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Updated: Jun 26, 2026
Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Comparative kinomics of human and chimpanzee reveal unique kinship and functional diversity generated by new domain
Krishanpal Anamika1, Juliette Martin, Narayanaswamy Srinivasan
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India. anamika@mbu.iisc.ernet.in
Background:
Phosphorylation by protein kinases is a common event in many cellular processes. Further, many kinases perform specialized roles and are regulated by non-kinase domains tethered to kinase domain. Perturbation in the regulation of kinases leads to malignancy. We have identified and analysed putative protein kinases encoded in the genome of chimpanzee which is a close evolutionary relative of human.
Result:
The shared core biology between chimpanzee and human is characterized by many orthologous protein kinases which are involved in conserved pathways. Domain architectures specific to chimp/human kinases have been observed. Chimp kinases with unique domain architectures are characterized by deletion of one or more non-kinase domains in the human kinases. Interestingly, counterparts of some of the multi-domain human kinases in chimp are characterized by identical domain architectures but with kinase-like non-kinase domain. Remarkably, out of 587 chimpanzee kinases no human orthologue with greater than 95% sequence identity could be identified for 160 kinases. Variations in chimpanzee kinases compared to human kinases are brought about also by differences in functions of domains tethered to the catalytic kinase domain. For example, the heterodimer forming PB1 domain related to the fold of ubiquitin/Ras-binding domain is seen uniquely tethered to PKC-like chimpanzee kinase.
Conclusion:
Though the chimpanzee and human are evolutionary very close, there are chimpanzee kinases with no close counterpart in the human suggesting differences in their functions. This analysis provides a direction for experimental analysis of human and chimpanzee protein kinases in order to enhance our understanding on their specific biological roles.
Insights
Chimpanzee and human share many protein kinases, but some chimpanzee kinases lack human counterparts, indicating functional differences. This comparative genomics study highlights unique kinase domain architectures and functions in chimpanzees, guiding future research.
Area of Science:
- Comparative genomics
- Molecular biology
- Evolutionary biology
Background:
- Protein kinases regulate crucial cellular processes through phosphorylation.
- Dysregulation of kinase activity is linked to cancer development.
- Kinase function is often modulated by associated non-kinase domains.
Purpose of the Study:
- To identify and analyze protein kinases in the chimpanzee genome.
- To compare chimpanzee kinases with their human orthologs.
- To understand evolutionary differences in kinase regulation and function.
Main Methods:
- Genome-wide identification of protein kinases in chimpanzees.
- Comparative analysis of kinase domain architectures between human and chimpanzee.
- Sequence identity comparison to identify orthologous kinases.
Main Results:
- Identified numerous orthologous protein kinases involved in conserved pathways between humans and chimpanzees.
- Observed unique domain architectures in chimpanzee kinases, including deletions of non-kinase domains.
- Found 160 chimpanzee kinases with no human orthologs above 95% sequence identity.
- Noted variations in tethered domain functions, such as the PB1 domain in chimpanzee PKC-like kinases.
Conclusions:
- Significant differences exist in protein kinase repertoires between humans and chimpanzees despite close evolutionary relationship.
- Unique chimpanzee kinases suggest distinct biological roles and regulatory mechanisms.
- This study provides a foundation for experimental investigation into human and chimpanzee kinase functions.
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