O14964: Hepatocyte growth factor-regulated tyrosine kinase substrate (HGS)

Hepatocyte growth factor-regulated tyrosine kinase substrate (HGS) is a 777-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14964.

Gene
HGS
Organism
Homo sapiens
Length
777 residues
Mean pLDDT
66.1
Model
AF-O14964-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 66.1 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate32%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions42%

What pLDDT means and how to read it

Function

Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as a sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential…

Subunit structure

Component of the ESCRT-0 complex composed of STAM or STAM2 and HGS. Part of a complex at least composed of HSG, STAM2 (or probably STAM) and EPS15 (PubMed:12551915). Interacts with STAM (PubMed:9407053). Interacts with STAM2 (By similarity). Interacts with EPS15; the interaction is direct, calcium-dependent and inhibited by SNAP25 (By similarity). Identified in a complex with STAM and LITAF…

Subcellular location

Cytoplasm, Early endosome membrane, Endosome, multivesicular body membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3OBQX-ray1.4 ÅB=346-354
3ZYQX-ray1.48 ÅA=1-225
4AVXX-ray1.68 ÅA=1-225
2D3GX-ray1.7 ÅP=257-277
3F1IX-ray2.3 ÅH=404-501

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