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Protein

Glutaminyl-peptide cyclotransferase

Gene

QPCT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.3 Publications

Catalytic activityi

L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3.4 Publications

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi159Zinc; catalytic1
Active sitei201Proton acceptor1 Publication1
Metal bindingi202Zinc; catalytic1
Active sitei248Proton acceptor1 Publication1
Metal bindingi330Zinc; catalytic1

GO - Molecular functioni

  • glutaminyl-peptide cyclotransferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular protein modification process Source: ProtInc
  • peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS03941-MONOMER.
BRENDAi2.3.2.5. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiM28.974.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9753. QPCT.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144K → A: Lowers activity by approximately 40%. 1 Publication1
Mutagenesisi146F → A: Lowers activity by approximately 30%. 1 Publication1
Mutagenesisi160S → A: Reduces activity by about 50%. 1 Publication1
Mutagenesisi160S → G: Reduces activity by 96%. 1 Publication1
Mutagenesisi201E → D: Reduces activity by about 98%. 2 Publications1
Mutagenesisi201E → L or Q: Abolishes activity. 2 Publications1
Mutagenesisi207W → L: Greatly lowers activity. 1 Publication1
Mutagenesisi248D → A: Reduces activity by 99%. 2 Publications1
Mutagenesisi248D → Q: Abolishes activity. 2 Publications1
Mutagenesisi304Q → L: Lowers activity by approximately 35%. 1 Publication1
Mutagenesisi305D → A, E or L: Abolishes activity. 2 Publications1
Mutagenesisi305D → N: Reduces activity by 99%. 2 Publications1
Mutagenesisi319H → L: Reduces activity by 87%. 1 Publication1
Mutagenesisi325F → A: Greatly lowers activity. 1 Publication1
Mutagenesisi329W → A: Abolishes activity. 1 Publication1

Organism-specific databases

DisGeNETi25797.
OpenTargetsiENSG00000115828.
PharmGKBiPA34095.

Chemistry databases

ChEMBLiCHEMBL4508.
GuidetoPHARMACOLOGYi2411.

Polymorphism and mutation databases

BioMutaiQPCT.
DMDMi2498824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000002219529 – 361Glutaminyl-peptide cyclotransferaseAdd BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi49N-linked (GlcNAc...)1 Publication1
Disulfide bondi139 ↔ 1641 Publication
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ16769.
PeptideAtlasiQ16769.
PRIDEiQ16769.
TopDownProteomicsiQ16769-2. [Q16769-2]

PTM databases

iPTMnetiQ16769.
PhosphoSitePlusiQ16769.

Expressioni

Gene expression databases

BgeeiENSG00000115828.
CleanExiHS_QPCT.
ExpressionAtlasiQ16769. baseline and differential.
GenevisibleiQ16769. HS.

Organism-specific databases

HPAiHPA008406.

Interactioni

Protein-protein interaction databases

BioGridi117329. 19 interactors.
IntActiQ16769. 3 interactors.
STRINGi9606.ENSP00000344829.

Chemistry databases

BindingDBiQ16769.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 38Combined sources3
Helixi39 – 42Combined sources4
Helixi50 – 59Combined sources10
Helixi62 – 68Combined sources7
Helixi71 – 73Combined sources3
Helixi82 – 96Combined sources15
Beta strandi98 – 100Combined sources3
Beta strandi103 – 111Combined sources9
Beta strandi116 – 128Combined sources13
Beta strandi131 – 140Combined sources10
Helixi149 – 151Combined sources3
Turni157 – 160Combined sources4
Helixi161 – 173Combined sources13
Helixi175 – 179Combined sources5
Helixi180 – 182Combined sources3
Beta strandi191 – 199Combined sources9
Beta strandi204 – 206Combined sources3
Beta strandi209 – 212Combined sources4
Helixi214 – 224Combined sources11
Beta strandi226 – 229Combined sources4
Turni237 – 240Combined sources4
Beta strandi241 – 247Combined sources7
Beta strandi252 – 254Combined sources3
Beta strandi257 – 259Combined sources3
Helixi262 – 264Combined sources3
Helixi265 – 280Combined sources16
Beta strandi284 – 286Combined sources3
Beta strandi293 – 295Combined sources3
Helixi308 – 311Combined sources4
Turni312 – 314Combined sources3
Beta strandi317 – 320Combined sources4
Turni327 – 330Combined sources4
Helixi336 – 338Combined sources3
Helixi341 – 359Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MOImodel-A1-361[»]
2AFMX-ray1.66A/B33-361[»]
2AFOX-ray2.35A/B33-361[»]
2AFSX-ray2.22A/B33-361[»]
2AFUX-ray2.22A/B33-361[»]
2AFWX-ray1.56A/B33-361[»]
2AFXX-ray1.64A/B33-361[»]
2AFZX-ray1.68A/B33-361[»]
2ZEDX-ray1.70A/B33-361[»]
2ZEEX-ray1.99A/B33-361[»]
2ZEFX-ray1.67A/B33-361[»]
2ZEGX-ray2.08A/B33-361[»]
2ZEHX-ray1.80A/B33-361[»]
2ZELX-ray1.97A/B33-361[»]
2ZEMX-ray2.18A/B33-361[»]
2ZENX-ray1.78A/B33-361[»]
2ZEOX-ray1.66A/B33-361[»]
2ZEPX-ray2.10A/B33-361[»]
3PBBX-ray1.95A/B33-361[»]
3PBEX-ray1.95A/B33-361[»]
3SI0X-ray2.10A38-361[»]
4YU9X-ray2.10A/B/C33-361[»]
4YWYX-ray1.95A/B/C1-361[»]
ProteinModelPortaliQ16769.
SMRiQ16769.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16769.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3946. Eukaryota.
ENOG410YIYE. LUCA.
GeneTreeiENSGT00390000003107.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ16769.
KOiK00683.
OMAiSVWHTFD.
OrthoDBiEOG091G09N2.
PhylomeDBiQ16769.
TreeFamiTF315071.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]

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. AlignAdd to basket

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

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

Show »
Length:312
Mass (Da):35,421
Checksum:i21EF984B639F5DEE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05395654R → W Lowers activity by approximately 30%. 1 PublicationCorresponds to variant rs2255991dbSNPEnsembl.1
Natural variantiVAR_00556971Q → R.1
Natural variantiVAR_053957360H → P.1 PublicationCorresponds to variant rs4670696dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03848741 – 89Missing in isoform 2. CuratedAdd BLAST49

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.
CCDSiCCDS1790.1. [Q16769-1]
PIRiI37421.
RefSeqiNP_036545.1. NM_012413.3. [Q16769-1]
UniGeneiHs.79033.

Genome annotation databases

EnsembliENST00000338415; ENSP00000344829; ENSG00000115828. [Q16769-1]
GeneIDi25797.
KEGGihsa:25797.
UCSCiuc002rqg.4. human. [Q16769-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS1790.1. [Q16769-1]
PIRiI37421.
RefSeqiNP_036545.1. NM_012413.3. [Q16769-1]
UniGeneiHs.79033.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MOImodel-A1-361[»]
2AFMX-ray1.66A/B33-361[»]
2AFOX-ray2.35A/B33-361[»]
2AFSX-ray2.22A/B33-361[»]
2AFUX-ray2.22A/B33-361[»]
2AFWX-ray1.56A/B33-361[»]
2AFXX-ray1.64A/B33-361[»]
2AFZX-ray1.68A/B33-361[»]
2ZEDX-ray1.70A/B33-361[»]
2ZEEX-ray1.99A/B33-361[»]
2ZEFX-ray1.67A/B33-361[»]
2ZEGX-ray2.08A/B33-361[»]
2ZEHX-ray1.80A/B33-361[»]
2ZELX-ray1.97A/B33-361[»]
2ZEMX-ray2.18A/B33-361[»]
2ZENX-ray1.78A/B33-361[»]
2ZEOX-ray1.66A/B33-361[»]
2ZEPX-ray2.10A/B33-361[»]
3PBBX-ray1.95A/B33-361[»]
3PBEX-ray1.95A/B33-361[»]
3SI0X-ray2.10A38-361[»]
4YU9X-ray2.10A/B/C33-361[»]
4YWYX-ray1.95A/B/C1-361[»]
ProteinModelPortaliQ16769.
SMRiQ16769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117329. 19 interactors.
IntActiQ16769. 3 interactors.
STRINGi9606.ENSP00000344829.

Chemistry databases

BindingDBiQ16769.
ChEMBLiCHEMBL4508.
GuidetoPHARMACOLOGYi2411.

Protein family/group databases

MEROPSiM28.974.

PTM databases

iPTMnetiQ16769.
PhosphoSitePlusiQ16769.

Polymorphism and mutation databases

BioMutaiQPCT.
DMDMi2498824.

Proteomic databases

PaxDbiQ16769.
PeptideAtlasiQ16769.
PRIDEiQ16769.
TopDownProteomicsiQ16769-2. [Q16769-2]

Protocols and materials databases

DNASUi25797.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338415; ENSP00000344829; ENSG00000115828. [Q16769-1]
GeneIDi25797.
KEGGihsa:25797.
UCSCiuc002rqg.4. human. [Q16769-1]

Organism-specific databases

CTDi25797.
DisGeNETi25797.
GeneCardsiQPCT.
HGNCiHGNC:9753. QPCT.
HPAiHPA008406.
MIMi607065. gene.
neXtProtiNX_Q16769.
OpenTargetsiENSG00000115828.
PharmGKBiPA34095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3946. Eukaryota.
ENOG410YIYE. LUCA.
GeneTreeiENSGT00390000003107.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ16769.
KOiK00683.
OMAiSVWHTFD.
OrthoDBiEOG091G09N2.
PhylomeDBiQ16769.
TreeFamiTF315071.

Enzyme and pathway databases

BioCyciZFISH:HS03941-MONOMER.
BRENDAi2.3.2.5. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiQPCT. human.
EvolutionaryTraceiQ16769.
GeneWikiiQPCT.
GenomeRNAii25797.
PROiQ16769.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115828.
CleanExiHS_QPCT.
ExpressionAtlasiQ16769. baseline and differential.
GenevisibleiQ16769. HS.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQPCT_HUMAN
AccessioniPrimary (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: November 30, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.