P17248
Gene name |
WARS1 (WARS) |
Protein name |
Tryptophan--tRNA ligase, cytoplasmic |
Names |
Tryptophanyl-tRNA synthetase, TrpRS |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:281576 |
EC number |
6.1.1.2: Ligases forming aminoacyl-tRNA and related compounds |
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 P17248
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P17248-F1 | Predicted | AlphaFoldDB |
50 variants for P17248
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs463033649 | 2 | A>S | No | EVA | |
| rs477663997 | 4 | M>I | No | EVA | |
| rs439646614 | 4 | M>K | No | EVA | |
| rs460707386 | 10 | G>C | No | EVA | |
| rs440740515 | 10 | G>D | No | EVA | |
| rs454559497 | 11 | C>G | No | EVA | |
| rs444024548 | 11 | C>S | No | EVA | |
| rs475373237 | 13 | S>P | No | EVA | |
| rs452131042 | 22 | A>S | No | EVA | |
| rs466771840 | 24 | Q>E | No | EVA | |
| rs436284132 | 24 | Q>H | No | EVA | |
| rs453071301 | 24 | Q>P | No | EVA | |
| rs450670550 | 25 | G>E | No | EVA | |
| rs467478777 | 25 | G>R | No | EVA | |
| rs437973212 | 30 | D>A | No | EVA | |
| rs469362386 | 30 | D>E | No | EVA | |
| rs446102336 | 31 | L>P | No | EVA | |
| rs434462272 | 32 | K>E | No | EVA | |
| rs460741328 | 33 | A>P | No | EVA | |
| rs481745738 | 35 | N>T | No | EVA | |
| rs444713621 | 36 | A>G | No | EVA | |
| rs461664497 | 36 | A>P | No | EVA | |
| rs458506031 | 37 | A>P | No | EVA | |
| rs455350316 | 45 | V>M | No | EVA | |
| rs461448545 | 65 | V>A | No | EVA | |
| rs451111377 | 70 | G>R | No | EVA | |
| rs451111377 | 70 | G>W | No | EVA | |
| rs463510261 | 79 | G>V | No | EVA | |
| rs443560560 | 88 | D>H | No | EVA | |
| rs457429348 | 103 | I>V | No | EVA | |
| rs471649983 | 106 | D>V | No | EVA | |
| rs447622412 | 110 | V>D | No | EVA | |
| rs517937759 | 263 | V>I | No | EVA | |
| rs434457222 | 319 | D>A | No | EVA | |
| rs465962692 | 326 | R>W | No | EVA | |
| rs449088520 | 327 | D>N | No | EVA | |
| rs435348560 | 333 | G>A | No | EVA | |
| rs524529221 | 333 | G>S | No | EVA | |
| rs470078154 | 334 | Y>S | No | EVA | |
| rs449958807 | 341 | H>N | No | EVA | |
| rs476402589 | 418 | L>V | No | EVA | |
| rs476043884 | 428 | G>R | No | EVA | |
| rs452768093 | 439 | L>R | No | EVA | |
| rs432637046 | 445 | P>H | No | EVA | |
| rs452804502 | 450 | H>D | No | EVA | |
| rs435920749 | 454 | R>P | No | EVA | |
| rs467304589 | 455 | K>Q | No | EVA | |
| rs450456262 | 457 | V>D | No | EVA | |
| rs437020680 | 461 | I>F | No | EVA | |
| rs445126470 | 466 | M>K | No | EVA |
No associated diseases with P17248
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.2 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| kinase inhibitor activity | Binds to and stops, prevents or reduces the activity of a kinase. |
| protein domain specific binding | Binding to a specific domain of a protein. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| tryptophan-tRNA ligase activity | Catalysis of the reaction: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophanyl-tRNA(Trp). |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of protein kinase activity | Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity. |
| positive regulation of gene expression | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). |
| positive regulation of protein-containing complex assembly | Any process that activates or increases the frequency, rate or extent of protein complex assembly. |
| regulation of angiogenesis | Any process that modulates the frequency, rate or extent of angiogenesis. |
| regulation of protein ADP-ribosylation | Any process that modulates the frequency, rate or extent of protein ADP-ribosylation. Protein ADP-ribosylation is the transfer, from NAD, of ADP-ribose to protein amino acids. |
| tryptophanyl-tRNA aminoacylation | The process of coupling tryptophan to tryptophanyl-tRNA, catalyzed by tryptophanyl-tRNA synthetase. The tryptophanyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tryptophan-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P23381 | WARS1 | Tryptophan--tRNA ligase, cytoplasmic | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADMSNGEQG | CGSPLELFHS | IAAQGELVRD | LKARNAAKDE | IDSAVKMLLS | LKTSYKAATG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EDYKVDCPPG | DPAPESGEGL | DATEADEDFV | DPWTVQTSSA | KGIDYDKLIV | RFGSSKIDKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVNRIERATG | QRPHRFLRRG | IFFSHRDMHQ | ILDAYENKKP | FYLYTGRGPS | SEAMHVGHLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PFIFTKWLQD | VFNVPLVIQM | TDDEKYLWKD | LTLDQAYGYA | VENAKDIIAC | GFDINKTFIF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SDLDYMGMSP | GFYKNVVKIQ | KHVTFNQVKG | IFGFTDSDCI | GKISFPAIQA | APSFSNSFPQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IFRDRTDVQC | LIPCAIDQDP | YFRMTRDVAP | RIGYPKPALL | HSTFFPALQG | AQTKMSASDP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NSSIFLTDTA | KQIKTKVNKH | AFSGGRDTVE | EHRQFGGNCD | VDVSFMYLTF | FLEDDDKLEQ |
| 430 | 440 | 450 | 460 | 470 | |
| IRRDYTSGAM | LTGELKKELI | EVLQPLIAEH | QARRKEVTDE | IVKEFMTPRK | LSYDFQ |