Q2KJI2
PR
Gene name |
STT3A |
Protein name |
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A |
Names |
Oligosaccharyl transferase subunit STT3A, STT3-A |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:507815 |
EC number |
2.4.99.18: Transferring other glycosyl groups |
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 Q2KJI2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2KJI2-F1 | Predicted | AlphaFoldDB |
31 variants for Q2KJI2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs463246061 | 7 | L>S | No | EVA | |
| rs438959503 | 34 | R>S | No | EVA | |
| rs477480519 | 119 | L>M | No | EVA | |
| rs438516309 | 202 | Y>* | No | EVA | |
| rs458585882 | 203 | F>I | No | EVA | |
| rs440958577 | 204 | Y>C | No | EVA | |
| rs472291910 | 204 | Y>D | No | EVA | |
| rs449679065 | 205 | M>I | No | EVA | |
| rs447139998 | 273 | V>L | No | EVA | |
| rs454520225 | 275 | G>D | No | EVA | |
| rs478672510 | 294 | Q>E | No | EVA | |
| rs471026549 | 335 | D>E | No | EVA | |
| rs526474609 | 359 | S>T | No | EVA | |
| rs453670141 | 467 | F>S | No | EVA | |
| rs441080473 | 502 | F>L | No | EVA | |
| rs459408755 | 504 | D>G | No | EVA | |
| rs447941333 | 511 | W>L | No | EVA | |
| rs432057622 | 520 | A>P | No | EVA | |
| rs452067587 | 520 | A>V | No | EVA | |
| rs479165225 | 596 | F>L | No | EVA | |
| rs468068782 | 597 | L>P | No | EVA | |
| rs451013384 | 605 | S>G | No | EVA | |
| rs433076381 | 616 | D>E | No | EVA | |
| rs464396591 | 616 | D>G | No | EVA | |
| rs450575003 | 616 | D>H | No | EVA | |
| rs453137679 | 617 | Y>S | No | EVA | |
| rs478007621 | 655 | K>R | No | EVA | |
| rs466843677 | 656 | R>C | No | EVA | |
| rs435508413 | 656 | R>P | No | EVA | |
| rs798034614 | 687 | W>R | No | EVA | |
| rs447741755 | 702 | L>F | No | EVA |
No associated diseases with Q2KJI2
No regional properties for Q2KJI2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q2KJI2 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.99.18 | Transferring other glycosyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| oligosaccharyltransferase III complex | An oligosaccharyltransferase (OST) complex that contains the seven polypeptides found in OST complex I, plus heterotrimeric Sec61alpha-beta-gamma and the tetrameric TRAP complex. Of the three forms of mammalian OST complexes identified, the OSTIII complex has the strongest affinity for ribosomes. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| dolichyl-diphosphooligosaccharide-protein glycotransferase activity | Catalysis of the reaction: dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by glycosylamine linkage to protein L-asparagine. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| co-translational protein modification | The process of covalently altering one or more amino acids in a protein after translation has begun but before the protein has been released from the ribosome. |
| post-translational protein modification | The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome. |
| protein N-linked glycosylation via asparagine | The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P39007 | STT3 | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q8TCJ2 | STT3B | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B | Homo sapiens (Human) | PR |
| P46977 | STT3A | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A | Homo sapiens (Human) | PR |
| Q3TDQ1 | Stt3b | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B | Mus musculus (Mouse) | PR |
| P46978 | Stt3a | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A | Mus musculus (Mouse) | PR |
| Q7XQ88 | STT3B | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B | Oryza sativa subsp japonica (Rice) | PR |
| P46975 | stt-3 | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3 | Caenorhabditis elegans | PR |
| Q93ZY3 | STT3A | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FX21 | STT3B | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTKLGFLRLS | YEKQDTLLKL | LILSMAAVLS | FSTRLFAVLR | FESVIHEFDP | YFNYRTTRFL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEEGFYKFHN | WFDDRAWYPL | GRIIGGTIYP | GLMITSAAIY | HVLHFFHITI | DIRNVCVFLA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLFSSFTTIV | TYHLTKELKD | AGAGLLAAAM | IAVVPGYISR | SVAGSYDNEG | IAIFCMLLTY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YMWIKAVKTG | SIYWAAKCAL | AYFYMVSSWG | GYVFLINLIP | LHVLVLMLTG | RFSHRIYVAY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CTVYCLGTIL | SMQISFVGFQ | PVLSSEHMAA | FGVFGLCQIH | AFVDYLRSKL | NPQQFEVLFR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVISLVGFVL | LTIGALLMLT | GKISPWTGRF | YSLLDPSYAK | NNIPIIASVS | EHQPTTWSSY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YFDLQLLVFM | FPVGLYYCFS | NLSDARIFII | MYGVTSMYFS | AVMVRLMLVL | APVMCILSGI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GVSQVLSTYM | KNLDISRQDK | KSKKQQDSTY | PIKNEVASGM | ILVMAFFLIT | YTFHSTWVTS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EAYSSPSIVL | SARGGDGSRI | IFDDFREAYY | WLRHNTPEDA | KVMSWWDYGY | QITAMANRTI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LVDNNTWNNT | HISRVGQAMA | STEEKAYEIM | RELDVSYVLV | IFGGLTGYSS | DDINKFLWMV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RIGGSTDTGK | HIKEHDYYTP | TGEFRVDREG | SPVLLNCLMY | KMCYYRFGQV | YTEAKRPLGY |
| 670 | 680 | 690 | 700 | ||
| DRVRNAEIGN | KDFELDVLEE | AYTTEHWLVR | IYKVKDLDNR | GLSRT |