Description: Homo sapiens ring finger protein 11 (RNF11), mRNA. RefSeq Summary (NM_014372): The protein encoded by this gene contains a RING-H2 finger motif, which is known to be important for protein-protein interactions. The expression of this gene has been shown to be induced by mutant RET proteins (MEN2A/MEN2B). The germline mutations in RET gene are known to be responsible for the development of multiple endocrine neoplasia (MEN). [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr1:51,701,945-51,739,119 Size: 37,175 Total Exon Count: 3 Strand: + Coding Region Position: hg19 chr1:51,702,429-51,736,994 Size: 34,566 Coding Exon Count: 3
ID:RNF11_HUMAN DESCRIPTION: RecName: Full=RING finger protein 11; FUNCTION: Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity). Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with GGA1. INTERACTION: Q9UJY5:GGA1; NbExp=2; IntAct=EBI-396669, EBI-447141; Q96J02:ITCH; NbExp=2; IntAct=EBI-396669, EBI-1564678; Q9HAU4:SMURF2; NbExp=3; IntAct=EBI-396669, EBI-396727; O95630:STAMBP; NbExp=2; IntAct=EBI-396669, EBI-396676; P0CG47:UBB; NbExp=2; IntAct=EBI-396669, EBI-413034; P51668:UBE2D1; NbExp=4; IntAct=EBI-396669, EBI-743540; P62837:UBE2D2; NbExp=4; IntAct=EBI-396669, EBI-347677; P61077:UBE2D3; NbExp=3; IntAct=EBI-396669, EBI-348268; P51965:UBE2E1; NbExp=2; IntAct=EBI-396669, EBI-348546; P61088:UBE2N; NbExp=3; IntAct=EBI-396669, EBI-1052908; SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1 (PubMed:16123141). TISSUE SPECIFICITY: Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines. DOMAIN: The WW-binding motif mediates interaction with NEDD4 (By similarity). PTM: Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1. PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome. PTM: May be acylated at Cys-4, possibly palmitoylated. Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes. SIMILARITY: Contains 1 RING-type zinc finger.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9Y3C5
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.