A4Q9F4
Gene name |
Ttll11 |
Protein name |
Tubulin polyglutamylase TTLL11 |
Names |
Tubulin--tyrosine ligase-like protein 11 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:74410 |
EC number |
|
Protein Class |
|
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 A4Q9F4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4Q9F4-F1 | Predicted | AlphaFoldDB |
30 variants for A4Q9F4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1132755138 | 10 | P>L | No | EVA | |
| rs237658517 | 31 | S>L | No | EVA | |
| rs257239227 | 41 | G>C | No | EVA | |
| rs248205336 | 64 | R>G | No | EVA | |
| rs3388551478 | 172 | S>N | No | EVA | |
| rs3413054452 | 180 | N>K | No | EVA | |
| rs247257023 | 265 | G>S | No | EVA | |
| rs3388547430 | 328 | N>D | No | EVA | |
| rs3388547816 | 358 | S>R | No | EVA | |
| rs3388546156 | 365 | F>I | No | EVA | |
| rs27205668 | 371 | R>K | No | EVA | |
| rs3388548301 | 430 | K>* | No | EVA | |
| rs3388550292 | 431 | N>D | No | EVA | |
| rs3388543257 | 492 | F>C | No | EVA | |
| rs3388547877 | 497 | M>K | No | EVA | |
| rs3388543271 | 506 | V>F | No | EVA | |
| rs3388551528 | 523 | V>I | No | EVA | |
| rs222670006 | 542 | P>L | No | EVA | |
| rs3388548989 | 558 | I>T | No | EVA | |
| rs3388547419 | 608 | C>Y | No | EVA | |
| rs3388542324 | 616 | S>P | No | EVA | |
| rs3388551500 | 641 | S>L | No | EVA | |
| rs3388548854 | 657 | Q>L | No | EVA | |
| rs3388550591 | 684 | D>E | No | EVA | |
| rs3388552315 | 685 | E>G | No | EVA | |
| rs225751025 | 691 | H>R | No | EVA | |
| rs259943112 | 694 | R>Q | No | EVA | |
| rs3388547381 | 696 | L>F | No | EVA | |
| rs3388552396 | 707 | E>Q | No | EVA | |
| rs3388543287 | 720 | G>E | No | EVA |
No associated diseases with A4Q9F4
No regional properties for A4Q9F4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A4Q9F4 | |||
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| ciliary basal body | A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport. |
| cilium | A specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface and of some cytoplasmic parts. Each cilium is largely bounded by an extrusion of the cytoplasmic (plasma) membrane, and contains a regular longitudinal array of microtubules, anchored to a basal body. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| tubulin binding | Binding to monomeric or multimeric forms of tubulin, including microtubules. |
| tubulin-glutamic acid ligase activity | Catalysis of the posttranslational transfer of one or more glutamate residues to the gamma-carboxyl group(s) of one or more specific glutamate residues on a tubulin molecule. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| microtubule cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins. |
| microtubule severing | The process in which a microtubule is broken down into smaller segments. Severing enzymes remove dimers from the middle of the filament to create new ends, unlike depolymerizing kinesins that use ATP to uncap microtubules at their ends. |
| protein polyglutamylation | The addition of one or more alpha-linked glutamyl units to the gamma carboxyl group of peptidyl-glutamic acid. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRRSSPEKKP | EAEWEADAAA | AAAATAAATE | SLPAETEKQQ | GVDAGAAGDP | ERLELEEQPK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DVGRIPTPTR | RHAPEEGEAR | VVRRLPPALP | LAQPRPAARA | LSQLVKARGR | SRSRVYRRSA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GSMRPVTVDS | SKARTSLDAL | KISLRQLRWK | EFPFGRRLPC | DIYWHGVSFR | DSDILSGQVN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KFPGMTEMVR | KVTLSRALRI | MQNLFPEEYN | FYPRSWILPE | EFQLFVSQVQ | TVKEGDPSWK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PTFIVKPDSG | CQGDGIYLIK | DPCDGRLTGT | LHNRPAVVQE | YIRKPLLIDK | LKFDIRLYVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LKSLDPLEIY | IAKDGLSRFC | TEPYQEPNPQ | NLHHVFMHLT | NYSLNIHSGK | FVHSDSASTG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SKRTFSSILC | RLSSKGVDIK | KVWSDIISLV | IKTVIALTPE | LKVFYQSDIP | TGRPGPTCFQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ILGFDILLMK | NLKPMLLEVN | ANPSMRIEHE | YELSPGVFEN | IPSLVDEEVK | VAVIRDTLRL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| MDPLKKKKEI | HFPDIYMDRK | HRIPPVSDRM | SSWKHKGSSL | SIVRSQQMEK | SFTSKEDLNC |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DPTGGDSEPN | PEAHLPSICL | KQVFPKYAKQ | FNYLRLVDRM | ANLFIRFLGI | KGTMKLGPTG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FRTFIRNCKL | SSSSLSMAAV | DILYIDITRR | WNSVTVDQRD | SGMCLQAFVE | AFFFLAQRKF |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KLQPLHEQVA | SLIDLCEYHL | SVLDEKRLLC | HRGRPLQRNP | PQMNRPEHSA | TGSSAPRVIG |
| ASKLSQS |