全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

HomoKinase: A Curated Database of Human Protein Kinases

DOI: 10.1155/2013/417634

Full-Text   Cite this paper   Add to My Lib

Abstract:

HomoKinase database is a comprehensive collection of curated human protein kinases and their relevant biological information. The entries in the database are curated by three criteria: HGNC approval, gene ontology-based biological process (protein phosphorylation), and molecular function (ATP binding and kinase activity). For a given query protein kinase name, the database provides its official symbol, full name, other known aliases, amino acid sequences, functional domain, gene ontology, pathways assignments, and drug compounds. In addition, as a search tool, it enables the retrieval of similar protein kinases with specific family, subfamily, group, and domain combinations and tabulates the information. The present version contains 498 curated human protein kinases and links to other popular databases. 1. Introduction In human genome, the protein kinase is one of the largest recognized protein families which regulate multiple biological processes by posttranslational phosphorylation of serine, threonine, and tyrosine residues [1]. Human genome contains 500 protein kinase genes that constitute about 2% of all genes [2]. Approximately 2000 protein kinases are encoded by human genome. Protein kinases and phosphatases play an important role in regulating and coordinating aspects of metabolism, cell growth, cell motility, cell differentiation and cell division, and signaling pathways involved in normal development and disease [3]. In human genome, 30% to 50% of proteins may undergo phosphorylation; therefore, improper functioning of kinase may lead to various human diseases [4]. Turning on and off of protein kinases and phosphatases maintains the functions of the cellular life in a systematic manner. Further, protein kinases are involved in regulation of many processes, so they are linked to many diseases and act as target for drug design. Protein kinases are the group of enzymes that share conserved catalytic domains involved in stimulating catalytic activity of enzymes and act as ATP binding sites. This result the need and availability of databases specific to protein kinases. There are many databases for protein kinases present, which include human protein kinases information as well [2, 5, 6]. For example, KinBase [2] contains manually curated kinomes based on Hanks and Hunter classification for nine genomes including humans. KinG [5] contains protein kinases entries for 40 genomes that have been classified by kinome-based sequence search methods. KinWeb [6] is a specific collection of protein kinases encoded in the human genome, and the classification

References

[1]  G. Manning, G. D. Plowman, T. Hunter, and S. Sudarsanam, “Evolution of protein kinase signaling from yeast to man,” Trends in Biochemical Sciences, vol. 27, no. 10, pp. 514–520, 2002.
[2]  G. Manning, D. B. Whyte, R. Martinez, T. Hunter, and S. Sudarsanam, “The protein kinase complement of the human genome,” Science, vol. 298, no. 5600, pp. 1912–1934, 2002.
[3]  L. N. Johnson, M. E. M. Noble, and D. J. Owen, “Active and inactive protein kinases: structural basis for regulation,” Cell, vol. 85, no. 2, pp. 149–158, 1996.
[4]  C. Y. Yang, C. H. Chang, Y. L. Yu, et al., “PhosphoPOINT: a comprehensive human kinase interactome and phospho-protein database,” Bioinformatics, vol. 24, no. 16, pp. i14–i20, 2008.
[5]  A. Krupa, K. R. Abhinandan, and N. Srinivasan, “KinG: a database of protein kinases in genomes,” Nucleic Acids Research, vol. 32, pp. D513–D515, 2004.
[6]  L. Milanesi, M. Petrillo, L. Sepe et al., “Systematic analysis of human kinase genes: a large number of genes and alternative splicing events result in functional and structural diversity,” BMC Bioinformatics, vol. 6, no. 4, article S20, 2005.
[7]  R. L. Seal, S. M. Gordon, M. J. Lush, M. W. Wright, and E. A. Bruford, “Genenames.org: the HGNC resources in 2011,” Nucleic Acids Research, vol. 39, no. 1, pp. D514–D519, 2011.
[8]  D. Binns, E. Dimmer, R. Huntley, D. Barrell, C. O'Donovan, and R. Apweiler, “QuickGO: a web-based tool for Gene Ontology searching,” Bioinformatics, vol. 25, no. 22, pp. 3045–3046, 2009.
[9]  M. Ashburner, C. A. Ball, J. A. Blake, et al., “Gene ontology: tool for the unification of biology. The Gene Ontology Consortium,” Nature Genetics, vol. 25, no. 1, pp. 25–29, 2000.
[10]  S. S. Taylor, E. Radzio-Andzelm, Madhusudan, X. Cheng, L. Ten Eyck, and N. Narayana, “Catalytic subunit of cyclic AMP-dependent protein kinasestructure and dynamics of the active site cleft,” Pharmacology and Therapeutics, vol. 82, no. 2-3, pp. 133–141, 1999.
[11]  QuickGO, 2013, http://www.ebi.ac.uk/QuickGO.
[12]  AmiGO, 2013, http://amigo.geneontology.org.
[13]  PhophoSitePlus, 2013, http://www.phosphosite.org .
[14]  UniProt, 2013, http://www.uniprot.org.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133