QPCT
entrez
25797
canonical
uniprot
Q16769
canonical
ensembl
ENSG00000115828
resolver
ensp
ENSP00000344829
resolver
genesymbol
QPCT
resolver
hgnc
HGNC:9753
resolver
uniprot
Q16770
resolver
uniprot
Q3KRG6
resolver
uniprot
Q53TR4
resolver
uniprot_entry
QPCT_HUMAN
resolver
uniprot_sec
Q16770
resolver
uniprot_sec
Q3KRG6
resolver
uniprot_sec
Q53TR4
resolver
amino_acid_sequence
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
uniprot
proteins
ec_number
2.3.2.5
uniprot
proteins
function
FUNCTION: Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides. {ECO:0000269|PubMed:15063747, ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}.
uniprot
proteins
mass_dalton
40877
uniprot
proteins
mutagenesis
MUTAGEN 144; /note="K->A: Lowers activity by approximately 40%."; /evidence="ECO:0000269|PubMed:16135565"; MUTAGEN 146; /note="F->A: Lowers activity by approximately 30%."; /evidence="ECO:0000269|PubMed:16135565"; MUTAGEN 160; /note="S->A: Reduces activity by about 50%."; /evidence="ECO:0000269|PubMed:18072935"; MUTAGEN 160; /note="S->G: Reduces activity by 96%."; /evidence="ECO:0000269|PubMed:18072935"; MUTAGEN 201; /note="E->D: Reduces activity by about 98%."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 201; /note="E->L,Q: Abolishes activity."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 207; /note="W->L: Greatly lowers activity."; /evidence="ECO:0000269|PubMed:16135565"; MUTAGEN 248; /note="D->A: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 248; /note="D->Q: Abolishes activity."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 304; /note="Q->L: Lowers activity by approximately 35%."; /evidence="ECO:0000269|PubMed:16135565"; MUTAGEN 305; /note="D->A,E,L: Abolishes activity."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 305; /note="D->N: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935"; MUTAGEN 319; /note="H->L: Reduces activity by 87%."; /evidence="ECO:0000269|PubMed:18072935"; MUTAGEN 325; /note="F->A: Greatly lowers activity."; /evidence="ECO:0000269|PubMed:16135565"; MUTAGEN 329; /note="W->A: Abolishes activity."; /evidence="ECO:0000269|PubMed:16135565
uniprot
proteins
protein_family
Glutaminyl-peptide cyclotransferase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15063747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16135565
uniprot
proteins
pubmed
18072935
uniprot
proteins
pubmed
18486145
uniprot
proteins
pubmed
21288892
uniprot
proteins
pubmed
21671571
uniprot
proteins
pubmed
7999256
uniprot
proteins
sequence_length
361
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18486145}.
uniprot
proteins