FAM111A

Chr 11q12.1

FAM111 trypsin like peptidase A

Aliases:: FLJ22794, KIAA1895
MANE:: ENST00000675163.1

OMIM: 615292 ↗NCBI: 63901 ↗Ensembl ↗

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Predicted protein structure

AlphaFold predicted structure

FAM111A · Q96PZ2

v62025-08-01

Predicted Aligned Error matrix for FAM111A — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

76.7/ 100

Confident

611 residues

Confidence breakdown

Very high(≥ 90)39%
Confident(70–90)34%
Low(50–70)9%
Very low(< 50)19%

Open interactive 3D viewer

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
Fetal anomalies
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Skeletal dysplasia
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Clefting
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Intellectual disability
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Structural eye disease
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted

Disease associations (Open Targets)

osteocraniostenosis
0.73
autosomal dominant Kenny-Caffey syndrome
0.68
Kenny-Caffey syndrome
0.60
prostate carcinoma
0.44
prostate cancer
0.40
neurodegenerative disease
0.38
FAM111A-related skeletal dysplasia
0.37
hereditary disease
0.34
hypertrophic cardiomyopathy
0.32
hypoparathyroidism
0.12

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

Protein function (UniProt)

Serine protease FAM111A

Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:32165630). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (PubMed:32165630). Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors (PubMed:32165630). Required for PCNA loading on replication sites (PubMed:24561620). Promotes S-phase entry and DNA synthesis (PubMed:24561620). Also acts as a restriction factor for some viruses including SV40 polyomavirus and vaccinia virus (PubMed:23093934, PubMed:37607234). Mechanistically, affects nuclear barrier function during viral replication by mediating the disruption of the nuclear pore complex (NPC) via its protease activity (PubMed:33369867, PubMed:37607234). In turn, interacts with vaccinia virus DNA-binding protein OPG079 in the cytoplasm and promotes its degradation without the need of its protease activity but through autophagy (PubMed:37607234)