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Q9NXS2 (QPCTL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaminyl-peptide cyclotransferase-like protein

EC=2.3.2.5
Alternative name(s):
Golgi-resident glutaminyl-peptide cyclotransferase
isoQC
Short name=gQC
Gene names
Name:QPCTL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the biosynthesis of pyroglutamyl peptides. Ref.5 Ref.7

Catalytic activity

L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3. Ref.5 Ref.7

Cofactor

Binds 1 zinc ion per subunit. Ref.7

Subcellular location

Golgi apparatus membrane; Single-pass type I membrane protein Ref.5.

Sequence similarities

Belongs to the glutaminyl-peptide cyclotransferase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

POLR1EQ9GZS11EBI-1052839,EBI-359458

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NXS2-1)

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.
Isoform 2 (identifier: Q9NXS2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     118-211: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Glutaminyl-peptide cyclotransferase-like protein
PRO_0000302002

Regions

Transmembrane35 – 5521Helical; Potential

Sites

Active site2251Proton acceptor
Active site2691Proton acceptor
Metal binding1861Zinc; catalytic
Metal binding2261Zinc; catalytic
Metal binding3511Zinc; catalytic

Natural variations

Alternative sequence118 – 21194Missing in isoform 2.
VSP_054066
Natural variant2141P → L.
Corresponds to variant rs28708996 [ dbSNP | Ensembl ].
VAR_034937

Experimental info

Sequence conflict2951I → T in BAD96356. Ref.2
Sequence conflict3211F → S in BAA90938. Ref.1
Sequence conflict3211F → S in BAD18747. Ref.1
Sequence conflict3341R → G in BAD96356. Ref.2

Secondary structure

.................................................. 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 2DCA79BED029DD4B

FASTA38242,924
        10         20         30         40         50         60 
MRSGGRGRPR LRLGERGLME PLLPPKRRLL PRVRLLPLLL ALAVGSAFYT IWSGWHRRTE 

        70         80         90        100        110        120 
ELPLGRELRV PLIGSLPEAR LRRVVGQLDP QRLWSTYLRP LLVVRTPGSP GNLQVRKFLE 

       130        140        150        160        170        180 
ATLRSLTAGW HVELDPFTAS TPLGPVDFGN VVATLDPRAA RHLTLACHYD SKLFPPGSTP 

       190        200        210        220        230        240 
FVGATDSAVP CALLLELAQA LDLELSRAKK QAAPVTLQLL FLDGEEALKE WGPKDSLYGS 

       250        260        270        280        290        300 
RHLAQLMESI PHSPGPTRIQ AIELFMLLDL LGAPNPTFYS HFPRTVRWFH RLRSIEKRLH 

       310        320        330        340        350        360 
RLNLLQSHPQ EVMYFQPGEP FGSVEDDHIP FLRRGVPVLH LISTPFPAVW HTPADTEVNL 

       370        380 
HPPTVHNLCR ILAVFLAEYL GL 

« Hide

Isoform 2 [UniParc].

Checksum: 9F23194B62336AD3
Show »

FASTA28832,912

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cerebellum.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Kidney.
[5]"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.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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 (1.05 ANGSTROMS) OF 53-382 IN COMPLEXES WITH SYNTHETIC INHIBITORS PBD150 AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000091 mRNA. Translation: BAA90938.1.
AK172764 mRNA. Translation: BAD18747.1.
AK222636 mRNA. Translation: BAD96356.1.
AC007191 Genomic DNA. No translation available.
BC011553 mRNA. Translation: AAH11553.1.
RefSeqNP_001156849.1. NM_001163377.1.
NP_060129.2. NM_017659.3.
UniGeneHs.631556.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PB4X-ray1.13X53-382[»]
3PB6X-ray1.05X53-382[»]
3PB7X-ray1.40X53-382[»]
3PB8X-ray1.13X53-382[»]
3PB9X-ray1.12X53-382[»]
ProteinModelPortalQ9NXS2.
SMRQ9NXS2. Positions 70-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120171. 11 interactions.
IntActQ9NXS2. 4 interactions.
STRING9606.ENSP00000012049.

Protein family/group databases

MEROPSM28.016.

Polymorphism databases

DMDM296452875.

Proteomic databases

PaxDbQ9NXS2.
PRIDEQ9NXS2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000012049; ENSP00000012049; ENSG00000011478.
ENST00000366382; ENSP00000387944; ENSG00000011478.
GeneID54814.
KEGGhsa:54814.
UCSCuc010ekn.3. human.

Organism-specific databases

CTD54814.
GeneCardsGC19P046195.
H-InvDBHIX0015239.
HGNCHGNC:25952. QPCTL.
HPAHPA040797.
neXtProtNX_Q9NXS2.
PharmGKBPA134922163.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298226.
HOGENOMHOG000189291.
HOVERGENHBG009812.
InParanoidQ9NXS2.
OMAQTYFRKD.
OrthoDBEOG76472W.
PhylomeDBQ9NXS2.
TreeFamTF315071.

Gene expression databases

ArrayExpressQ9NXS2.
BgeeQ9NXS2.
CleanExHS_QPCTL.
GenevestigatorQ9NXS2.

Family and domain databases

InterProIPR007484. Peptidase_M28.
[Graphical view]
PfamPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NXS2.
GenomeRNAi54814.
NextBio57549.
PROQ9NXS2.

Entry information

Entry nameQPCTL_HUMAN
AccessionPrimary (citable) accession number: Q9NXS2
Secondary accession number(s): Q53HE4, Q96F74
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM