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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
8 | O-linked_Glycosylation | MRKRAPQSEMAPAGV CCCCCCHHHCCCCCH | 28.42 | 30620550 | |
8 | Phosphorylation | MRKRAPQSEMAPAGV CCCCCCHHHCCCCCH | 28.42 | 26074081 | |
16 | O-linked_Glycosylation | EMAPAGVSLRATILC HCCCCCHHHHHHHHH | 15.95 | 30620550 | |
16 | Phosphorylation | EMAPAGVSLRATILC HCCCCCHHHHHHHHH | 15.95 | 26074081 | |
20 | Phosphorylation | AGVSLRATILCLLAW CCHHHHHHHHHHHHH | 14.19 | 26074081 | |
34 | Beta-decarboxylated aspartate | WAGLAAGDRVYIHPF HHHHHCCCCEEEECC | 31.95 | - | |
34 | Decarboxylation | WAGLAAGDRVYIHPF HHHHHCCCCEEEECC | 31.95 | 17138938 | |
47 | N-linked_Glycosylation | PFHLVIHNESTCEQL CCEEEEECHHHHHHH | 33.52 | 3934016 | |
47 | N-linked_Glycosylation | PFHLVIHNESTCEQL CCEEEEECHHHHHHH | 33.52 | 3934016 | |
100 | Ubiquitination | AKLDTEDKLRAAMVG EECCHHHHHHHHHHH | 33.37 | - | |
170 | N-linked_Glycosylation | GVPWKDKNCTSRLDA CCCCCCCCCCCCCCH | 44.42 | 9757569 | |
170 | N-linked_Glycosylation | GVPWKDKNCTSRLDA CCCCCCCCCCCCCCH | 44.42 | 3934016 | |
242 | Phosphorylation | LPRSLDFTELDVAAE ECCCCCCCHHHHHHH | 34.99 | 28555341 | |
287 | Acetylation | TYVHFQGKMKGFSLL EEEEECCEECCEEEE | 27.01 | 30586881 | |
304 | N-linked_Glycosylation | PQEFWVDNSTSVSVP CCEEEECCCCCCCCE | 37.25 | 9757569 | |
304 | N-linked_Glycosylation | PQEFWVDNSTSVSVP CCEEEECCCCCCCCE | 37.25 | 3934016 | |
328 | N-linked_Glycosylation | HWSDIQDNFSVTQVP CHHHCCCCCEECCCC | 18.08 | 9757569 | |
328 | N-linked_Glycosylation | HWSDIQDNFSVTQVP CHHHCCCCCEECCCC | 18.08 | 3934016 | |
440 | O-linked_Glycosylation | EADEREPTESTQQLN CCCCCCCCCCCHHCC | 37.50 | OGP |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
34 | D | Carboxylation |
| 17138938 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EWS_HUMAN | EWSR1 | physical | 16189514 | |
GSDMB_HUMAN | GSDMB | physical | 21988832 | |
RENI_HUMAN | REN | physical | 20927107 | |
RENR_HUMAN | ATP6AP2 | physical | 20927107 | |
NDUA3_HUMAN | NDUFA3 | physical | 28514442 | |
CALX_HUMAN | CANX | physical | 28514442 | |
GRP78_HUMAN | HSPA5 | physical | 28514442 |
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N-linked Glycosylation | |
Reference | PubMed |
"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. |