CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutaminyl-peptide cyclotransferase 
Protein Synonyms/Alias
 Glutaminyl cyclase; QC; sQC; Glutaminyl-tRNA cyclotransferase; Glutamyl cyclase; EC 
Gene Name
 QPCT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
222GSRHLAAKMASTPHPubiquitination[1]
285LHELGLLKDHSLEGRubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 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. 
Sequence Annotation
 ACT_SITE 201 201 Proton acceptor.
 ACT_SITE 248 248 Proton acceptor.
 METAL 159 159 Zinc; catalytic.
 METAL 202 202 Zinc; catalytic.
 METAL 330 330 Zinc; catalytic.
 CARBOHYD 49 49 N-linked (GlcNAc...).
 CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
 DISULFID 139 164  
Keyword
 3D-structure; Acyltransferase; Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein; Metal-binding; Polymorphism; Reference proteome; Secreted; Signal; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 361 AA 
Protein Sequence
MAGGRHRRVV GTLHLLLLVA ALPWASRGVS PSASAWPEEK NYHQPAILNS SALRQIAEGT 60
SISEMWQNDL QPLLIERYPG SPGSYAARQH IMQRIQRLQA DWVLEIDTFL SQTPYGYRSF 120
SNIISTLNPT AKRHLVLACH YDSKYFSHWN NRVFVGATDS AVPCAMMLEL ARALDKKLLS 180
LKTVSDSKPD LSLQLIFFDG EEAFLHWSPQ DSLYGSRHLA AKMASTPHPP GARGTSQLHG 240
MDLLVLLDLI GAPNPTFPNF FPNSARWFER LQAIEHELHE LGLLKDHSLE GRYFQNYSYG 300
GVIQDDHIPF LRRGVPVLHL IPSPFPEVWH TMDDNEENLD ESTIDNLNKI LQVFVLEYLH 360
L 361 
Gene Ontology
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IDA:UniProtKB.
 GO:0008233; F:peptidase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0017186; P:peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IEA:InterPro. 
Interpro
 IPR007484; Peptidase_M28. 
Pfam
 PF04389; Peptidase_M28 
SMART
  
PROSITE
  
PRINTS