Prediction of human protein function from post-translational modifications and localization features
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Prediction of human protein function from post-translational modifications and localization features. / Jensen, L J; Gupta, Ramneek; Blom, Nikolaj; Devos, D; Tamames, J; Kesmir, Can; Nielsen, H; Staerfeldt, H H; Rapacki, Kristoffer; Workman, Christopher; Andersen, C A F; Knudsen, S; Krogh, A; Valencia, A; Brunak, S.
In: Journal of Molecular Biology, Vol. 319, No. 5, 2002, p. 1257-65.Research output: Contribution to journal › Journal article › peer-review
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TY - JOUR
T1 - Prediction of human protein function from post-translational modifications and localization features
AU - Jensen, L J
AU - Gupta, Ramneek
AU - Blom, Nikolaj
AU - Devos, D
AU - Tamames, J
AU - Kesmir, Can
AU - Nielsen, H
AU - Staerfeldt, H H
AU - Rapacki, Kristoffer
AU - Workman, Christopher
AU - Andersen, C A F
AU - Knudsen, S
AU - Krogh, A
AU - Valencia, A
AU - Brunak, S
N1 - (c) 2002 Elsevier Science Ltd.
PY - 2002
Y1 - 2002
N2 - We have developed an entirely sequence-based method that identifies and integrates relevant features that can be used to assign proteins of unknown function to functional classes, and enzyme categories for enzymes. We show that strategies for the elucidation of protein function may benefit from a number of functional attributes that are more directly related to the linear sequence of amino acids, and hence easier to predict, than protein structure. These attributes include features associated with post-translational modifications and protein sorting, but also much simpler aspects such as the length, isoelectric point and composition of the polypeptide chain.
AB - We have developed an entirely sequence-based method that identifies and integrates relevant features that can be used to assign proteins of unknown function to functional classes, and enzyme categories for enzymes. We show that strategies for the elucidation of protein function may benefit from a number of functional attributes that are more directly related to the linear sequence of amino acids, and hence easier to predict, than protein structure. These attributes include features associated with post-translational modifications and protein sorting, but also much simpler aspects such as the length, isoelectric point and composition of the polypeptide chain.
U2 - 10.1016/S0022-2836(02)00379-0
DO - 10.1016/S0022-2836(02)00379-0
M3 - Journal article
C2 - 12079362
VL - 319
SP - 1257
EP - 1265
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 5
ER -
ID: 40749858