Q92182
Gene name |
ST6GAL1 (SIAT1) |
Protein name |
Beta-galactoside alpha-2,6-sialyltransferase 1 |
Names |
Alpha 2,6-ST 1, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, ST6Gal I, ST6GalI, Sialyltransferase 1 |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:396169 |
EC number |
2.4.3.1: Sialyltransferases |
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 Q92182
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q92182-F1 | Predicted | AlphaFoldDB |
No variants for Q92182
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q92182 | |||||
No associated diseases with Q92182
No regional properties for Q92182
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q92182 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.3.1 | Sialyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi cisterna membrane | The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| beta-galactoside alpha-2,6-sialyltransferase activity | Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl-(2->6)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| N-acetylneuraminate metabolic process | The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid. |
| 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. |
| sialylation | The covalent attachment of sialic acid to a substrate molecule. |
11 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q92184 | ST6GALNAC2 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 | Gallus gallus (Chicken) | PR |
| Q701R0 | ST6GAL2 | Beta-galactoside alpha-2,6-sialyltransferase 2 | Gallus gallus (Chicken) | PR |
| Q9UJ37 | ST6GALNAC2 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 | Homo sapiens (Human) | PR |
| Q96JF0 | ST6GAL2 | Beta-galactoside alpha-2,6-sialyltransferase 2 | Homo sapiens (Human) | PR |
| Q9BVH7 | ST6GALNAC5 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 | Homo sapiens (Human) | PR |
| P15907 | ST6GAL1 | Beta-galactoside alpha-2,6-sialyltransferase 1 | Homo sapiens (Human) | PR |
| Q9QYJ1 | St6galnac5 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 | Mus musculus (Mouse) | PR |
| P70277 | St6galnac2 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 | Mus musculus (Mouse) | PR |
| Q64685 | St6gal1 | Beta-galactoside alpha-2,6-sialyltransferase 1 | Mus musculus (Mouse) | PR |
| P13721 | St6gal1 | Beta-galactoside alpha-2,6-sialyltransferase 1 | Rattus norvegicus (Rat) | PR |
| Q9SGD2 | GALT29A | Beta-1,6-galactosyltransferase GALT29A | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVHINVLKKF | MCVLVVILIA | LTVCLWKETR | GSYYVPLKND | GTQVHRALDK | WNLLKSQGLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HEAAGEMGQM | PKALPNNQNK | VKGITSGAVE | KSRKAAEHVK | VWDKDSSSRN | LIPRLQKVRK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NYLSMNKYNV | TYNGKMNAAK | LSPEQLLCRL | RDRVNVTMIR | GSDGPFNSSE | WQHYLPDKSL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NETVGRLGRC | AVVSSAGSLK | SSHLGPEIDS | HDAVLRFNGA | PVKGFQEDVG | QKTTIRLVNS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QLVTVEEQQF | LKDALYNTGI | LIVWDPAPYH | AEIHEWYRKP | DYKFFEAYKS | YRIRHPEQPF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YILNPKMQWQ | LWDILQENSL | EHIQPNPPSS | GMLGIVIMMT | LCDEVDVYEF | LPSKRQTDIC |
| 370 | 380 | 390 | 400 | 410 | |
| HYYQKFHDHA | CTMGAYHPLL | FEKNLVKHLN | QGTDEDIYTH | GKVTLPGFRN | VHC |