SUPFAM

SSF63411. Metalloenz_metal-bd. 4 hits.

PROSITE

PS00143. INSULINASE. 1 hit.
[Graphical view]

ProtoNet

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Other

DrugBank

DB00626. Bacitracin.
DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.

SOURCE

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Entry information

Entry name

IDE_HUMAN

Accession

Primary (citable) accession number: P14735
Secondary accession number(s): B2R721, D3DR35, Q5T5N2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 120 of the entry and version 4 of the sequence. [Complete history]

Entry status

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.