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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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From DNA to Protein03:06

From DNA to Protein

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The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
21.9K
Leaky Scanning02:28

Leaky Scanning

5.6K
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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tRNA Activation02:26

tRNA Activation

22.5K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Related Experiment Video

Updated: Jan 10, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Decoding protein N-phosphorylation functionality and sequence patterns.

Ming-Xiao Zhao1,2, Hua-Huan Cai1,2, Qiang Chen3

  • 1Institute of Drug Discovery Technology, Ningbo University, 818 Fenghua Road, Jiangbei District, Ningbo 315211, China.

Briefings in Bioinformatics
|November 26, 2025
PubMed
Summary

Protein N-phosphorylation is crucial in biological processes and linked to diseases like cancer. Its functional, sequential, and structural features offer new research avenues, especially by comparing it to O-phosphorylation.

Keywords:
Nphosfunctionmotifprotein N-phosphorylation

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Related Experiment Videos

Last Updated: Jan 10, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Systems Biology

Background:

  • Protein N-phosphorylation is a key post-translational modification in prokaryotes and eukaryotes.
  • Existing knowledge gaps hinder understanding of its functional roles, sequence motifs, and structural properties.

Purpose of the Study:

  • To comprehensively analyze N-phosphorylation using integrated functional, sequential, and structural approaches.
  • To elucidate the biological significance and disease associations of N-phosphorylation.
  • To explore novel research perspectives by comparing N- and O-phosphorylation.

Main Methods:

  • Integrated analysis of large-scale, experimentally verified N-phosphorylation datasets.
  • Functional, sequential, and structural analyses of phosphorylation sites.
  • Comparative motif analysis between N- and O-phosphorylation.
  • Structural-sequence pattern analysis focusing on relative solvent accessibility.

Main Results:

  • N-phosphorylation broadly participates in diverse biological processes.
  • Strong associations found between N-phosphorylation and human diseases, particularly cancer.
  • High motif conservation observed between eukaryotic N- and O-phosphorylation.
  • Relative solvent accessibility is a distinctive descriptor for phosphorylation sites.

Conclusions:

  • N-phosphorylation plays a significant role in biological functions and disease pathogenesis.
  • Conserved motifs between N- and O-phosphorylation provide new research directions.
  • Structural features, like solvent accessibility, are critical for characterizing phosphorylation sites.
  • Findings support N-phosphorylation's potential in biological sciences, analytical chemistry, and medical research.