Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for D3TLL6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-D3TLL6-F1 | Predicted | AlphaFoldDB |
No variants for D3TLL6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for D3TLL6 | |||||
No associated diseases with D3TLL6
13 regional properties for D3TLL6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 97 - 180 | IPR001680-1 |
| repeat | WD40 repeat | 182 - 326 | IPR001680-2 |
| repeat | WD40 repeat | 328 - 411 | IPR001680-3 |
| domain | LIS1 homology motif | 9 - 41 | IPR006594 |
| conserved_site | WD40 repeat, conserved site | 123 - 137 | IPR019775-1 |
| conserved_site | WD40 repeat, conserved site | 165 - 179 | IPR019775-2 |
| conserved_site | WD40 repeat, conserved site | 208 - 222 | IPR019775-3 |
| conserved_site | WD40 repeat, conserved site | 312 - 326 | IPR019775-4 |
| conserved_site | WD40 repeat, conserved site | 354 - 368 | IPR019775-5 |
| conserved_site | WD40 repeat, conserved site | 396 - 410 | IPR019775-6 |
| repeat | G-protein beta WD-40 repeat | 123 - 137 | IPR020472-1 |
| repeat | G-protein beta WD-40 repeat | 312 - 326 | IPR020472-2 |
| repeat | G-protein beta WD-40 repeat | 354 - 368 | IPR020472-3 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| microtubule associated complex | Any multimeric complex connected to a microtubule. |
| microtubule organizing center | An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| dynein complex binding | Binding to a dynein complex, a protein complex that contains two or three dynein heavy chains and several light chains, and has microtubule motor activity. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cell division | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. |
| establishment of mitotic spindle orientation | A cell cycle process that sets the alignment of mitotic spindle relative to other cellular structures. |
| microtubule sliding | The movement of one microtubule along another microtubule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKMVLSQRQR | EELNQAIADY | LGSNGYSSAL | EAFRKEADIS | GEAERKIVGL | LEKKWTSVIR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LQKKVMELEA | KLSEAEKEVI | EGAPSRAKRS | PGEWIPRPPE | KFSLSGHRAS | ITRVIFHPTY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLMLSASEDA | VIKIWDFETG | EYERSLKGHT | SSVQDIAFDS | QGKLLASCSA | DLSIKLWDFQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QSYDCVKTML | GHDHNVSSVA | FVPAGDYVLS | ASRDQTIKMW | EVATGYCVKT | YSGHREWIRM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VRVHMDGNIF | ASCSIDHSIR | IWSINSRDCK | AELRAHDHTV | ECIAWAPDIS | TTHINEAAGS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DNKKGHHQGP | FLASGSRDKT | IRVWDVGVGL | CLFVLTGHDN | WVRELTFHPG | GKYLVSASDD |
| 370 | 380 | 390 | 400 | 410 | |
| KTIRVWDLRN | KRFMKTLYAH | QHFCTSVDFH | KKLPYVISGS | VDNTVKVWEC | R |