Rampant purifying selection conserves positions with posttranslational modifications in human proteins

Molecular Biology and Evolution

Volumn 28, Issue 5, 2011, Pages 1565-1568

  Gray, Vanessa E ^a   Kumar, Sudhir ^a,b  

^a ARIZONA STATE UNIVERSITY   (United States)

^b ARIZONA STATE UNIVERSITY   (United States)

Author keywords

evolution; genomics; posttranslational modifications; proteomics

Indexed keywords

ASPARAGINE; GLYCOSYLATED PROTEIN; SERINE; THREONINE; TYROSINE;

ARTICLE; HUMAN; PROTEIN ANALYSIS; PROTEIN GLYCOSYLATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARAGINE; EVOLUTION, MOLECULAR; HUMANS; MODELS, GENETIC; PHYLOGENY; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; SELECTION, GENETIC; SEQUENCE ALIGNMENT; SERINE; THREONINE; TYROSINE;

EID: 79955407314     PISSN: 07374038     EISSN: 15371719     Source Type: Journal    
DOI: 10.1093/molbev/msr013     Document Type: Article

References (22)

1. Aly A, Higuchi M, Kasper C, Kazazian HJ, Antonarakis S, Hoyer L. 1992. Hemophilia A due to mutations that create new N-glycosylation sites. Proc Natl Acad Sci USA. 89:4933-4937.
2. Apweiler R, Hermjakob H, Sharon N. 1999. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta. 1473:4-8.
3. Ba A, Moses A. 2010. Evolution of characterized phosphorylation sites in budding yeast. Mol Biol Evol. 27:2027-2037.
4. Boekhorst J, van Breukelen B, Heck A, Snel B. 2008. Comparative phosphoproteomics reveals evolutionary and functional conservation of phosphorylation across eukaryotes. Genome Biol. 9:R144.
5. Chen S, Chen F, Li W. 2010. Phosphorylated and non-phosphory-lated serine and threonine residues evolve at different rates in mammals. Mol Biol Evol. 27:2548-2554.
6. Gnad F, Ren S, Cox J, Olsen JV, Macek B, Oroshi M, Mann M. 2007. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phos-phosites. Genome Biol. 8:R250.
7. Kumar S, Suleski M, Markov G, Lawrence S, Marco A, Filipski A. 2009Positional conservation and amino acids shape the correct diagnosis and population frequencies of benign and damaging personal amino acid mutations. Genome Res. 19:1562-1569.
8. Landry C, Levy E, Michnick S. 2009. Weak functional constraints on phosphoproteomes. Trends Genet. 25:193-197.
9. Lee T, Huang H, Hung J, Huang H, Yang Y, Wang T. 2006. dbPTM: an information repository of protein post-translational modification. Nucleic Acids Res. 34:D622-D627.
10. Lemeer S, Heck A. 2009. The phosphoproteomics data explosion. Curr Opin Chem Biol. 13:414-420.
11. Li S, Iakoucheva L, Mooney S, Radivojac P. 2010. Loss of post-translational modification sites in disease. Pac Symp Biocomput. 337-347.
12. Lu P, Wulf G, Zhou X, Davies P, Lu K. 1999. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphory-lated tau protein. Nature 399:784-788. (Pubitemid 29293174)
13. Macek B, Gnad F, Soufi B, Kumar C, Olsen J, Mijakovic I, Mann M. 2008. Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics. 7:299-307. (Pubitemid 351298444)
14. Mann M, Jensen O. 2003. Proteomic analysis of post-translational modifications. Nat Biotechnol. 21:255-261. (Pubitemid 36314808)
15. Mann M, Ong S, Grønborg M, Steen H, Jensen O, Pandey A. 2002. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20:261-268. (Pubitemid 34451062)
16. Marquardt T, Denecke J. 2003. Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies. Eur J Pediatr. 162:359-379. (Pubitemid 36693736)
17. Nakajima M, Koga T, Sakai H, Yamanaka H, Fujiwara R, Yokoi T. 2010N-Glycosylation plays a role in protein folding of human UGT1A9. Biochem Pharmacol. 79:1165-1172.
18. Pruitt K, Tatusova T, Maglott D. 2007. NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res. 35:D61-D65. (Pubitemid 46056171)
19. Rhead B, Karolchik D, Kuhn RM, et al. (23 co-authors). 2010. The UCSC Genome Browser database: update 2010. Nucleic Acids Res. 38:D613-D619.
20. Seo J, Lee K. 2004. Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J Biochem Mol Biol. 37:35-44. (Pubitemid 38402572)
21. Subramanian S, Kumar S. 2006. Evolutionary anatomies of positions and types of disease-associated and neutral amino acid mutations in the human genome. BMC Genomics. 7:306.
22. Tan C, Bodenmiller B, Pasculescu A, Jovanovic M, Hengartner M, Jørgensen C, Bader G, Aebersold R, Pawson T, Linding R. 2009. Comparative analysis reveals conserved protein phosphorylation networks implicated in multiple diseases. Sci Signal. 2:ra39.