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

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, 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 IONS, CATALYTIC ACTIVITY, COFACTOR, 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 IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
EC:2.3.2.5
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, 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 IONS, CATALYTIC ACTIVITY, COFACTOR, 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 IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
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

Cofactorⁱ

Zn²⁺2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	159	Zinc; catalytic	1
Active siteⁱ	201	Proton acceptor1 Publication	1
Metal bindingⁱ	202	Zinc; catalytic	1
Active siteⁱ	248	Proton acceptor1 Publication	1
Metal bindingⁱ	330	Zinc; catalytic	1

GO - Molecular functionⁱ

glutaminyl-peptide cyclotransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 21288892
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21288892

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular protein modification process
Source: ProtInc
Traceable author statementⁱ
- 7999256
neutrophil degranulation Source: Reactome
peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
Source: UniProtKB
Inferred from direct assayⁱ
- 21288892

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS03941-MONOMER
BRENDAⁱ	2.3.2.5 2681
Reactomeⁱ	R-HSA-6798695 Neutrophil degranulation

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

EuPathDBⁱ	HostDB:ENSG00000115828.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9753 QPCT
MIMⁱ	607065 gene
neXtProtⁱ	NX_Q16769

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

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

Polymorphism and mutation 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

jPOSTⁱ	Q16769
PaxDbⁱ	Q16769
PeptideAtlas More...PeptideAtlasⁱ	Q16769
PRIDEⁱ	Q16769
ProteomicsDBⁱ	61056 61057 [Q16769-2]
TopDownProteomicsⁱ	Q16769-2 [Q16769-2]

PTM databases

iPTMnetⁱ	Q16769
PhosphoSitePlusⁱ	Q16769

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000115828 Expressed in 204 organ(s), highest expression level in bone marrow
CleanExⁱ	HS_QPCT
ExpressionAtlasⁱ	Q16769 baseline and differential
Genevisibleⁱ	Q16769 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA008406

HPAⁱ

HPA008406

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	117329, 22 interactors
IntActⁱ	Q16769, 3 interactors
STRINGⁱ	9606.ENSP00000344829

Chemistry databases

BindingDBⁱ

Q16769

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

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
	1MOI	model	-	A	1-361	[»]
	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	[»]
ProteinModelPortalⁱ	Q16769
SMRⁱ	Q16769
ModBaseⁱ	Search...
MobiDBⁱ	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 ENOG410YIYE LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000003107
HOGENOMⁱ	HOG000189291
HOVERGENⁱ	HBG009812
InParanoidⁱ	Q16769
KEGG Orthology (KO) More...KOⁱ	K00683
OMAⁱ	HYDSKYE
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_like 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 'canonical' 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	QPCT	284	Annotation score:
C9JS14	C9JS14_HUMAN	Glutaminyl-peptide cyclotransferase Glutaminyl-peptide cyclotransferase	QPCT	117	Annotation score:
A0A3B3IUD5	A0A3B3IUD5_HUMAN	Glutaminyl-peptide cyclotransferase Glutaminyl-peptide cyclotransferase	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]
UniGeneⁱ	Hs.79033

Genome annotation databases

Ensemblⁱ	ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1]
GeneIDⁱ	25797
KEGGⁱ	hsa:25797
UCSC genome browser More...UCSCⁱ	uc002rqg.4 human [Q16769-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

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
UPI000059CF34		HUMAN		329
Q16769-2	Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		284	UniRef100_Q16769-2

Protein	Similar proteins		Species	Score	Length	Source
Q16769	Glutaminyl-peptide cyclotransferase		PANPA		361	UniRef90_Q16769
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		137
UPI0006438292		MICMU		402
UPI000C2A5729		Ugandan red Colobus		361
UPI000059CF34		HUMAN		329
+13
Q16769-2	Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		284	UniRef90_Q16769-2
QPCT isoform 4 (Fragment)		PONAB		284
QPCT isoform 2 (Fragment)		PANTR		284
UPI0005F36E7B		COLAP		312
UPI00062A9487		NOMLE		312
+2

Protein	Similar proteins		Species	Score	Length	Source
Q16769	Glutaminyl-peptide cyclotransferase		PANPA		361	UniRef50_Q16769
Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		137
Glutaminyl-peptide cyclotransferase		BOVIN		361
Glutaminyl-peptide cyclotransferase		wild yak		361
Glutaminyl-peptide cyclotransferase		CHICK		355
+99
Q16769-2	Glutaminyl-peptide cyclotransferase (Fragment)		HUMAN		284	UniRef50_Q16769-2
QPCT isoform 4 (Fragment)		PONAB		284
QPCT isoform 2 (Fragment)		PANTR		284
Glutaminyl-peptide cyclotransferase		ANAPL		299
Uncharacterized protein		BAMTH		302
+18

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]
UniGeneⁱ	Hs.79033

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1MOI	model	-	A	1-361	[»]
	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	[»]
ProteinModelPortalⁱ	Q16769
SMRⁱ	Q16769
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	117329, 22 interactors
IntActⁱ	Q16769, 3 interactors
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

iPTMnetⁱ	Q16769
PhosphoSitePlusⁱ	Q16769

Polymorphism and mutation databases

BioMutaⁱ	QPCT
DMDMⁱ	2498824

Proteomic databases

jPOSTⁱ	Q16769
PaxDbⁱ	Q16769
PeptideAtlasⁱ	Q16769
PRIDEⁱ	Q16769
ProteomicsDBⁱ	61056 61057 [Q16769-2]
TopDownProteomicsⁱ	Q16769-2 [Q16769-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	25797
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000338415; ENSP00000344829; ENSG00000115828 [Q16769-1]
GeneIDⁱ	25797
KEGGⁱ	hsa:25797
UCSCⁱ	uc002rqg.4 human [Q16769-1]

Organism-specific databases

CTDⁱ	25797
DisGeNETⁱ	25797
EuPathDBⁱ	HostDB:ENSG00000115828.15
GeneCardsⁱ	QPCT
HGNCⁱ	HGNC:9753 QPCT
HPAⁱ	HPA008406
MIMⁱ	607065 gene
neXtProtⁱ	NX_Q16769
OpenTargetsⁱ	ENSG00000115828
PharmGKBⁱ	PA34095
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3946 Eukaryota ENOG410YIYE LUCA
GeneTreeⁱ	ENSGT00390000003107
HOGENOMⁱ	HOG000189291
HOVERGENⁱ	HBG009812
InParanoidⁱ	Q16769
KOⁱ	K00683
OMAⁱ	HYDSKYE
OrthoDBⁱ	1257754at2759
PhylomeDBⁱ	Q16769
TreeFamⁱ	TF315071

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS03941-MONOMER
BRENDAⁱ	2.3.2.5 2681
Reactomeⁱ	R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSⁱ	QPCT human
EvolutionaryTraceⁱ	Q16769
GeneWikiⁱ	QPCT
GenomeRNAiⁱ	25797
Protein Ontology More...PROⁱ	PR:Q16769
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000115828 Expressed in 204 organ(s), highest expression level in bone marrow
CleanExⁱ	HS_QPCT
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_like IPR007484 Peptidase_M28 IPR040234 QC/QCL
PANTHERⁱ	PTHR12283 PTHR12283, 1 hit
Pfamⁱ	View protein in Pfam PF04389 Peptidase_M28, 1 hit
ProtoNetⁱ	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:	January 16, 2019
	This is version 155 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, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
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
Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q16769 (QPCT_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Glutaminyl-peptide cyclotransferase

Select a section on the left to see content.

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

Chemistry databases

Polymorphism and mutation 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

Protein-protein interaction databases

Chemistry 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

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation 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

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

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