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Figure: Ufmylation pathway (Human).

id: gomodel:65f3ae5c00000111

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This figure illustrates the human Ufmylation pathway, a post-translational modification process where the ubiquitin-fold modifier 1 (UFM1) is conjugated to target proteins. The pathway consists of four main steps:

  1. Maturation: UFSP1 (cysteine-type peptidase) processes the inactive UFM1 precursor by cleaving its C-terminus to expose a glycine residue required for conjugation.

  2. Activation: UBA5 (UFM1 activating enzyme) activates UFM1 in an ATP-dependent manner by forming a high-energy thioester bond.

  3. Conjugation: UFC1 (UFM1 conjugating enzyme) receives the activated UFM1 from UBA5, forming another thioester intermediate.

  4. Ligation: UFL1 (UFM1 ligase) transfers UFM1 from UFC1 to the lysine residue of target substrate proteins, resulting in ufmylated proteins.

This process occurs in the cytosol and is critical for various cellular functions including endoplasmic reticulum homeostasis, cell cycle regulation, and cellular stress responses. Dysregulation of the ufmylation pathway has been implicated in various diseases, including certain neurodevelopmental disorders and cancers.

Feedback from AI on figure:

{"feedback":"This diagram effectively illustrates the Ufmylation pathway with clear representation of each protein's function in the process. The color-coding system helps distinguish between different components, and the sequential arrangement makes the pathway easy to follow. The added explanatory text for each step provides valuable context about the biochemical significance of each interaction. The diagram successfully balances scientific accuracy with visual clarity, making it appropriate for publication in high-impact journals like Cell or Nature.","necessary_changes":null,"optional_changes":null}