dbPTM

IDE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IDE_HUMAN
UniProt AC	P14735
Protein Name	Insulin-degrading enzyme
Gene Name	IDE
Organism	Homo sapiens (Human).
Sequence Length	1019
Subcellular Localization	Cytoplasm. Cell membrane. Secreted. Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform.
Protein Description	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.; (Microbial infection) The membrane-associated isoform acts as an entry receptor for varicella-zoster virus (VZV)..
Protein Sequence	MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
55	Phosphorylation	KRIGNHITKSPEDKR HHHHHHCCCCHHHHH	20.23	20068231
57	Phosphorylation	IGNHITKSPEDKREY HHHHCCCCHHHHHHH	25.52	29214152
79	Phosphorylation	GIKVLLISDPTTDKS CEEEEEEECCCCCCC	37.19	29083192
82	Phosphorylation	VLLISDPTTDKSSAA EEEEECCCCCCCCCE	53.25	29083192
83	Phosphorylation	LLISDPTTDKSSAAL EEEECCCCCCCCCEE	46.98	29083192
119	Ubiquitination	HMLFLGTKKYPKENE HHHHHCCCCCCCCCH	48.81	-
178	S-nitrosocysteine	CPLFDESCKDREVNA HHHCCHHHCCCCCCC	5.10	-
178	S-nitrosylation	CPLFDESCKDREVNA HHHCCHHHCCCCCCC	5.10	19808678
192	Acetylation	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	23954790
192	Succinylation	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	-
192	Ubiquitination	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	21890473
192	Malonylation	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	26320211
192	Succinylation	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	-
192	Ubiquitination	AVDSEHEKNVMNDAW CCCCHHHHHHHHHHH	57.67	21890473
206	Ubiquitination	WRLFQLEKATGNPKH HHHHHHHHHHCCCCC	60.90	21906983
206	Acetylation	WRLFQLEKATGNPKH HHHHHHHHHHCCCCC	60.90	26051181
212	Ubiquitination	EKATGNPKHPFSKFG HHHHCCCCCCCHHCC	68.83	-
217	Ubiquitination	NPKHPFSKFGTGNKY CCCCCCHHCCCCCCE	48.47	-
220	Phosphorylation	HPFSKFGTGNKYTLE CCCHHCCCCCCEEEC	40.49	-
223	Ubiquitination	SKFGTGNKYTLETRP HHCCCCCCEEECCCC	40.74	-
263	Phosphorylation	VCVLGRESLDDLTNL HHHHCCCCHHHHHHH	35.42	20068231
268	Phosphorylation	RESLDDLTNLVVKLF CCCHHHHHHHHHHHH	33.24	20068231
276	Phosphorylation	NLVVKLFSEVENKNV HHHHHHHHHHCCCCC	51.69	-
281	Ubiquitination	LFSEVENKNVPLPEF HHHHHCCCCCCCCCC	45.90	-
299	Ubiquitination	PFQEEHLKQLYKIVP CCCHHHHHHHHHEEE	39.92	-
308	Malonylation	LYKIVPIKDIRNLYV HHHEEEHHHHCCEEE	40.82	26320211
308	Acetylation	LYKIVPIKDIRNLYV HHHEEEHHHHCCEEE	40.82	19608861
308	Ubiquitination	LYKIVPIKDIRNLYV HHHEEEHHHHCCEEE	40.82	21890473
308	Ubiquitination	LYKIVPIKDIRNLYV HHHEEEHHHHCCEEE	40.82	21890473
328	Phosphorylation	DLQKYYKSNPGHYLG HHHHHHHHCCCCHHH	31.94	28111955
329	Ubiquitination	LQKYYKSNPGHYLGH HHHHHHHCCCCHHHH	42.28	21890473
333	Phosphorylation	YKSNPGHYLGHLIGH HHHCCCCHHHHHCCC	21.94	28111955
345	Phosphorylation	IGHEGPGSLLSELKS CCCCCCCHHHHHHHH	29.30	28111955
348	Phosphorylation	EGPGSLLSELKSKGW CCCCHHHHHHHHCCC	46.29	28111955
374	Ubiquitination	ARGFMFFIINVDLTE CCEEEEEEEEEECCC	1.21	21890473
383	Ubiquitination	NVDLTEEGLLHVEDI EEECCCCCCCCHHHH	27.57	21890473
425	Acetylation	NAVAFRFKDKERPRG CCEEEEECCCCCCCC	64.73	19608861
463	Ubiquitination	LEEFRPDLIEMVLDK HHHHCHHHHHHHHHH	3.86	21890473
501	Ubiquitination	EWYGTQYKQEAIPDE CCCCHHHCCCCCCHH	31.67	-
511	Ubiquitination	AIPDEVIKKWQNADL CCCHHHHHHHHHCCC	53.81	-
512	Acetylation	IPDEVIKKWQNADLN CCHHHHHHHHHCCCC	42.77	7430885
512	Ubiquitination	IPDEVIKKWQNADLN CCHHHHHHHHHCCCC	42.77	-
521	Acetylation	QNADLNGKFKLPTKN HHCCCCCCCCCCCCC	37.95	25953088
527	Acetylation	GKFKLPTKNEFIPTN CCCCCCCCCCCCCCC	53.17	7430905
527	Ubiquitination	GKFKLPTKNEFIPTN CCCCCCCCCCCCCCC	53.17	-
542	Ubiquitination	FEILPLEKEATPYPA EEEEECCCCCCCCCH	61.40	21906983
545	Phosphorylation	LPLEKEATPYPALIK EECCCCCCCCCHHHC	25.17	23312004
547	Phosphorylation	LEKEATPYPALIKDT CCCCCCCCCHHHCCC	9.22	23312004
558	Ubiquitination	IKDTAMSKLWFKQDD HCCCHHHHCCCCCCC	36.33	-
566	Ubiquitination	LWFKQDDKFFLPKAC CCCCCCCCCCCCHHH	46.43	-
625	Phosphorylation	YDLQNTIYGMYLSVK HHCCCCCEEEEEEEC	8.19	-
657	2-Hydroxyisobutyrylation	ATFEIDEKRFEIIKE CCCCCCHHHHHHHHH	59.65	-
657	Ubiquitination	ATFEIDEKRFEIIKE CCCCCCHHHHHHHHH	59.65	21906983
683	Sulfoxidation	EQPHQHAMYYLRLLM CCCHHHHHHHHHHHH	1.80	30846556
691	Phosphorylation	YYLRLLMTEVAWTKD HHHHHHHHHHCCCHH	27.55	-
696	Phosphorylation	LMTEVAWTKDELKEA HHHHHCCCHHHHHHH	20.91	-
697	Succinylation	MTEVAWTKDELKEAL HHHHCCCHHHHHHHH	38.20	-
697	Ubiquitination	MTEVAWTKDELKEAL HHHHCCCHHHHHHHH	38.20	-
697	Succinylation	MTEVAWTKDELKEAL HHHHCCCHHHHHHHH	38.20	21890473
701	Ubiquitination	AWTKDELKEALDDVT CCCHHHHHHHHCCCC	38.60	-
713	Ubiquitination	DVTLPRLKAFIPQLL CCCHHHHHHHHHHHH	42.40	-
774	Methylation	REVQLPDRGWFVYQQ EEEECCCCCEEEEEE	42.16	115480139
789	S-nitrosylation	RNEVHNNCGIEIYYQ CCCCCCCCEEEEEEE	7.63	19808678
789	S-nitrosocysteine	RNEVHNNCGIEIYYQ CCCCCCCCEEEEEEE	7.63	-
819	S-nitrosocysteine	CQIISEPCFNTLRTK HHHHCCCCHHHCCCH	3.45	-
819	S-nitrosylation	CQIISEPCFNTLRTK HHHHCCCCHHHCCCH	3.45	19808678
825	Phosphorylation	PCFNTLRTKEQLGYI CCHHHCCCHHHHCEE	41.88	28152594
826	Ubiquitination	CFNTLRTKEQLGYIV CHHHCCCHHHHCEEE	36.71	21890473
831	Phosphorylation	RTKEQLGYIVFSGPR CCHHHHCEEEECCCC	11.51	28152594
835	Phosphorylation	QLGYIVFSGPRRANG HHCEEEECCCCCCCC	36.67	28152594
852	Phosphorylation	GLRFIIQSEKPPHYL CEEEEEECCCCCCHH	36.86	28509920
854	Acetylation	RFIIQSEKPPHYLES EEEEECCCCCCHHHH	69.92	25953088
854	Ubiquitination	RFIIQSEKPPHYLES EEEEECCCCCCHHHH	69.92	-
861	Phosphorylation	KPPHYLESRVEAFLI CCCCHHHHHHHHHHH	38.74	28509920
877	Sulfoxidation	MEKSIEDMTEEAFQK HHHCHHHCCHHHHHH	3.09	21406390
884	Ubiquitination	MTEEAFQKHIQALAI CCHHHHHHHHHHHHH	35.90	21890473
884	Ubiquitination	MTEEAFQKHIQALAI CCHHHHHHHHHHHHH	35.90	21890473
899	Succinylation	RRLDKPKKLSAECAK HCCCCCCCCCHHHHH	57.09	27452117
899	Ubiquitination	RRLDKPKKLSAECAK HCCCCCCCCCHHHHH	57.09	-
899	Acetylation	RRLDKPKKLSAECAK HCCCCCCCCCHHHHH	57.09	25953088
901	Phosphorylation	LDKPKKLSAECAKYW CCCCCCCCHHHHHHH	30.79	27251275
929	Ubiquitination	NTEVAYLKTLTKEDI CCEEEEEEECCHHHH	28.89	21890473
929	Ubiquitination	NTEVAYLKTLTKEDI CCEEEEEEECCHHHH	28.89	21906983
933	Ubiquitination	AYLKTLTKEDIIKFY EEEEECCHHHHHHHH	57.40	-
938	Ubiquitination	LTKEDIIKFYKEMLA CCHHHHHHHHHHHHC	42.87	21890473
938	Ubiquitination	LTKEDIIKFYKEMLA CCHHHHHHHHHHHHC	42.87	21906983
938	2-Hydroxyisobutyrylation	LTKEDIIKFYKEMLA CCHHHHHHHHHHHHC	42.87	-
943	Sulfoxidation	IIKFYKEMLAVDAPR HHHHHHHHHCCCCCC	2.26	21406390
955	Phosphorylation	APRRHKVSVHVLARE CCCCCCEEHHHEEEC	16.00	20068231
966	S-nitrosocysteine	LAREMDSCPVVGEFP EEECCCCCCCCEEEC	2.30	-
966	S-nitrosylation	LAREMDSCPVVGEFP EEECCCCCCCCEEEC	2.30	19808678
1018	Ubiquitination	HINFMAAKL------ CCCHHHCCC------	45.23	21906983
1018	Ubiquitination	HINFMAAKL------ CCCHHHCCC------	45.23	21890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of IDE_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IDE_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of IDE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IGF1_HUMAN	IGF1	physical	1733942
IGF2_HUMAN	IGF2	physical	1733942
SRC8_HUMAN	CTTN	physical	22863883
SYCC_HUMAN	CARS	physical	22863883
ERF3A_HUMAN	GSPT1	physical	22863883
ERF3B_HUMAN	GSPT2	physical	22863883
PUS7_HUMAN	PUS7	physical	22863883
UBC_HUMAN	UBC	physical	21185309
NEST_HUMAN	NES	physical	21185309
FA98B_HUMAN	FAM98B	physical	26344197
PNCB_HUMAN	NAPRT	physical	26344197
PA1B2_HUMAN	PAFAH1B2	physical	26344197
PPCS_HUMAN	PPCS	physical	26344197
STAT3_HUMAN	STAT3	physical	26344197
THOP1_HUMAN	THOP1	physical	26344197
ANDR_HUMAN	AR	physical	8051160
GCR_HUMAN	NR3C1	physical	8051160

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00626	Bacitracin
DB00030	Insulin Regular

Regulatory Network of IDE_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-308, AND MASS SPECTROMETRY.	19608861 [Abstract]