Q7Z3B3: KAT8 regulatory NSL complex subunit 1 (KANSL1)

KAT8 regulatory NSL complex subunit 1 (KANSL1) is a 1105-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7Z3B3.

Gene
KANSL1
Organism
Homo sapiens
Length
1105 residues
Mean pLDDT
50.3
Model
AF-Q7Z3B3-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 50.3 (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 accurate5%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions65%

What pLDDT means and how to read it

Function

Non-catalytic component of the NSL histone acetyltransferase complex, a multiprotein complex that mediates histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) at transcription start sites and promotes transcription initiation (PubMed:20018852, PubMed:22547026, PubMed:33657400). The NSL complex also acts as a regulator of gene expression in mitochondria (PubMed:27768893). In addition to its role in transcription, KANSL1 also plays an essential role in spindle assembly during mitosis (PubMed:26243146). Associates with microtubule ends and contributes to microtubule stability (PubMed:26243146)

Subunit structure

Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts (via PEHE domain) with KAT8 (via HAT domain); the interaction is direct (PubMed:16227571, PubMed:16543150, PubMed:20018852, PubMed:20620954, PubMed:21217699, PubMed:22547026, PubMed:27768893, PubMed:33657400). Component of some MLL1/MLL complex, at least composed…

Subcellular location

Nucleus, Chromosome, centromere, kinetochore, Mitochondrion, Cytoplasm, cytoskeleton, spindle pole

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CY1X-ray1.5 ÅC/D=585-598
4CY2X-ray2.0 ÅD=585-598

More AlphaFold highlights

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