Ser83

Ser83 denotes a serine residue at position 83 in a protein sequence. The numbering is specific to each protein, so Ser83 in one protein is not the same as Ser83 in another. The functional significance of Ser83 depends on the local structural environment, nearby residues, and whether the serine participates in catalysis, binding, or regulation.

Role and significance: Serine residues can serve as catalytic components in enzymes, participate in hydrogen bonding networks that stabilize structure, or act as sites for regulatory post-translational modifications. The particular role of Ser83 varies by protein context; in some proteins it may contribute to active-site geometry, while in others it may be solvent-exposed and functionally inert unless modified.

Post-translational modifications: Ser83 can be a target for phosphorylation by serine/threonine kinases, which can modulate activity, interactions, or localization. Serine residues can also undergo other modifications in certain contexts, though phosphorylation is one of the most common regulatory events for serine residues.

Conservation and study: If Ser83 is conserved across homologous proteins, it often indicates functional importance. Researchers investigate Ser83 through approaches such as site-directed mutagenesis (for example, replacing serine with alanine or aspartate to probe function), mass spectrometry to detect modifications, and structural methods like X-ray crystallography or NMR to reveal the residue’s environment.

Annotation and resources: For a given protein, Ser83-related information appears in databases such as UniProt and PDB, which describe its location, modification state, and potential functional notes. Because residue numbering is protein-specific, precise implications require the relevant protein context.