TBCD — Tubulin folding cofactor D
TBCD belongs to a gene co-expression module in 3 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.
TBCD's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD8⁺ T cells | Cytotoxic Gut Effector cytotoxicity | ATP8B4, CCND2, CD63, CEBPB, CSF1, CTSA, GNLY, GNPTAB +3 more | View in SCUBA |
| Endothelial | Coagulation Protease Signaling Inflammation | CFDP1, F2RL3, FRMD8, HTRA1, ITIH5, ME3, PASK, PRSS23 +1 more | View in SCUBA |
| Pericytes | Cytoskeletal Remodeling Cytoskeletal | ARHGAP18, F2RL3, FSCN1, IVNS1ABP, JUP, PASK, SEMA3F, VWA1 | View in SCUBA |
About the gene
| Chromosome | 17: 82752042-82945914 |
|---|---|
| Predicted location | Intracellular, Membrane |
| Essential gene | Yes |
| Protein class | Disease related genes, Essential proteins, Human disease related genes, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Chaperone, GTPase activation |
Function
Tubulin-folding protein implicated in the first step of the tubulin folding pathway and required for tubulin complex assembly. Involved in the regulation of microtubule polymerization or depolymerization, it modulates microtubule dynamics by capturing GTP- bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Acts as a GTPase-activating protein (GAP) for ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. Required for correct assembly and maintenance of the mitotic spindle, and proper progression of mitosis. Involved in neuron morphogenesis.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.