ID:KCTD5_HUMAN DESCRIPTION: RecName: Full=BTB/POZ domain-containing protein KCTD5; FUNCTION: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4. SUBUNIT: Homopentamer. Interacts (via C-terminus) with GRASP55/GORASP2. Interacts with CUL3 and with ubiquitinated proteins. Interacts with adeno-associated virus 2 (AAV-2) REP proteins. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins. INDUCTION: Up-regulated in peripheral blood lymphocytes stimulated through the T-cell receptor. DOMAIN: The BTB (POZ) domain is atypical and mediates the formation of a homopentamer instead of a homotetramer. Homopentamerization is due to the presence of 4 residues in the BTB (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118. SIMILARITY: Contains 1 BTB (POZ) domain.
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 Q9NXV2
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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.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0005515 protein binding GO:0042802 identical protein binding GO:0044877 macromolecular complex binding GO:0097602 cullin family protein binding
Biological Process: GO:0016032 viral process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process GO:0051260 protein homooligomerization