ECE1_HUMAN - dbPTM
ECE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECE1_HUMAN
UniProt AC P42892
Protein Name Endothelin-converting enzyme 1
Gene Name ECE1
Organism Homo sapiens (Human).
Sequence Length 770
Subcellular Localization Cell membrane
Single-pass type II membrane protein.
Protein Description Converts big endothelin-1 to endothelin-1..
Protein Sequence MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNGLQVNFHSPRSGQRCWAARTQVEKRLVVLVVLLAAGLVACLAALGIQYQTRSPSVCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4 (in isoform 3)Phosphorylation-4.97-
7 (in isoform 4)Phosphorylation-26.6428787133
9 (in isoform 3)Phosphorylation-6.8829507054
16 (in isoform 4)Phosphorylation-5.4828787133
19PhosphorylationLLSALGMSTYKRATL
HHHHHCCCCCCCCCC		27.13-
25 (in isoform 2)Phosphorylation-38.4822210691
25PhosphorylationMSTYKRATLDEEDLV
CCCCCCCCCCHHHHH		38.4830266825
32 (in isoform 2)Phosphorylation-7.9022210691
34PhosphorylationDEEDLVDSLSEGDAY
CHHHHHHHCCCCCCC		26.7330266825
36PhosphorylationEDLVDSLSEGDAYPN
HHHHHHCCCCCCCCC		43.4130266825
39 (in isoform 2)Phosphorylation-38.5922210691
41PhosphorylationSLSEGDAYPNGLQVN
HCCCCCCCCCCEEEE		11.2830266825
42S-palmitoylationLSEGDAYPNGLQVNF
CCCCCCCCCCEEEEE		30.0810359648
46S-palmitoylationDAYPNGLQVNFHSPR
CCCCCCEEEEEECCC		29.5210359648
51PhosphorylationGLQVNFHSPRSGQRC
CEEEEEECCCCCCCC		20.1925159151
58S-palmitoylationSPRSGQRCWAARTQV
CCCCCCCCCHHCCHH		1.9210359648
91PhosphorylationLAALGIQYQTRSPSV
HHHHCCCCCCCCCCH		15.2124043423
93PhosphorylationALGIQYQTRSPSVCL
HHCCCCCCCCCCHHH		28.3424043423
166N-linked_GlycosylationIIKHLLENSTASVSE
HHHHHHHCCCCCCCH		44.6317660510
166N-linked_GlycosylationIIKHLLENSTASVSE
HHHHHHHCCCCCCCH		44.6319349973
177UbiquitinationSVSEAERKAQVYYRA
CCCHHHHHHHHHHHH		34.38-
187N-linked_GlycosylationVYYRACMNETRIEEL
HHHHHHCCCHHHHHH		47.58UniProtKB CARBOHYD
197UbiquitinationRIEELRAKPLMELIE
HHHHHHHHHHHHHHH		32.05-
210N-linked_GlycosylationIERLGGWNITGPWAK
HHHHCCCCCCCCCHH		25.8116263699
210N-linked_GlycosylationIERLGGWNITGPWAK
HHHHCCCCCCCCCHH		25.8116263699
255 (in isoform 3)Ubiquitination-5.0621906983
259 (in isoform 2)Ubiquitination-20.3821906983
268 (in isoform 4)Ubiquitination-14.2121906983
270N-linked_GlycosylationPSRDYYLNKTENEKV
CCCCEECCCCCCHHH		32.8419159218
271UbiquitinationSRDYYLNKTENEKVL
CCCEECCCCCCHHHH		55.4021906983
271 (in isoform 1)Ubiquitination-55.4021906983
316N-linked_GlycosylationDFETALANITIPQEK
CHHHHHHHCCCCHHH		32.5519349973
316N-linked_GlycosylationDFETALANITIPQEK
CHHHHHHHCCCCHHH		32.5519159218
331PhosphorylationRRDEELIYHKVTAAE
CCCCHHHHEEHHHHH		14.28-
362N-linked_GlycosylationIFYPVEINESEPIVV
EEEEEECCCCCCEEE		32.9819349973
362N-linked_GlycosylationIFYPVEINESEPIVV
EEEEEECCCCCCEEE		32.9819349973
383N-linked_GlycosylationEQISTLINTTDRCLL
HHHHHHHHHCCCHHH		39.7919349973
383N-linked_GlycosylationEQISTLINTTDRCLL
HHHHHHHHHCCCHHH		39.7919349973
416UbiquitinationRFQDADEKFMEVMYG
HHHHHHHHHHHHHHC		51.03-
422PhosphorylationEKFMEVMYGTKKTCL
HHHHHHHHCCCCCCC		27.1529116813
424PhosphorylationFMEVMYGTKKTCLPR
HHHHHHCCCCCCCCC		16.3322468782
4252-HydroxyisobutyrylationMEVMYGTKKTCLPRW
HHHHHCCCCCCCCCC		41.54-
425UbiquitinationMEVMYGTKKTCLPRW
HHHHHCCCCCCCCCC		41.54-
456 (in isoform 3)Ubiquitination-9.2921906983
460 (in isoform 2)Ubiquitination-21.5821906983
469 (in isoform 4)Ubiquitination-7.3721906983
472UbiquitinationTEIILEIKKAFEESL
HHHHHHHHHHHHHHH		28.7721906983
472 (in isoform 1)Ubiquitination-28.7721906983
473UbiquitinationEIILEIKKAFEESLS
HHHHHHHHHHHHHHH		65.06-
478PhosphorylationIKKAFEESLSTLKWM
HHHHHHHHHHHHHHC		22.0321406692
480 (in isoform 3)Ubiquitination-40.7621906983
480PhosphorylationKAFEESLSTLKWMDE
HHHHHHHHHHHHCCH		40.7621406692
481PhosphorylationAFEESLSTLKWMDEE
HHHHHHHHHHHCCHH		37.3421406692
483UbiquitinationEESLSTLKWMDEETR
HHHHHHHHHCCHHHH		40.33-
484 (in isoform 2)Ubiquitination-11.5421906983
493 (in isoform 4)Ubiquitination-27.3621906983
496UbiquitinationTRKSAKEKADAIYNM
HHHHHHHHHHHHHHH		51.3521906983
496 (in isoform 1)Ubiquitination-51.3521906983
539N-linked_GlycosylationENAMRFFNFSWRVTA
HCCHHHCCEEEEECH		27.5917660510
539N-linked_GlycosylationENAMRFFNFSWRVTA
HCCHHHCCEEEEECH		27.5919349973
559PhosphorylationAPNRDQWSMTPPMVN
CCCCCCCCCCCCCCC		13.7229507054
623 (in isoform 3)Ubiquitination-48.6021906983
627 (in isoform 2)Ubiquitination-28.8821906983
632N-linked_GlycosylationNLRPWWKNSSVEAFK
CCCCCCCCCHHHHHH		26.2917660510
633PhosphorylationLRPWWKNSSVEAFKR
CCCCCCCCHHHHHHH		31.8427251275
634PhosphorylationRPWWKNSSVEAFKRQ
CCCCCCCHHHHHHHH		33.1127251275
636 (in isoform 4)Ubiquitination-50.7921906983
639UbiquitinationNSSVEAFKRQTECMV
CCHHHHHHHHHHHHH		51.1221906983
639 (in isoform 1)Ubiquitination-51.1221906983
651N-linked_GlycosylationCMVEQYSNYSVNGEP
HHHEECCCCCCCCEE		28.32UniProtKB CARBOHYD
660 (in isoform 3)Ubiquitination-53.1221906983
664 (in isoform 2)Ubiquitination-34.7921906983
664PhosphorylationEPVNGRHTLGENIAD
EECCCCCCCCCCCCC		34.7928450419
673 (in isoform 4)Ubiquitination-43.2721906983
676 (in isoform 1)Ubiquitination-33.9621906983
676UbiquitinationIADNGGLKAAYRAYQ
CCCCCCHHHHHHHHH		33.962190698
733PhosphorylationGLITDPHSPSRFRVI
CCCCCCCCCCCEEEE		29.93-
735PhosphorylationITDPHSPSRFRVIGS
CCCCCCCCCEEEEEE		47.25-
759PhosphorylationHFRCPPGSPMNPPHK
HCCCCCCCCCCCCCC		27.1020363803
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
9TPhosphorylationKinaseCSNK2A1P68400
GPS
18SPhosphorylationKinaseCSNK2A1P68400
GPS
20SPhosphorylationKinaseCSNK2A1P68400
GPS
34SPhosphorylationKinaseCSNK1A1P48729
GPS
36SPhosphorylationKinaseCSNK1A1P48729
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECE1_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 ECE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSRD_HUMANSSR4physical
22939629
LTOR2_HUMANLAMTOR2physical
22939629
RS26_HUMANRPS26physical
22939629
RSSA_HUMANRPSAphysical
22939629
FKB10_HUMANFKBP10physical
22939629
RL19_HUMANRPL19physical
22939629
FAF2_HUMANFAF2physical
22939629
VMA21_HUMANVMA21physical
22939629
CALC_HUMANCALCAphysical
18039931
CALCA_HUMANCALCAphysical
18039931
ANGT_HUMANAGTphysical
18039931
KNG1_HUMANKNG1physical
18039931
KR101_HUMANKRTAP10-1physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613870Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECE1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-362 ANDASN-383, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-270 ANDASN-316, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND MASSSPECTROMETRY.

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