Large-scale analysis of phosphorylation site occupancy in eukaryotic proteins

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Large-scale analysis of phosphorylation site occupancy in eukaryotic proteins. / Rao, R Shyama Prasad; Møller, Ian Max.

I: B B A - Proteins and Proteomics, Bind 1824, Nr. 3, 03.2012, s. 405-412.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Rao, R Shyama Prasad ; Møller, Ian Max. / Large-scale analysis of phosphorylation site occupancy in eukaryotic proteins. I: B B A - Proteins and Proteomics. 2012 ; Bind 1824, Nr. 3. s. 405-412.

Bibtex

@article{5680aacc4b33443e88488f07b7fc2c63,
title = "Large-scale analysis of phosphorylation site occupancy in eukaryotic proteins",
abstract = "Many recent high throughput technologies have enabled large-scale discoveries of new phosphorylation sites and phosphoproteins. Although they have provided a number of insights into protein phosphorylation and the related processes, an inclusive analysis on the nature of phosphorylated sites in proteins is currently lacking. We have therefore analyzed the occurrence and occupancy of phosphorylated sites (~ 100,281) in a large set of eukaryotic proteins (~ 22,995). Phosphorylation probability was found to be much higher in both the  termini of protein sequences and this is much pronounced in transmembrane proteins. A large proportion (51.3%) of occupied sites had a nearby phosphorylation within a distance of 10 amino acids; however, this proportion is very high compared to the expected one (16.9%). The distribution of phosphorylated sites in proteins showed a strong deviation from the expected maximum randomness. An analysis of phosphorylation motifs indicated that just 40 motifs and a much lower number of associated kinases might account for nearly 50% of the known phosphorylations in eukaryotic proteins. Our results provide a broad picture of the phosphorylation sites in eukaryotic proteins.",
keywords = "Motif, Occupancy, Phosphoprotein, Phosphorylation, Probability",
author = "Rao, {R Shyama Prasad} and M{\o}ller, {Ian Max}",
year = "2012",
month = mar,
doi = "10.1016/j.bbapap.2011.12.001",
language = "English",
volume = "1824",
pages = "405--412",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier BV",
number = "3",

}

RIS

TY - JOUR

T1 - Large-scale analysis of phosphorylation site occupancy in eukaryotic proteins

AU - Rao, R Shyama Prasad

AU - Møller, Ian Max

PY - 2012/3

Y1 - 2012/3

N2 - Many recent high throughput technologies have enabled large-scale discoveries of new phosphorylation sites and phosphoproteins. Although they have provided a number of insights into protein phosphorylation and the related processes, an inclusive analysis on the nature of phosphorylated sites in proteins is currently lacking. We have therefore analyzed the occurrence and occupancy of phosphorylated sites (~ 100,281) in a large set of eukaryotic proteins (~ 22,995). Phosphorylation probability was found to be much higher in both the  termini of protein sequences and this is much pronounced in transmembrane proteins. A large proportion (51.3%) of occupied sites had a nearby phosphorylation within a distance of 10 amino acids; however, this proportion is very high compared to the expected one (16.9%). The distribution of phosphorylated sites in proteins showed a strong deviation from the expected maximum randomness. An analysis of phosphorylation motifs indicated that just 40 motifs and a much lower number of associated kinases might account for nearly 50% of the known phosphorylations in eukaryotic proteins. Our results provide a broad picture of the phosphorylation sites in eukaryotic proteins.

AB - Many recent high throughput technologies have enabled large-scale discoveries of new phosphorylation sites and phosphoproteins. Although they have provided a number of insights into protein phosphorylation and the related processes, an inclusive analysis on the nature of phosphorylated sites in proteins is currently lacking. We have therefore analyzed the occurrence and occupancy of phosphorylated sites (~ 100,281) in a large set of eukaryotic proteins (~ 22,995). Phosphorylation probability was found to be much higher in both the  termini of protein sequences and this is much pronounced in transmembrane proteins. A large proportion (51.3%) of occupied sites had a nearby phosphorylation within a distance of 10 amino acids; however, this proportion is very high compared to the expected one (16.9%). The distribution of phosphorylated sites in proteins showed a strong deviation from the expected maximum randomness. An analysis of phosphorylation motifs indicated that just 40 motifs and a much lower number of associated kinases might account for nearly 50% of the known phosphorylations in eukaryotic proteins. Our results provide a broad picture of the phosphorylation sites in eukaryotic proteins.

KW - Motif

KW - Occupancy

KW - Phosphoprotein

KW - Phosphorylation

KW - Probability

U2 - 10.1016/j.bbapap.2011.12.001

DO - 10.1016/j.bbapap.2011.12.001

M3 - Journal article

C2 - 22178296

VL - 1824

SP - 405

EP - 412

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 3

ER -