Evidence map›Paper›PMID 12537555›Full record

ArticleGenome biology2002

The repertoire of protein kinases encoded in the draft version of the human genome: atypical variations and uncommon domain combinations.

A Krupa, N Srinivasan

Open access · goldAbstract readComparative Study
In one paragraph

Article in Genome biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Arterial Thrombotic Complications of Tyrosine Kinase Inhibitors.Arteriosclerosis, thrombosis, and vascular biology · 2021
    Review
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  13. Classification of nonenzymatic homologues of protein kinases.Comparative and functional genomics · 2009
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

A KrupaMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
N Srinivasan
Indian Institute of Science Bangalore · IN

Funding

Wellcome Trust
6 · The paper itself

Abstract

backgroundPhosphorylation by protein kinases is central to cellular signal transduction. Abnormal functioning of kinases has been implicated in developmental disorders and malignancies. Their activity is regulated by second messengers and by the binding of associated domains, which are also influential in translocating the catalytic component to their substrate sites, in mediating interaction with other proteins and carrying out their biological roles.

resultUsing sensitive profile-search methods and manual analysis, the human genome has been surveyed for protein kinases. A set of 448 sequences, which show significant similarity to protein kinases and contain the critical residues essential for kinase function, have been selected for an analysis of domain combinations after classifying the kinase domains into subfamilies. The unusual domain combinations in particular kinases suggest their involvement in ubiquitination pathways and alternative modes of regulation for mitogen-activated protein kinase kinases (MAPKKs) and cyclin-dependent kinase (CDK)-like kinases. Previously unexplored kinases have been implicated in osteoblast differentiation and embryonic development on the basis of homology with kinases of known functions from other organisms. Kinases potentially unique to vertebrates are involved in highly evolved processes such as apoptosis, protein translation and tyrosine kinase signaling. In addition to coevolution with the kinase domain, duplication and recruitment of non-catalytic domains is apparent in signaling domains such as the PH, DAG-PE, SH2 and SH3 domains.

conclusionsExpansion of the functional repertoire and possible existence of alternative modes of regulation of certain kinases is suggested by their uncommon domain combinations. Experimental verification of the predicted implications of these kinases could enhance our understanding of their biological roles.

Indexed as

Genetic VariationGenome, HumanAmino Acid MotifsAnimalsBacterial ProteinsCaenorhabditis elegansCatalytic DomainDatabases, GeneticDrosophila melanogasterGenomeHumansMiceProtein KinasesProtein Structure, TertiarySequence Homology, Nucleic Acidsrc Homology DomainsBacterial ProteinsProtein Kinases

Identifiers

PMID12537555
PMCPMC151168
OpenAlexW2155646400

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.