ANGT_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANGT_RAT
• UniProt AC: P01015
• Protein Name: Angiotensinogen
• Gene Name: Agt
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 477
• 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 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets..
• Protein Sequence: MTPTGAGLKATIFCILTWVSLTAGDRVYIHPFHLLYYSKSTCAQLENPSVETLPEPTFEPVPIQAKTSPVDEKTLRDKLVLATEKLEAEDRQRAAQVAMIANFMGFRMYKMLSEARGVASGAVLSPPALFGTLVSFYLGSLDPTASQLQVLLGVPVKEGDCTSRLDGHKVLTALQAVQGLLVTQGGSSSQTPLLQSTVVGLFTAPGLRLKQPFVESLGPFTPAIFPRSLDLSTDPVLAAQKINRFVQAVTGWKMNLPLEGVSTDSTLFFNTYVHFQGKMRGFSQLTGLHEFWVDNSTSVSVPMLSGTGNFQHWSDAQNNFSVTRVPLGESVTLLLIQPQCASDLDRVEVLVFQHDFLTWIKNPPPRAIRLTLPQLEIRGSYNLQDLLAQAKLSTLLGAEANLGKMGDTNPRVGEVLNSILLELQAGEEEQPTESAQQPGSPEVLDVTLSSPFLFAIYERDSGALHFLGRVDNPQNVV

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
11	Phosphorylation	TGAGLKATIFCILTW CCHHHHHHHHHHHHH	17.01	16641100
28	Phosphorylation	LTAGDRVYIHPFHLL CCCCCCEEECCCEEE	8.39	16641100
36	Phosphorylation	IHPFHLLYYSKSTCA ECCCEEEEEECCCCC	16.44	16641100
37	Phosphorylation	HPFHLLYYSKSTCAQ CCCEEEEEECCCCCC	15.02	16641100
38	Phosphorylation	PFHLLYYSKSTCAQL CCEEEEEECCCCCCC	13.43	16641100
40	Phosphorylation	HLLYYSKSTCAQLEN EEEEEECCCCCCCCC	23.84	23984901
41	Phosphorylation	LLYYSKSTCAQLENP EEEEECCCCCCCCCC	18.65	23984901
49	Phosphorylation	CAQLENPSVETLPEP CCCCCCCCCCCCCCC	44.14	23984901
52	Phosphorylation	LENPSVETLPEPTFE CCCCCCCCCCCCCCC	45.52	23984901
57	Phosphorylation	VETLPEPTFEPVPIQ CCCCCCCCCCCCCCC	38.68	25575281
295	N-linked_Glycosylation	LHEFWVDNSTSVSVP CEEEEECCCCEEEEE	37.25	-
319	N-linked_Glycosylation	HWSDAQNNFSVTRVP CCCCCCCCEEEEEEE	20.63	-

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

Oops, there are no upstream regulatory protein records of ANGT_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANGT_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ANGT_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ANGT_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.