QPCT

Functionⁱ

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.

3 Publications

Caution

It is unclear whether this protein requires a metal cofactor for catalysis. It was originally proposed to be a Zn²⁺-dependent metalloenzyme based on structural similarities to bacterial aminopeptidases and the observation that it can bind Zn²⁺ ions, typically in a 1:1 stoichiometry (PubMed:18072935, PubMed:21288892). However, a recent study suggests a Zn²⁺-independent catalytic mechanism (By similarity).By similarityCurated2 Publications

Catalytic activityⁱ

N-terminal L-glutaminyl-[peptide]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
N-terminal 5-oxo-L-prolyl-[peptide]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
NH₄⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
  Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S.
  J. Mol. Biol. 379:966-980(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.8
  "Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation."
  Huang K.-F., Liu Y.-L., Cheng W.-J., Ko T.-P., Wang A.H.-J.
  Proc. Natl. Acad. Sci. U.S.A. 102:13117-13122(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-144; PHE-146; GLU-201; TRP-207; ASP-248; GLN-304; ASP-305; PHE-325 AND TRP-329, CHARACTERIZATION OF VARIANT TRP-54.
- Ref.9
  "A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
  Huang K.F., Wang Y.R., Chang E.C., Chou T.L., Wang A.H.
  Biochem. J. 411:181-190(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319.
- Ref.11
  "Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
  Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
  J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY.
EC:
2.3.2.5
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Isolation of an isoenzyme of human glutaminyl cyclase: retention in the Golgi complex suggests involvement in the protein maturation machinery."
  Cynis H., Rahfeld J.U., Stephan A., Kehlen A., Koch B., Wermann M., Demuth H.U., Schilling S.
  J. Mol. Biol. 379:966-980(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.8
  "Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation."
  Huang K.-F., Liu Y.-L., Cheng W.-J., Ko T.-P., Wang A.H.-J.
  Proc. Natl. Acad. Sci. U.S.A. 102:13117-13122(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-144; PHE-146; GLU-201; TRP-207; ASP-248; GLN-304; ASP-305; PHE-325 AND TRP-329, CHARACTERIZATION OF VARIANT TRP-54.
- Ref.9
  "A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis."
  Huang K.F., Wang Y.R., Chang E.C., Chou T.L., Wang A.H.
  Biochem. J. 411:181-190(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 33-361 OF MUTANTS ALA-160; GLY-160; ASP-201; LEU-201; GLN-201; ALA-248; GLN-248; ALA-305; GLU-305 AND LEU-319 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF SER-160; GLU-201; ASP-248; ASP-305 AND HIS-319.
- Ref.11
  "Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding."
  Huang K.F., Liaw S.S., Huang W.L., Chia C.Y., Lo Y.C., Chen Y.L., Wang A.H.
  J. Biol. Chem. 286:12439-12449(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-361 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
N-terminal L-glutaminyl-[peptide]
N-terminal L-glutamine residue
zoom
=
N-terminal 5-oxo-L-prolyl-[peptide]
N-terminal 5-oxo-L-proline residue
zoom
+
NH₄⁺
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	159	ZincCombined sources4 Publications	1
Active siteⁱ	201	Proton acceptor1 Publication	1
Metal bindingⁱ	202	ZincCombined sources4 Publications	1
Active siteⁱ	248	Proton acceptor1 Publication	1
Metal bindingⁱ	330	ZincCombined sources4 Publications	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	2.3.2.5, 2681
PathwayCommonsⁱ	Q16769
Reactomeⁱ	R-HSA-6798695, Neutrophil degranulation
SignaLinkⁱ	Q16769

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M28.974

MEROPSⁱ

M28.974

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutaminyl-peptide cyclotransferase (EC:2.3.2.5) Alternative name(s): Glutaminyl cyclase Short name: QC Short name: sQC Glutaminyl-tRNA cyclotransferase Glutamyl cyclase Short name: EC
Gene namesⁱ	Name:QPCT
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9753, QPCT
MIMⁱ	607065, gene
neXtProtⁱ	NX_Q16769
VEuPathDBⁱ	HostDB:ENSG00000115828

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	144	K → A: Lowers activity by approximately 40%. 1 Publication	1
Mutagenesisⁱ	146	F → A: Lowers activity by approximately 30%. 1 Publication	1
Mutagenesisⁱ	160	S → A: Reduces activity by about 50%. 1 Publication	1
Mutagenesisⁱ	160	S → G: Reduces activity by 96%. 1 Publication	1
Mutagenesisⁱ	201	E → D: Reduces activity by about 98%. 2 Publications	1
Mutagenesisⁱ	201	E → L or Q: Abolishes activity. 2 Publications	1
Mutagenesisⁱ	207	W → L: Greatly lowers activity. 1 Publication	1
Mutagenesisⁱ	248	D → A: Reduces activity by 99%. 2 Publications	1
Mutagenesisⁱ	248	D → Q: Abolishes activity. 2 Publications	1
Mutagenesisⁱ	304	Q → L: Lowers activity by approximately 35%. 1 Publication	1
Mutagenesisⁱ	305	D → A, E or L: Abolishes activity. 2 Publications	1
Mutagenesisⁱ	305	D → N: Reduces activity by 99%. 2 Publications	1
Mutagenesisⁱ	319	H → L: Reduces activity by 87%. 1 Publication	1
Mutagenesisⁱ	325	F → A: Greatly lowers activity. 1 Publication	1
Mutagenesisⁱ	329	W → A: Abolishes activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	25797
Open Targets More...OpenTargetsⁱ	ENSG00000115828
PharmGKBⁱ	PA34095

Miscellaneous databases

Pharosⁱ	Q16769, Tchem

Pharosⁱ

Q16769, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL4508
Drug and drug target database More...DrugBankⁱ	DB04581, 1-benzylimidazole DB04636, Glutamine t-butyl ester DB04622, N-acetylhistamine
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2411

Genetic variation databases

BioMutaⁱ	QPCT
DMDMⁱ	2498824

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 28	Sequence analysisAdd BLAST		28
ChainⁱPRO_0000022195	29 – 361	Glutaminyl-peptide cyclotransferaseAdd BLAST		333

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	49	N-linked (GlcNAc...) asparagine1 Publication	1
Disulfide bondⁱ	139 ↔ 164	1 Publication
Glycosylationⁱ	296	N-linked (GlcNAc...) asparagineSequence analysis	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-1301
jPOSTⁱ	Q16769
MassIVEⁱ	Q16769
PaxDbⁱ	Q16769
PeptideAtlas More...PeptideAtlasⁱ	Q16769
PRIDEⁱ	Q16769
ProteomicsDBⁱ	61056 [Q16769-1] 61057 [Q16769-2]
TopDownProteomicsⁱ	Q16769-2 [Q16769-2]

PTM databases

GlyGenⁱ	Q16769, 2 sites, 2 N-linked glycans (1 site)
iPTMnetⁱ	Q16769
PhosphoSitePlusⁱ	Q16769

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000115828, Expressed in bone marrow and 217 other tissues
ExpressionAtlasⁱ	Q16769, baseline and differential
Genevisibleⁱ	Q16769, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000115828, Tissue enhanced (adrenal gland, epididymis)

HPAⁱ

ENSG00000115828, Tissue enhanced (adrenal gland, epididymis)

Interactionⁱ

Binary interactionsⁱ

Q16769

With	#Exp.	IntAct
UBQLN2 [Q9UHD9]	3	EBI-2856807,EBI-947187

Protein-protein interaction databases

BioGRIDⁱ	117329, 39 interactors
IntActⁱ	Q16769, 25 interactors
Molecular INTeraction database More...MINTⁱ	Q16769
STRINGⁱ	9606.ENSP00000344829

Chemistry databases

BindingDBⁱ

Q16769

Miscellaneous databases

RNActⁱ	Q16769, protein

RNActⁱ

Q16769, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	36 – 38	Combined sources	3
Helixⁱ	39 – 42	Combined sources	4
Helixⁱ	50 – 59	Combined sources	10
Helixⁱ	62 – 68	Combined sources	7
Helixⁱ	71 – 73	Combined sources	3
Helixⁱ	82 – 96	Combined sources	15
Beta strandⁱ	98 – 100	Combined sources	3
Beta strandⁱ	103 – 111	Combined sources	9
Beta strandⁱ	116 – 128	Combined sources	13
Beta strandⁱ	131 – 140	Combined sources	10
Helixⁱ	149 – 151	Combined sources	3
Turnⁱ	157 – 160	Combined sources	4
Helixⁱ	161 – 173	Combined sources	13
Helixⁱ	175 – 179	Combined sources	5
Helixⁱ	180 – 182	Combined sources	3
Beta strandⁱ	191 – 199	Combined sources	9
Beta strandⁱ	204 – 206	Combined sources	3
Beta strandⁱ	209 – 212	Combined sources	4
Helixⁱ	214 – 224	Combined sources	11
Beta strandⁱ	226 – 229	Combined sources	4
Turnⁱ	237 – 240	Combined sources	4
Beta strandⁱ	241 – 247	Combined sources	7
Beta strandⁱ	252 – 254	Combined sources	3
Beta strandⁱ	257 – 259	Combined sources	3
Helixⁱ	262 – 264	Combined sources	3
Helixⁱ	265 – 280	Combined sources	16
Beta strandⁱ	284 – 286	Combined sources	3
Beta strandⁱ	293 – 295	Combined sources	3
Helixⁱ	308 – 311	Combined sources	4
Turnⁱ	312 – 314	Combined sources	3
Beta strandⁱ	317 – 320	Combined sources	4
Turnⁱ	327 – 330	Combined sources	4
Helixⁱ	336 – 338	Combined sources	3
Helixⁱ	341 – 359	Combined sources	19

Show more details

3D structure databases

SMRⁱ	Q16769
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q16769

EvolutionaryTraceⁱ

Q16769

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glutaminyl-peptide cyclotransferase family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG3946, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000003107
HOGENOMⁱ	CLU_045003_1_0_1
InParanoidⁱ	Q16769
OMAⁱ	HTFDDNE
Database of Orthologous Groups More...OrthoDBⁱ	1257754at2759
PhylomeDBⁱ	Q16769
TreeFamⁱ	TF315071

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03880, M28_QC_like, 1 hit
InterProⁱ	View protein in InterPro IPR037457, M28_QC IPR007484, Peptidase_M28 IPR040234, QC/QCL
PANTHERⁱ	PTHR12283, PTHR12283, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04389, Peptidase_M28, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q16769-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK NYHQPAILNS 
        60         70         80         90        100
SALRQIAEGT SISEMWQNDL QPLLIERYPG SPGSYAARQH IMQRIQRLQA 
       110        120        130        140        150
DWVLEIDTFL SQTPYGYRSF SNIISTLNPT AKRHLVLACH YDSKYFSHWN 
       160        170        180        190        200
NRVFVGATDS AVPCAMMLEL ARALDKKLLS LKTVSDSKPD LSLQLIFFDG 
       210        220        230        240        250
EEAFLHWSPQ DSLYGSRHLA AKMASTPHPP GARGTSQLHG MDLLVLLDLI 
       260        270        280        290        300
GAPNPTFPNF FPNSARWFER LQAIEHELHE LGLLKDHSLE GRYFQNYSYG 
       310        320        330        340        350
GVIQDDHIPF LRRGVPVLHL IPSPFPEVWH TMDDNEENLD ESTIDNLNKI 
       360 
LQVFVLEYLH L

Length:361

Mass (Da):40,877

Last modified:November 1, 1997 - v1

Checksum:ⁱ32C26041BCF5ED75

GO

Isoform 2 (identifier: Q16769-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
41-89: Missing.

« Hide

        10         20         30         40         50
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK HIMQRIQRLQ 
        60         70         80         90        100
ADWVLEIDTF LSQTPYGYRS FSNIISTLNP TAKRHLVLAC HYDSKYFSHW 
       110        120        130        140        150
NNRVFVGATD SAVPCAMMLE LARALDKKLL SLKTVSDSKP DLSLQLIFFD 
       160        170        180        190        200
GEEAFLHWSP QDSLYGSRHL AAKMASTPHP PGARGTSQLH GMDLLVLLDL 
       210        220        230        240        250
IGAPNPTFPN FFPNSARWFE RLQAIEHELH ELGLLKDHSL EGRYFQNYSY 
       260        270        280        290        300
GGVIQDDHIP FLRRGVPVLH LIPSPFPEVW HTMDDNEENL DESTIDNLNK 
       310 
ILQVFVLEYL HL

Show »

Length:312

Mass (Da):35,421

Checksum:ⁱ21EF984B639F5DEE

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B5MCZ9	B5MCZ9_HUMAN	Glutaminyl-peptide cyclotransferase Glutaminyl-peptide cyclotransferase, EC 2.3.2.5	QPCT	284	Annotation score:
C9JS14	C9JS14_HUMAN	Glutaminyl-peptide cyclotransferase Glutaminyl-peptide cyclotransferase, EC 2.3.2.5	QPCT	117	Annotation score:
A0A3B3IUD5	A0A3B3IUD5_HUMAN	Glutaminyl-peptide cyclotransferase Glutaminyl-peptide cyclotransferase, EC 2.3.2.5	QPCT	137	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_053956	54	R → W Lowers activity by approximately 30%. 1 PublicationCorresponds to variant dbSNP:rs2255991Ensembl.	1
Natural variantⁱVAR_005569	71	Q → R. Corresponds to variant dbSNP:rs895245310Ensembl.	1
Natural variantⁱVAR_053957	360	H → P1 PublicationCorresponds to variant dbSNP:rs4670696Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_038487	41 – 89	Missing in isoform 2. CuratedAdd BLAST		49

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1790.1 [Q16769-1]
PIRⁱ	I37421
NCBI Reference Sequences More...RefSeqⁱ	NP_036545.1, NM_012413.3 [Q16769-1]

Genome annotation databases

Ensemblⁱ	ENST00000338415; ENSP00000344829; ENSG00000115828
GeneIDⁱ	25797
KEGGⁱ	hsa:25797
MANE-Selectⁱ	ENST00000338415.8; ENSP00000344829.3; NM_012413.4; NP_036545.1
UCSC genome browser More...UCSCⁱ	uc002rqg.4, human [Q16769-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q16769	Glutaminyl-peptide cyclotransferase		PANPA		361	UniRef100_Q16769
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		137
+2
Q16769-2	Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		284	UniRef100_Q16769-2
+1

Protein	Similar proteins		Species	Score	Length	Source
Q16769	Glutaminyl-peptide cyclotransferase		PANPA		361	UniRef90_Q16769
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		137
Isoform 2 of Glutaminyl-peptide cyclotransferase		HUMAN		312
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		284
+3

Protein	Similar proteins		Species	Score	Length	Source
Q16769	Glutaminyl-peptide cyclotransferase		PANPA		361	UniRef50_Q16769
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		137
Glutaminyl-peptide cyclotransferase (Fragment)		MONMO		488
Glutaminyl-peptide cyclotransferase		VARKO		468
Glutaminyl-peptide cyclotransferase		HETGA		472
+15

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X71125 mRNA Translation: CAA50438.1 X67731 mRNA Translation: CAA47961.1 AK290605 mRNA Translation: BAF83294.1 AC007391 Genomic DNA Translation: AAY14804.1 CH471053 Genomic DNA Translation: EAX00392.1 CH471053 Genomic DNA Translation: EAX00394.1 CH471053 Genomic DNA Translation: EAX00396.1 BC036721 mRNA Translation: AAH36721.1 BC047756 mRNA Translation: AAH47756.1
CCDSⁱ	CCDS1790.1 [Q16769-1]
PIRⁱ	I37421
RefSeqⁱ	NP_036545.1, NM_012413.3 [Q16769-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2AFM	X-ray	1.66	A/B	33-361	[»]
	2AFO	X-ray	2.35	A/B	33-361	[»]
	2AFS	X-ray	2.22	A/B	33-361	[»]
	2AFU	X-ray	2.22	A/B	33-361	[»]
	2AFW	X-ray	1.56	A/B	33-361	[»]
	2AFX	X-ray	1.64	A/B	33-361	[»]
	2AFZ	X-ray	1.68	A/B	33-361	[»]
	2ZED	X-ray	1.70	A/B	33-361	[»]
	2ZEE	X-ray	1.99	A/B	33-361	[»]
	2ZEF	X-ray	1.67	A/B	33-361	[»]
	2ZEG	X-ray	2.08	A/B	33-361	[»]
	2ZEH	X-ray	1.80	A/B	33-361	[»]
	2ZEL	X-ray	1.97	A/B	33-361	[»]
	2ZEM	X-ray	2.18	A/B	33-361	[»]
	2ZEN	X-ray	1.78	A/B	33-361	[»]
	2ZEO	X-ray	1.66	A/B	33-361	[»]
	2ZEP	X-ray	2.10	A/B	33-361	[»]
	3PBB	X-ray	1.95	A/B	33-361	[»]
	3PBE	X-ray	1.95	A/B	33-361	[»]
	3SI0	X-ray	2.10	A	38-361	[»]
	4YU9	X-ray	2.10	A/B/C	33-361	[»]
	4YWY	X-ray	1.95	A/B/C	1-361	[»]
	6GBX	X-ray	1.72	A/B/C	33-361	[»]
	6YI1	X-ray	1.92	A/B	35-361	[»]
	6YJY	X-ray	1.67	A/B	35-361	[»]
	7COZ	X-ray	1.85	A/B/C	35-361	[»]
	7CP0	X-ray	1.70	A/B/C	35-361	[»]
SMRⁱ	Q16769
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	117329, 39 interactors
IntActⁱ	Q16769, 25 interactors
MINTⁱ	Q16769
STRINGⁱ	9606.ENSP00000344829

Chemistry databases

BindingDBⁱ	Q16769
ChEMBLⁱ	CHEMBL4508
DrugBankⁱ	DB04581, 1-benzylimidazole DB04636, Glutamine t-butyl ester DB04622, N-acetylhistamine
GuidetoPHARMACOLOGYⁱ	2411

Protein family/group databases

MEROPSⁱ	M28.974

MEROPSⁱ

M28.974

PTM databases

GlyGenⁱ	Q16769, 2 sites, 2 N-linked glycans (1 site)
iPTMnetⁱ	Q16769
PhosphoSitePlusⁱ	Q16769

Genetic variation databases

BioMutaⁱ	QPCT
DMDMⁱ	2498824

Proteomic databases

CPTACⁱ	CPTAC-1301
jPOSTⁱ	Q16769
MassIVEⁱ	Q16769
PaxDbⁱ	Q16769
PeptideAtlasⁱ	Q16769
PRIDEⁱ	Q16769
ProteomicsDBⁱ	61056 [Q16769-1] 61057 [Q16769-2]
TopDownProteomicsⁱ	Q16769-2 [Q16769-2]

Protocols and materials databases

Antibodypediaⁱ	1981, 226 antibodies from 28 providers
The DNASU plasmid repository More...DNASUⁱ	25797

Genome annotation databases

Ensemblⁱ	ENST00000338415; ENSP00000344829; ENSG00000115828
GeneIDⁱ	25797
KEGGⁱ	hsa:25797
MANE-Selectⁱ	ENST00000338415.8; ENSP00000344829.3; NM_012413.4; NP_036545.1
UCSCⁱ	uc002rqg.4, human [Q16769-1]

Organism-specific databases

CTDⁱ	25797
DisGeNETⁱ	25797
GeneCardsⁱ	QPCT
HGNCⁱ	HGNC:9753, QPCT
HPAⁱ	ENSG00000115828, Tissue enhanced (adrenal gland, epididymis)
MIMⁱ	607065, gene
neXtProtⁱ	NX_Q16769
OpenTargetsⁱ	ENSG00000115828
PharmGKBⁱ	PA34095
VEuPathDBⁱ	HostDB:ENSG00000115828
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3946, Eukaryota
GeneTreeⁱ	ENSGT00390000003107
HOGENOMⁱ	CLU_045003_1_0_1
InParanoidⁱ	Q16769
OMAⁱ	HTFDDNE
OrthoDBⁱ	1257754at2759
PhylomeDBⁱ	Q16769
TreeFamⁱ	TF315071

Enzyme and pathway databases

BRENDAⁱ	2.3.2.5, 2681
PathwayCommonsⁱ	Q16769
Reactomeⁱ	R-HSA-6798695, Neutrophil degranulation
SignaLinkⁱ	Q16769

Miscellaneous databases

BioGRID-ORCSⁱ	25797, 8 hits in 1039 CRISPR screens
ChiTaRSⁱ	QPCT, human
EvolutionaryTraceⁱ	Q16769
GeneWikiⁱ	QPCT
GenomeRNAiⁱ	25797
Pharosⁱ	Q16769, Tchem
Protein Ontology More...PROⁱ	PR:Q16769
RNActⁱ	Q16769, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000115828, Expressed in bone marrow and 217 other tissues
ExpressionAtlasⁱ	Q16769, baseline and differential
Genevisibleⁱ	Q16769, HS

Family and domain databases

CDDⁱ	cd03880, M28_QC_like, 1 hit
InterProⁱ	View protein in InterPro IPR037457, M28_QC IPR007484, Peptidase_M28 IPR040234, QC/QCL
PANTHERⁱ	PTHR12283, PTHR12283, 1 hit
Pfamⁱ	View protein in Pfam PF04389, Peptidase_M28, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	QPCT_HUMAN
Accessionⁱ	Q16769Primary (citable) accession number: Q16769 Secondary accession number(s): Q16770, Q3KRG6, Q53TR4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 1, 1997
	Last modified:	February 23, 2022
	This is version 172 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

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Supporting data

UniProtKB - Q16769 (QPCT_HUMAN)

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Glutaminyl-peptide cyclotransferase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

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Sites

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GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Extracellular region or secreted

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Q16769

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ