Glycobiology Advance Access originally published online on September 26, 2003
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Glycobiology vol 14 no 2 pp. 95-101, 2004
© Oxford University Press 2004; all rights reserved.
Biases and complex patterns in the residues flanking protein N-glycosylation sites
2 Department of Biological Services, Weizmann Institute of Science, Rehovot 76100, Israel; and 3 Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Received on June 10, 2003; revised on August 8, 2003; accepted on September 3, 2003
N-Glycosylation, the most common and most versatile protein modification reaction, occurs at the ß-amide of the aspargine of the Asn-Xaa-Ser/Thr sequon. For reasons that are unclear, not all such sequons are glycosylated. To find patterns that affect glycosylation, we examined the amino acid residues from the 20th preceding the sequon to the 20th residue following it, using bioinformatics tools. A clean data set of annotated, experimentally verified, glycosylated and nonglycosylated sequons derived from 617 well-defined nonredundant N- and N-,O-glycoproteins listed in SWISS-PROT (June 2002) was used. NXS and NXT sequons were analyzed separately. Although no overt patterns were found to explain sequon occupancy or nonoccupancy, trends for over- or underrepresentation of certain amino acids at particular positions were statistically significant and different in NXS and NXT sequons. In extension of earlier reports, none of the 80 Asn-Pro-Ser/Thr found were glycosylated, and a markedly low level of glycosylation was seen in sequons with Pro at the position following the Ser/Thr. In addition, a general observation was made that the considerable number of glycosylated sequons in the C-terminal 10 residues of glycoproteins suggests that N-glycosylation in these cases may be posttranslational and not cotranslational, as widely accepted.
1 To whom correspondence should be addressed; e-mail: nathan.sharon{at}weizmann.weizmann.ac.il
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  P. B. Das, P. X. Dinh, I. H. Ansari, M. de Lima, F. A. Osorio, and A. K. Pattnaik The Minor Envelope Glycoproteins GP2a and GP4 of Porcine Reproductive and Respiratory Syndrome Virus Interact with the Receptor CD163 J. Virol., February 15, 2010; 84(4): 1731 - 1740. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Cui, T. Smith, P. W. Robbins, and J. Samuelson Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses PNAS, August 11, 2009; 106(32): 13421 - 13426. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. L. Schulz and M. Aebi Analysis of Glycosylation Site Occupancy Reveals a Role for Ost3p and Ost6p in Site-specific N-Glycosylation Efficiency Mol. Cell. Proteomics, February 1, 2009; 8(2): 357 - 364. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. Sun, S. Parry, M. Panico, H. R. Morris, M. Kjellberg, A. Engstrom, A. Dell, and S. Schedin-Weiss N-Glycans and the N Terminus of Protein C Inhibitor Affect the Cofactor-enhanced Rates of Thrombin Inhibition J. Biol. Chem., July 4, 2008; 283(27): 18601 - 18611. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Koles, J.-M. Lim, K. Aoki, M. Porterfield, M. Tiemeyer, L. Wells, and V. Panin Identification of N-Glycosylated Proteins from the Central Nervous System of Drosophila Melanogaster Glycobiology, December 1, 2007; 17(12): 1388 - 1403. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Kohda, M. Yamada, M. Igura, J. Kamishikiryo, and K. Maenaka New oligosaccharyltransferase assay method Glycobiology, November 1, 2007; 17(11): 1175 - 1182. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J.-M. Krause, P. Berger, J. Roig, V. Singh, and W. E. Merz Rapid Maturation of Glycoprotein Hormone Free {alpha}-Subunit (GPH{alpha}) and GPH{alpha}{alpha} Homodimers Mol. Endocrinol., October 1, 2007; 21(10): 2551 - 2564. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Stahl-Zeng, V. Lange, R. Ossola, K. Eckhardt, W. Krek, R. Aebersold, and B. Domon High Sensitivity Detection of Plasma Proteins by Multiple Reaction Monitoring of N-Glycosites Mol. Cell. Proteomics, October 1, 2007; 6(10): 1809 - 1817. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Hashimoto, S. Goto, S. Kawano, K. F. Aoki-Kinoshita, N. Ueda, M. Hamajima, T. Kawasaki, and M. Kanehisa KEGG as a glycome informatics resource Glycobiology, May 1, 2006; 16(5): 63R - 70R. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Bohne-Lang and C.-W. von der Lieth GlyProt: in silico glycosylation of proteins Nucleic Acids Res., July 1, 2005; 33(suppl_2): W214 - W219. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Bolt, C. Kristensen, and T. D. Steenstrup Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII Glycobiology, May 1, 2005; 15(5): 541 - 547. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Lutteke, M. Frank, and C.-W. von der Lieth Carbohydrate Structure Suite (CSS): analysis of carbohydrate 3D structures derived from the PDB Nucleic Acids Res., January 1, 2005; 33(suppl_1): D242 - D246. [Abstract] [Full Text] [PDF]
|
|