BPTF

Chr 17q24.2

bromodomain PHD finger transcription factor

Aliases:: FAC1, NURF301
MANE:: ENST00000306378.11

OMIM: 601819 ↗NCBI: 2186 ↗Ensembl ↗

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Predicted protein structure

AlphaFold predicted structure

BPTF · Q12830

Mean pLDDT

Not published

AlphaFold has not published a prediction for this sequence. This is common for very long proteins.

Confidence breakdown

Check AlphaFold DB

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

DDG2P
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Intellectual disability
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Severe microcephaly
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Fetal anomalies
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted

Disease associations (Open Targets)

neurodevelopmental disorder with dysmorphic facies and distal limb anomalies
0.78
Intellectual disability
0.54
hereditary disease
0.54
neurodegenerative disease
0.54
Global developmental delay
0.51
Expressive language delay
0.51
Secondary microcephaly
0.51
syndromic intellectual disability
0.41
type 2 diabetes mellitus
0.39
diabetes mellitus
0.34

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Nucleosome-remodeling factor subunit BPTF

Regulatory subunit of the ATP-dependent NURF-1 and NURF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:14609955, PubMed:28801535). The NURF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the NURF-5 ISWI chromatin remodeling complex (PubMed:28801535). Within the NURF-1 ISWI chromatin-remodeling complex, binds to the promoters of En1 and En2 to positively regulate their expression and promote brain development (PubMed:14609955). Histone-binding protein which binds to H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of active genes (PubMed:16728976, PubMed:16728978). Binds to histone H3 tails dimethylated on 'Lys-4' (H3K4Me2) to a lesser extent (PubMed:16728976, PubMed:16728978, PubMed:18042461). May also regulate transcription through direct binding to DNA or transcription factors (PubMed:10575013)