SCUBA

RNF111 — Ring finger protein 111

RNF111 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

RNF111's module in each cell type

Cell typeModuleShares the module with
MacrophagesRho GTPase Signaling
Cytoskeletal
ABCC1, ABR, ANKRD17, ARFGEF2, ARHGAP10, ARID2, ATAD2B, ATP9B +44 moreView in SCUBA

About the gene

SynonymsARK, Arkadia, DKFZP761D081, FLJ38008
Chromosome15: 58865175-59097419
Predicted locationIntracellular
Essential geneNo
Protein classEnzymes, Predicted intracellular proteins
Molecular functionDevelopmental protein, Transferase
Biological processDNA damage, DNA repair, Ubl conjugation pathway

Function

E3 ubiquitin-protein ligase. Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP. Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP. In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL. Associates with UBE2D2 as an E2 enzyme. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates. Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair. Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.