ANGT_HUMAN - dbPTM
ANGT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANGT_HUMAN
UniProt AC P01019
Protein Name Angiotensinogen
Gene Name AGT
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Secreted.
Protein Description Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.; Angiotensin-2: acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone.; Angiotensin-3: stimulates aldosterone release.; Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets..
Protein Sequence MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA
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
8O-linked_GlycosylationMRKRAPQSEMAPAGV
CCCCCCHHHCCCCCH
28.4230620550
8PhosphorylationMRKRAPQSEMAPAGV
CCCCCCHHHCCCCCH
28.4226074081
16O-linked_GlycosylationEMAPAGVSLRATILC
HCCCCCHHHHHHHHH
15.9530620550
16PhosphorylationEMAPAGVSLRATILC
HCCCCCHHHHHHHHH
15.9526074081
20PhosphorylationAGVSLRATILCLLAW
CCHHHHHHHHHHHHH
14.1926074081
34Beta-decarboxylated aspartateWAGLAAGDRVYIHPF
HHHHHCCCCEEEECC
31.95-
34DecarboxylationWAGLAAGDRVYIHPF
HHHHHCCCCEEEECC
31.9517138938
47N-linked_GlycosylationPFHLVIHNESTCEQL
CCEEEEECHHHHHHH
33.523934016
47N-linked_GlycosylationPFHLVIHNESTCEQL
CCEEEEECHHHHHHH
33.523934016
100UbiquitinationAKLDTEDKLRAAMVG
EECCHHHHHHHHHHH
33.37-
170N-linked_GlycosylationGVPWKDKNCTSRLDA
CCCCCCCCCCCCCCH
44.429757569
170N-linked_GlycosylationGVPWKDKNCTSRLDA
CCCCCCCCCCCCCCH
44.423934016
242PhosphorylationLPRSLDFTELDVAAE
ECCCCCCCHHHHHHH
34.9928555341
287AcetylationTYVHFQGKMKGFSLL
EEEEECCEECCEEEE
27.0130586881
304N-linked_GlycosylationPQEFWVDNSTSVSVP
CCEEEECCCCCCCCE
37.259757569
304N-linked_GlycosylationPQEFWVDNSTSVSVP
CCEEEECCCCCCCCE
37.253934016
328N-linked_GlycosylationHWSDIQDNFSVTQVP
CHHHCCCCCEECCCC
18.089757569
328N-linked_GlycosylationHWSDIQDNFSVTQVP
CHHHCCCCCEECCCC
18.083934016
440O-linked_GlycosylationEADEREPTESTQQLN
CCCCCCCCCCCHHCC
37.50OGP

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 ANGT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
34DCarboxylation

17138938

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 ANGT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EWS_HUMANEWSR1physical
16189514
GSDMB_HUMANGSDMBphysical
21988832
RENI_HUMANRENphysical
20927107
RENR_HUMANATP6AP2physical
20927107
NDUA3_HUMANNDUFA3physical
28514442
CALX_HUMANCANXphysical
28514442
GRP78_HUMANHSPA5physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
145500Essential hypertension (EHT)
267430Renal tubular dysgenesis (RTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANGT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-47, 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-47, AND MASS SPECTROMETRY.
"Processing of rat and human angiotensinogen precursors by microsomalmembranes.";
Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.;
Mol. Cell. Endocrinol. 43:31-40(1985).
Cited for: GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328.

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