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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi159 – 1591Zinc; catalytic
Active sitei201 – 2011Proton acceptor1 Publication
Metal bindingi202 – 2021Zinc; catalytic
Active sitei248 – 2481Proton acceptor1 Publication
Metal bindingi330 – 3301Zinc; catalytic

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

BRENDAi2.3.2.5. 2681.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441K → A: Lowers activity by approximately 40%. 1 Publication
Mutagenesisi146 – 1461F → A: Lowers activity by approximately 30%. 1 Publication
Mutagenesisi160 – 1601S → A: Reduces activity by about 50%. 1 Publication
Mutagenesisi160 – 1601S → G: Reduces activity by 96%. 1 Publication
Mutagenesisi201 – 2011E → D: Reduces activity by about 98%. 2 Publications
Mutagenesisi201 – 2011E → L or Q: Abolishes activity. 2 Publications
Mutagenesisi207 – 2071W → L: Greatly lowers activity. 1 Publication
Mutagenesisi248 – 2481D → A: Reduces activity by 99%. 2 Publications
Mutagenesisi248 – 2481D → Q: Abolishes activity. 2 Publications
Mutagenesisi304 – 3041Q → L: Lowers activity by approximately 35%. 1 Publication
Mutagenesisi305 – 3051D → A, E or L: Abolishes activity. 2 Publications
Mutagenesisi305 – 3051D → N: Reduces activity by 99%. 2 Publications
Mutagenesisi319 – 3191H → L: Reduces activity by 87%. 1 Publication
Mutagenesisi325 – 3251F → A: Greatly lowers activity. 1 Publication
Mutagenesisi329 – 3291W → A: Abolishes activity. 1 Publication

Organism-specific databases

PharmGKBiPA34095.

Chemistry

ChEMBLiCHEMBL4508.
GuidetoPHARMACOLOGYi2411.

Polymorphism and mutation databases

BioMutaiQPCT.
DMDMi2498824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 361333Glutaminyl-peptide cyclotransferasePRO_0000022195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
Disulfide bondi139 ↔ 1641 Publication
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ16769.
PaxDbiQ16769.
PeptideAtlasiQ16769.
PRIDEiQ16769.
TopDownProteomicsiQ16769-2. [Q16769-2]

PTM databases

iPTMnetiQ16769.
PhosphoSiteiQ16769.

Expressioni

Gene expression databases

BgeeiQ16769.
CleanExiHS_QPCT.
ExpressionAtlasiQ16769. baseline and differential.
GenevisibleiQ16769. HS.

Organism-specific databases

HPAiHPA008406.

Interactioni

Protein-protein interaction databases

BioGridi117329. 19 interactions.
IntActiQ16769. 2 interactions.
STRINGi9606.ENSP00000344829.

Chemistry

BindingDBiQ16769.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 383Combined sources
Helixi39 – 424Combined sources
Helixi50 – 5910Combined sources
Helixi62 – 687Combined sources
Helixi71 – 733Combined sources
Helixi82 – 9615Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi116 – 12813Combined sources
Beta strandi131 – 14010Combined sources
Helixi149 – 1513Combined sources
Turni157 – 1604Combined sources
Helixi161 – 17313Combined sources
Helixi175 – 1795Combined sources
Helixi180 – 1823Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi209 – 2124Combined sources
Helixi214 – 22411Combined sources
Beta strandi226 – 2294Combined sources
Turni237 – 2404Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi257 – 2593Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 28016Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi293 – 2953Combined sources
Helixi308 – 3114Combined sources
Turni312 – 3143Combined sources
Beta strandi317 – 3204Combined sources
Turni327 – 3304Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 35919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 35-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16769.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3946. Eukaryota.
ENOG410YIYE. LUCA.
GeneTreeiENSGT00390000003107.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ16769.
KOiK00683.
OMAiSVWHTFD.
OrthoDBiEOG76472W.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541R → W Lowers activity by approximately 30%. 1 Publication
Corresponds to variant rs2255991 [ dbSNP | Ensembl ].
VAR_053956
Natural varianti71 – 711Q → R.
VAR_005569
Natural varianti360 – 3601H → P.1 Publication
Corresponds to variant rs4670696 [ dbSNP | Ensembl ].
VAR_053957

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 8949Missing in isoform 2. CuratedVSP_038487Add
BLAST

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
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. Positions 35-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117329. 19 interactions.
IntActiQ16769. 2 interactions.
STRINGi9606.ENSP00000344829.

Chemistry

BindingDBiQ16769.
ChEMBLiCHEMBL4508.
GuidetoPHARMACOLOGYi2411.

Protein family/group databases

MEROPSiM28.974.

PTM databases

iPTMnetiQ16769.
PhosphoSiteiQ16769.

Polymorphism and mutation databases

BioMutaiQPCT.
DMDMi2498824.

Proteomic databases

EPDiQ16769.
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.
GeneCardsiQPCT.
HGNCiHGNC:9753. QPCT.
HPAiHPA008406.
MIMi607065. gene.
neXtProtiNX_Q16769.
PharmGKBiPA34095.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3946. Eukaryota.
ENOG410YIYE. LUCA.
GeneTreeiENSGT00390000003107.
HOGENOMiHOG000189291.
HOVERGENiHBG009812.
InParanoidiQ16769.
KOiK00683.
OMAiSVWHTFD.
OrthoDBiEOG76472W.
PhylomeDBiQ16769.
TreeFamiTF315071.

Enzyme and pathway databases

BRENDAi2.3.2.5. 2681.

Miscellaneous databases

ChiTaRSiQPCT. human.
EvolutionaryTraceiQ16769.
GeneWikiiQPCT.
GenomeRNAii25797.
NextBioi46985.
PROiQ16769.
SOURCEiSearch...

Gene expression databases

BgeeiQ16769.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase."
    Song I., Chuang C.Z., Bateman R.C. Jr.
    J. Mol. Endocrinol. 13:77-86(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pituitary.
  2. "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.
    , 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: Heart.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1), VARIANT PRO-360.
    Tissue: Lung and Pancreas.
  6. "Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions."
    Schilling S., Hoffmann T., Manhart S., Hoffmann M., Demuth H.U.
    FEBS Lett. 563:191-196(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS GLUTAMYL CYCLASE.
  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.
  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.
  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.
  10. "Structures of glycosylated mammalian glutaminyl cyclases reveal conformational 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-361, GLYCOSYLATION AT ASN-49, DISULFIDE BOND.
  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.

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: April 13, 2016
This is version 137 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.