ACE_HUMAN - dbPTM
ACE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACE_HUMAN
UniProt AC P12821
Protein Name Angiotensin-converting enzyme
Gene Name ACE
Organism Homo sapiens (Human).
Sequence Length 1306
Subcellular Localization Angiotensin-converting enzyme, soluble form: Secreted.
Cell membrane
Single-pass type I membrane protein. Cytoplasm. Detected in both cell membrane and cytoplasm in neurons..
Protein Description Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety..
Protein Sequence MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKLRKVLQAGSSRPWQEVLKDMVGLDALDAQPLLKYFQPVTQWLQEQNQQNGEVLGWPEYQWHPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHRSLHRHSHGPQFGSEVELRHS
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
38N-linked_GlycosylationDPGLQPGNFSADEAG
CCCCCCCCCCHHHHH		34.099013598
54N-linked_GlycosylationQLFAQSYNSSAEQVL
HHHHHHCCCCHHHHH		34.439013598
74N-linked_GlycosylationASWAHDTNITAENAR
HHHHHHCCCCHHHHH		35.3516476442
111N-linked_GlycosylationLYEPIWQNFTDPQLR
HHHHHHHHCCCHHHH		27.139013598
136AcetylationSANLPLAKRQQYNAL
CCCCCHHHHHHHHHH		59.427933021
140PhosphorylationPLAKRQQYNALLSNM
CHHHHHHHHHHHHHH		8.2824043423
144 (in isoform 3)Ubiquitination-3.0221890473
144UbiquitinationRQQYNALLSNMSRIY
HHHHHHHHHHHHHHH		3.0221890473
145PhosphorylationQQYNALLSNMSRIYS
HHHHHHHHHHHHHHH		31.1924043423
146N-linked_GlycosylationQYNALLSNMSRIYST
HHHHHHHHHHHHHHH		32.209013598
148PhosphorylationNALLSNMSRIYSTAK
HHHHHHHHHHHHHCC		21.5624043423
151PhosphorylationLSNMSRIYSTAKVCL
HHHHHHHHHHCCEEC		10.0046157531
160N-linked_GlycosylationTAKVCLPNKTATCWS
HCCEECCCCCCEEEE		41.16UniProtKB CARBOHYD
318N-linked_GlycosylationTMLQQGWNATHMFRV
HHHHCCCCHHHHHHH		41.6116476442
445N-linked_GlycosylationGLLDRVTNDTESDIN
CCHHHHCCCCHHHHH		51.8819159218
449PhosphorylationRVTNDTESDINYLLK
HHCCCCHHHHHHHHH		45.9728842319
509N-linked_GlycosylationICPPVTRNETHFDAG
CCCCCCCCCCCCCCC		49.5016476442
677N-linked_GlycosylationANWNYNTNITTETSK
HHCCCCCCCCCHHHH		26.43UniProtKB CARBOHYD
695N-linked_GlycosylationQKNMQIANHTLKYGT
HHCHHHHHHHHHCCC		30.2416335952
697PhosphorylationNMQIANHTLKYGTQA
CHHHHHHHHHCCCCC		25.4246157519
714N-linked_GlycosylationFDVNQLQNTTIKRII
CCHHHHCHHHHHHHH		48.029013598
716PhosphorylationVNQLQNTTIKRIIKK
HHHHCHHHHHHHHHH		31.8617924679
718 (in isoform 2)Ubiquitination-35.1421890473
718UbiquitinationQLQNTTIKRIIKKVQ
HHCHHHHHHHHHHHH		35.1421890473
718 (in isoform 1)Ubiquitination-35.1421890473
760N-linked_GlycosylationVATVCHPNGSCLQLE
EEEEECCCCCEEECC		31.209013598
804AcetylationAILQFYPKYVELINQ
HHHHHHHHHHHHHHH		51.0225038526
814MethylationELINQAARLNGYVDA
HHHHHHHHHCCCCCC		31.53-
824PhosphorylationGYVDAGDSWRSMYET
CCCCCCCCHHHHHCC		24.3850563091
826MethylationVDAGDSWRSMYETPS
CCCCCCHHHHHCCCC		18.59-
827PhosphorylationDAGDSWRSMYETPSL
CCCCCHHHHHCCCCH		21.3229209046
829PhosphorylationGDSWRSMYETPSLEQ
CCCHHHHHCCCCHHH		20.2129209046
831PhosphorylationSWRSMYETPSLEQDL
CHHHHHCCCCHHHHH		10.7329209046
833PhosphorylationRSMYETPSLEQDLER
HHHHCCCCHHHHHHH		52.5429209046
942N-linked_GlycosylationPVPPEFWNKSMLEKP
CCCHHHCCHHHCCCC		31.679013598
1034PhosphorylationSTPKHLHSLNLLSSE
CCCCCHHHCCCCCCC		25.8827732954
1039PhosphorylationLHSLNLLSSEGGSDE
HHHCCCCCCCCCCCH		29.5227732954
1040PhosphorylationHSLNLLSSEGGSDEH
HHCCCCCCCCCCCHH		39.9827732954
1092PhosphorylationNYNQEWWSLRLKYQG
CCCCCHHEEEEEECC		12.5124719451
1191N-linked_GlycosylationQLITGQPNMSASAML
HHHHCCCCCCHHHHH		29.209013598
1233PhosphorylationWTPNSARSEGPLPDS
CCCCCCCCCCCCCCC		46.7725693802
1240PhosphorylationSEGPLPDSGRVSFLG
CCCCCCCCCCEEEEE		26.9325693802
1244PhosphorylationLPDSGRVSFLGLDLD
CCCCCCEEEEEECCC		17.2525693802
1292PhosphorylationHRSLHRHSHGPQFGS
HHHHHCCCCCCCCCC		30.0528857561
1299PhosphorylationSHGPQFGSEVELRHS
CCCCCCCCCEECCCC		39.4916476442
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
1299SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1299SPhosphorylation

12386153
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 ACE_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYH9_HUMANMYH9physical
16186248
CSK21_HUMANCSNK2A1physical
16186248
ACTB_HUMANACTBphysical
16186248
BKRB2_HUMANBDKRB2physical
17077303
ANGT_HUMANAGTphysical
10969042
ANGT_HUMANAGTphysical
15283675
ANGT_HUMANAGTphysical
23056909
Drug and Disease Associations
Kegg Disease
H00083 Allograft rejection
H00575 Renal tubular dysgenesis
OMIM Disease
601367Ischemic stroke (ISCHSTR)
267430Renal tubular dysgenesis (RTD)
612624Microvascular complications of diabetes 3 (MVCD3)
614519Intracerebral hemorrhage (ICH)
Kegg Drug
D00251 Captopril (JP16/USP/INN); Apopril (TN); Capoten (TN)
D00362 Lisinopril hydrate (JP16); Lisinopril (USP); Lisinopril dihydrate; Prinivil (TN); Zestril (TN)
D00383 Trandolapril (JAN/INN); Mavik (TN)
D00421 Ramipril (USP/INN); Altace (TN)
D00459 Quinapril hydrochloride (JP16/USP); Accupril (TN)
D00620 Benazepril hydrochloride (JAN/USAN); Lotensin (TN)
D00621 Enalapril maleate (JP16/USP); Renivace (TN); Vasotec (TN)
D00622 Fosinopril sodium (USAN); Monopril (TN)
D00623 Moexipril hydrochloride (USAN); Univasc (TN)
D00624 Perindopril erbumine (JAN/USAN); Aceon (TN)
D01069 Cilazapril hydrate (JP16); Cilazapril (USAN); Inhibace (TN)
D01119 Temocapril hydrochloride (JP16/USAN); Acecol (TN)
D01549 Imidapril hydrochloride (JP16); Tanatril (TN)
D01667 Delapril hydrochloride (JAN/USAN); Adecut (TN)
D01900 Alacepril (JP16/INN); Cetapril (TN)
D03077 Benazeprilat (USAN/INN)
D03440 Ceronapril (USAN/INN)
D03752 Quinapril (USP/INN)
D03753 Perindopril (USAN/INN)
D03756 Indolapril hydrochloride (USAN)
D03758 Libenzapril (USAN/INN)
D03760 Pentopril (USAN/INN)
D03763 Pivopril (USAN/INN)
D03765 Spirapril hydrochloride (USAN); Renormax (TN)
D03767 Zofenopril calcium (USAN); Zoprace (TN)
D03769 Enalaprilat (USP); Vasotec (TN)
D03772 Fosinoprilat (USAN/INN)
D03773 Quinaprilat (USAN/INN)
D03775 Spiraprilat (USAN/INN)
D03776 Zofenoprilat arginine (USAN)
D06076 Teprotide (USAN/INN)
D07499 Benazepril (INN); Benazepril Sandoz (TN); Forteekor [veterinary] (TN)
D07699 Cilazapril (INN); Inhibace (TN)
D07781 Delapril (INN); Delaket (TN)
D07892 Enalapril (INN); Enalapril (TN)
D07992 Fosinopril (INN); Monopril (TN)
D08068 Imidapril (INN); Hipertene (TN)
D08131 Lisinopril (INN); Zestril (TN)
D08225 Moexipril (INN)
D08529 Spirapril (INN)
D08566 Temocapril (INN)
D08688 Zofenopril (INN); Zofenil (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACE_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specificinhibitor design.";
Corradi H.R., Schwager S.L.U., Nchinda A.T., Sturrock E.D.,Acharya K.R.;
J. Mol. Biol. 357:964-974(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-641 IN COMPLEX WITHLISINOPRIL; ZINC AND CHLORIDE IONS, AND GLYCOSYLATION AT ASN-54;ASN-74; ASN-146; ASN-318 AND ASN-509.
"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-111; ASN-445 AND ASN-714,AND MASS SPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509; ASN-695 AND ASN-714,AND MASS SPECTROMETRY.
"Identification of N-linked glycosylation sites in human testisangiotensin-converting enzyme and expression of an activedeglycosylated form.";
Yu X.C., Sturrock E.D., Wu Z., Biemann K., Ehlers M.R.W.,Riordan J.F.;
J. Biol. Chem. 272:3511-3519(1997).
Cited for: GLYCOSYLATION AT ASN-38; ASN-54; ASN-111; ASN-146; ASN-509; ASN-695;ASN-714; ASN-760; ASN-942 AND ASN-1191, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"CK2 phosphorylates the angiotensin-converting enzyme and regulatesits retention in the endothelial cell plasma membrane.";
Kohlstedt K., Shoghi F., Mueller-Esterl W., Busse R., Fleming I.;
Circ. Res. 91:749-756(2002).
Cited for: PHOSPHORYLATION AT SER-1299, AND MUTAGENESIS OF SER-1299.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-716, AND MASSSPECTROMETRY.

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