QPCT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: QPCT_HUMAN
• UniProt AC: Q16769
• Protein Name: Glutaminyl-peptide cyclotransferase
• Gene Name: QPCT
• Organism: Homo sapiens (Human).
• Sequence Length: 361
• Subcellular Localization: Secreted .
• Protein Description: 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..
• Protein Sequence: MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL

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
49	N-linked_Glycosylation	YHQPAILNSSALRQI CCCCCCCCHHHHHHH	28.01	21671571
119	Phosphorylation	QTPYGYRSFSNIIST CCCCCCCHHHHHHHH	25.25	-
126	Phosphorylation	SFSNIISTLNPTAKR HHHHHHHHCCCCHHH	21.83	-
130	Phosphorylation	IISTLNPTAKRHLVL HHHHCCCCHHHHEEE	43.68	-
132	Ubiquitination	STLNPTAKRHLVLAC HHCCCCHHHHEEEEE	42.71	-
180	Phosphorylation	ALDKKLLSLKTVSDS HHHHHHHCCCCCCCC	37.95	24719451
222	Ubiquitination	GSRHLAAKMASTPHP CHHHHHHHHHCCCCC	29.41	22817900
264	Phosphorylation	FPNFFPNSARWFERL CCCCCCCHHHHHHHH	21.32	22496350
285	Ubiquitination	LHELGLLKDHSLEGR HHHCCCCCCCCCCCC	59.44	22817900
296	N-linked_Glycosylation	LEGRYFQNYSYGGVI CCCCCCCCCCCCCEE	20.16	UniProtKB CARBOHYD

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHRS4_HUMAN	DHRS4	physical	26186194
NUBP1_HUMAN	NUBP1	physical	26186194
FRAS1_HUMAN	FRAS1	physical	26186194
ELP3_HUMAN	ELP3	physical	26186194
NUBP2_HUMAN	NUBP2	physical	26186194
UBAP2_HUMAN	UBAP2	physical	26186194
DHRS4_HUMAN	DHRS4	physical	28514442
NUBP1_HUMAN	NUBP1	physical	28514442
ELP3_HUMAN	ELP3	physical	28514442
NUBP2_HUMAN	NUBP2	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structures of glycosylated mammalian glutaminyl cyclases revealconformational variability near the active center.";
Ruiz-Carrillo D., Koch B., Parthier C., Wermann M., Dambe T.,Buchholz M., Ludwig H.H., Heiser U., Rahfeld J.U., Stubbs M.T.,Schilling S., Demuth H.U.;
Biochemistry 50:6280-6288(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-361, GLYCOSYLATION ATASN-49, AND DISULFIDE BOND.
PubMed: 21671571