Q76KB1
Gene name |
HS2ST1 (HS2ST) |
Protein name |
Heparan sulfate 2-O-sulfotransferase 1 |
Names |
cHS2ST |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:395140 |
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
3 structures for Q76KB1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3F5F | X-ray | 265 A | A | 69-356 | PDB |
| 4NDZ | X-ray | 345 A | A/B/C/D/E/F | 69-356 | PDB |
| AF-Q76KB1-F1 | Predicted | AlphaFoldDB |
7 variants for Q76KB1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1057724270 | 32 | Q>H | No | Ensembl | |
| rs1060457858 | 33 | K>M | No | Ensembl | |
| rs1059149497 | 33 | K>N | No | Ensembl | |
| rs739494205 | 147 | D>A | No | Ensembl | |
| rs736873524 | 171 | V>G | No | Ensembl | |
| rs735865524 | 175 | Y>F | No | Ensembl | |
| rs734291166 | 207 | S>A | No | Ensembl |
No associated diseases with Q76KB1
No regional properties for Q76KB1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q76KB1 | |||
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| heparan sulfate 2-O-sulfotransferase activity | Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + heparan sulfate = adenosine 3',5'-bisphosphate + heparan sulfate 2-O-sulfate; results in 2-O-sulfation of iduronic acid residues in heparan sulfate. |
| identical protein binding | Binding to an identical protein or proteins. |
| sulfotransferase activity | Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| gene expression | The process in which a gene's sequence is converted into a mature gene product (protein or RNA). This includes the production of an RNA transcript and its processing, translation and maturation for protein-coding genes. |
| heparan sulfate proteoglycan biosynthetic process, enzymatic modification | The modification, often by sulfation, of sugars incorporated into heparan sulfate after polymerization. |
| heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process | The chemical reactions and pathways resulting in the formation of polysaccharide chain component of heparan sulfate proteoglycan. |
| heparin metabolic process | The chemical reactions and pathways involving heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells. They are similar to heparan sulfates but are of somewhat higher average Mr (6000-20000) and contain fewer N-acetyl groups and more N-sulfate and O-sulfate groups; they may be attached in the same manner to protein, forming proteoglycans. They consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues. |
| ureteric bud formation | The developmental process pertaining to the initial formation of the ureteric bud from the Wolffian duct. This process begins when the bud protrudes from the duct and ends when it is a recognizable bud. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGLLRIMLPP | KLQLLAVLVF | GVAVLFLENQ | IQKLEESRGK | LERAIARHEV | REIEQRHTAD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPRQEVALDE | EDDVVIIYNR | VPKTASTSFT | NIAYDLCAKN | RYHVLHINTT | KNNPVMSLQD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QVRFVKNVTS | WKEMKPGFYH | GHVSYLDFAK | FGVKKKPIYI | NVIRDPIERL | VSYYYFLRFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DDYRPGLRRR | KQGDKKTFDE | CVAAGGSDCA | PEKLWLQIPF | FCGHSSECWN | VGSRWALEQA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KYNLINEYFL | VGVTEELEDF | IMLLEAALPR | FFRGATELYR | TGKKSHLRKT | TEKKLPTKET |
| 310 | 320 | 330 | 340 | 350 | |
| IAKLQQSEIW | KMENEFYEFA | LEQFQFVRAH | AVREKDGELY | ILAQNFFYEK | IYPKSN |