Target Name: RNF111
NCBI ID: G54778
Other Name(s): ARK | E3 ubiquitin-protein ligase Arkadia (isoform 4) | RNF111 variant 3 | Ring finger protein 111, transcript variant 4 | RNF111 variant 4 | Ring finger protein 111, transcript variant 3 | RNF111 variant 2 | E3 ubiquitin-protein ligase Arkadia (isoform 1) | ring finger protein 111 | E3 ubiquitin-protein ligase Arkadia (isoform 2) | hRNF111 | E3 ubiquitin-protein ligase Arkadia (isoform 3) | RING finger protein 111 | E3 ubiquitin-protein ligase Arkadia | Arkadia | RN111_HUMAN | Ring finger protein 111, transcript variant 2 | Ring finger protein 111, transcript variant 1 | RING-type E3 ubiquitin transferase Arkadia | RNF111 variant 1

RNF111: A Drug Target / Disease Biomarker

RNA-Nucleic Acid (RNA) Fold 111 (RNF111) is a protein that is expressed in various cell types of the human body, including epithelial, muscle, and neural tissues. It is a member of the RNA-Nucleic Acid (RNA-NA) family, which is characterized by the presence of a nucleic acid-binding domain in the protein.

RNF111 is involved in various cellular processes that are essential for cell survival and growth, including cell signaling, cell division, and tissue repair. It plays a critical role in the regulation of cell proliferation, as it has been shown to be involved in the G1/S transition, which is the process by which cells prepare for cell division.

In addition to its role in cell proliferation, RNF111 is also involved in the regulation of cell apoptosis (programmed cell death), which is the process by which cells are killed when they have reached their maximum number of copies and are no longer needed. Apoptosis is a natural and essential process that helps to remove damaged or dysfunctional cells from the body, and it is critical for the development and maintenance of tissues and organs.

Another important function of RNF111 is its role in cell-cell adhesion. Adhesion is the process by which cells stick together to form tissues and organs, and it is critical for the development and maintenance of these structures. RNF111 has been shown to be involved in the regulation of cell-cell adhesion, as it has been shown to play a role in the formation of tight junctions, which are the connections between adjacent cells that help to maintain tissue structure.

In conclusion, RNF111 is a protein that is involved in various cellular processes that are essential for cell survival and growth. It plays a critical role in the regulation of cell proliferation, apoptosis, and cell-cell adhesion, and it is a potential drug target (or biomarker) that could be targeted by researchers to develop new treatments for various diseases.

Protein Name: Ring Finger Protein 111

Functions: E3 ubiquitin-protein ligase (PubMed:26656854). 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 (PubMed:14657019, PubMed:16601693). 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 (PubMed:14657019, PubMed:16601693). 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 (PubMed:17591695). Associates with UBE2D2 as an E2 enzyme (PubMed:22411132). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23751493). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (PubMed:23751493). 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)

More Common Targets

RNF112 | RNF113A | RNF113B | RNF114 | RNF115 | RNF121 | RNF122 | RNF123 | RNF125 | RNF126 | RNF126P1 | RNF128 | RNF13 | RNF130 | RNF133 | RNF135 | RNF138 | RNF138P1 | RNF139 | RNF139-DT | RNF14 | RNF141 | RNF144A | RNF144B | RNF145 | RNF146 | RNF148 | RNF149 | RNF150 | RNF151 | RNF152 | RNF157 | RNF157-AS1 | RNF165 | RNF166 | RNF167 | RNF168 | RNF169 | RNF17 | RNF170 | RNF175 | RNF180 | RNF181 | RNF182 | RNF183 | RNF185 | RNF186 | RNF187 | RNF19A | RNF19B | RNF2 | RNF20 | RNF207 | RNF208 | RNF212 | RNF212B | RNF213 | RNF213-AS1 | RNF214 | RNF215 | RNF216 | RNF216-IT1 | RNF216P1 | RNF217 | RNF217-AS1 | RNF220 | RNF222 | RNF224 | RNF225 | RNF227 | RNF24 | RNF25 | RNF26 | RNF31 | RNF32 | RNF32-DT | RNF34 | RNF38 | RNF39 | RNF4 | RNF40 | RNF41 | RNF43 | RNF44 | RNF5 | RNF5P1 | RNF6 | RNF7 | RNF7P1 | RNF8 | RNFT1 | RNFT2 | RNGTT | RNH1 | RNLS | RNMT | RNPC3 | RNPC3-DT | RNPEP | RNPEPL1