Code
import requests
import urllib3
urllib3.disable_warnings()
def fetch_uniprot_data(uniprot_id):
url = f"https://rest.uniprot.org/uniprotkb/{uniprot_id}.json"
response = requests.get(url, verify=False) # Disable SSL verification
response.raise_for_status() # Raise an error for bad status codes
return response.json()
def display_uniprot_data(data):
primary_accession = data.get('primaryAccession', 'N/A')
protein_name = data.get('proteinDescription', {}).get('recommendedName', {}).get('fullName', {}).get('value', 'N/A')
gene_name = data.get('gene', [{'geneName': {'value': 'N/A'}}])[0]['geneName']['value']
organism = data.get('organism', {}).get('scientificName', 'N/A')
function_comment = next((comment for comment in data.get('comments', []) if comment['commentType'] == "FUNCTION"), None)
function = function_comment['texts'][0]['value'] if function_comment else 'N/A'
# Printing the data
print(f"UniProt ID: {primary_accession}")
print(f"Protein Name: {protein_name}")
print(f"Organism: {organism}")
print(f"Function: {function}")
# Replace this with the UniProt ID you want to fetch
uniprot_id = "Q9Y487"
data = fetch_uniprot_data(uniprot_id)
display_uniprot_data(data)UniProt ID: Q9Y487
Protein Name: V-type proton ATPase 116 kDa subunit a 2
Organism: Homo sapiens
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (PubMed:16415858). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (PubMed:18157129). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633)