FEM1C

Chr 5q22.3

fem-1 homolog C

Aliases:: KIAA1785, EUROIMAGE686608, EUROIMAGE783647, FEM1A
MANE:: ENST00000274457.5

OMIM: 608767 ↗NCBI: 56929 ↗Ensembl ↗

Annotations refreshed 9 hours ago.

Predicted protein structure

AlphaFold predicted structure

FEM1C · Q96JP0

v62025-08-01

Predicted Aligned Error matrix for FEM1C — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

94.1/ 100

Very high

617 residues

Confidence breakdown

Very high(≥ 90)88%
Confident(70–90)10%
Low(50–70)2%
Very low(< 50)0%

Open interactive 3D viewer

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

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

Ataxia and cerebellar anomalies - narrow panel
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Intellectual disability
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
DDG2P
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown

Disease associations (Open Targets)

Ataxia
0.37
cerebellar ataxia
0.37
neurodevelopmental disorder
0.30
neurodegenerative disease
0.23
Intellectual disability
0.18
colorectal carcinoma
0.07
atrial fibrillation
0.03
alcohol drinking
0.03
hypertensive disorder
0.03
Premature ovarian insufficiency
0.02

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

Protein function (UniProt)

Protein fem-1 homolog C

Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29775578, PubMed:29779948, PubMed:33398168, PubMed:33398170, PubMed:38326650). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29775578, PubMed:29779948, PubMed:33398168, PubMed:33398170). The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation (PubMed:33398168, PubMed:33398170, PubMed:38326650). The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding (PubMed:26138980). Promotes ubiquitination and degradation of SLBP (PubMed:28118078)