Bioinformatic prediction and analysis of eukaryotic protein kinases in the rat genome.
Kazi, Julhash U. LU
; Kabir, Nuzhat N.
and Soh, Jae Won
(2008)
In Gene
410(1)(Feb,29).
p.147-153
- Abstract
- Eukaryotic protein kinases, containing a conserved catalytic domain, represent one of the largest superfamilies of the eukaryotic proteins and play distinct roles in cell signaling and diseases. Near completion of rat genome sequencing project enables the evaluation of a near complete set of rat protein kinases. Publicly accessible genetic sequence databases were searched for rat protein kinases, and 515 eukaryotic protein kinases, 40 atypical protein kinases and 45 kinase pseudogenes were identified. The rat has 509 putative protein kinases orthologous to human kinases. Unlike microtubule affinity-regulating kinases, the rat has a few more kinases, in addition to the orthologous pairs of mouse kinases. The comparison of 11 different... (More)
- Eukaryotic protein kinases, containing a conserved catalytic domain, represent one of the largest superfamilies of the eukaryotic proteins and play distinct roles in cell signaling and diseases. Near completion of rat genome sequencing project enables the evaluation of a near complete set of rat protein kinases. Publicly accessible genetic sequence databases were searched for rat protein kinases, and 515 eukaryotic protein kinases, 40 atypical protein kinases and 45 kinase pseudogenes were identified. The rat has 509 putative protein kinases orthologous to human kinases. Unlike microtubule affinity-regulating kinases, the rat has a few more kinases, in addition to the orthologous pairs of mouse kinases. The comparison of 11 different eukaryotic species revealed the evolutionary conservation of this diverse family of proteins. The evolutionary rate studies of human disease and non-disease associated kinases suggested that relatively uniform selective pressures have been applied to these kinase classes. This bioinformatic study of the rat protein kinases provides a suitable framework for further characterization of the functional and structural properties of these protein kinases (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3915643
- author
- Kazi, Julhash U.
LU
; Kabir, Nuzhat N.
and Soh, Jae Won
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Gene
- volume
- 410(1)
- issue
- Feb,29
- pages
- 147 - 153
- publisher
- Elsevier
- external identifiers
-
- scopus:40649110027
- ISSN
- 1879-0038
- DOI
- 10.1016/j.gene.2007.12.003
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- 5e1614ed-735f-4712-89cd-ac771ca3f7ab (old id 3915643)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/18201844?dopt=AbstractPlus
- date added to LUP
- 2016-04-04 12:13:47
- date last changed
- 2022-01-29 23:08:47
@article{5e1614ed-735f-4712-89cd-ac771ca3f7ab,
abstract = {{Eukaryotic protein kinases, containing a conserved catalytic domain, represent one of the largest superfamilies of the eukaryotic proteins and play distinct roles in cell signaling and diseases. Near completion of rat genome sequencing project enables the evaluation of a near complete set of rat protein kinases. Publicly accessible genetic sequence databases were searched for rat protein kinases, and 515 eukaryotic protein kinases, 40 atypical protein kinases and 45 kinase pseudogenes were identified. The rat has 509 putative protein kinases orthologous to human kinases. Unlike microtubule affinity-regulating kinases, the rat has a few more kinases, in addition to the orthologous pairs of mouse kinases. The comparison of 11 different eukaryotic species revealed the evolutionary conservation of this diverse family of proteins. The evolutionary rate studies of human disease and non-disease associated kinases suggested that relatively uniform selective pressures have been applied to these kinase classes. This bioinformatic study of the rat protein kinases provides a suitable framework for further characterization of the functional and structural properties of these protein kinases}},
author = {{Kazi, Julhash U. and Kabir, Nuzhat N. and Soh, Jae Won}},
issn = {{1879-0038}},
language = {{eng}},
number = {{Feb,29}},
pages = {{147--153}},
publisher = {{Elsevier}},
series = {{Gene}},
title = {{Bioinformatic prediction and analysis of eukaryotic protein kinases in the rat genome.}},
url = {{https://lup.lub.lu.se/search/files/5957727/4250522.pdf}},
doi = {{10.1016/j.gene.2007.12.003}},
volume = {{410(1)}},
year = {{2008}},
}