O77783
PR
Gene name |
EXT2 |
Protein name |
Exostosin-2 |
Names |
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase, HS-polymerase, HS-POL, Multiple exostoses protein 2 homolog |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
|
EC number |
2.4.1.224: Hexosyltransferases |
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 O77783
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O77783-F1 | Predicted | AlphaFoldDB |
No variants for O77783
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O77783 | |||||
No associated diseases with O77783
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.224 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| 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 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. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetylglucosaminyltransferase activity | Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar. |
| glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity | Catalysis of the reaction: beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan + UDP-N-acetyl-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan + UDP. |
| glucuronosyltransferase activity | Catalysis of the reaction: UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside. |
| glycosyltransferase activity | Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor). |
| metal ion binding | Binding to a metal ion. |
| N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity | Catalysis of the reaction: N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-proteoglycan + UDP-alpha-D-glucuronate = beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-proteoglycan + UDP. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| glycosaminoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of glycosaminoglycans, any of a group of polysaccharides that contain amino sugars. |
| heparan sulfate proteoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of the heparan sulfate proteoglycan, a glycosaminoglycan with repeat unit consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues; the former are a mixture of sulfated and nonsulfated D-glucuronic acid and L-iduronic acid; the L-iduronic acid is either sulfated or acetylated on its amino group as well as being sulfated on one of its hydroxyl groups; heparan sulfate chains are covalently linked to peptidyl-serine by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylosyl to serine residues. |
| N-acetylglucosamine metabolic process | The chemical reactions and pathways involving N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A5D7I4 | EXT1 | Exostosin-1 | Bos taurus (Bovine) | PR |
| Q9Y169 | sotv | Exostosin-2 | Drosophila melanogaster (Fruit fly) | PR |
| Q9ES89 | Extl2 | Exostosin-like 2 | Mus musculus (Mouse) | PR |
| P70428 | Ext2 | Exostosin-2 | Mus musculus (Mouse) | PR |
| Q94AA9 | XGD1 | Xylogalacturonan beta-1,3-xylosyltransferase | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q3EAR7 | At3g42180 | Probable glycosyltransferase At3g42180 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9LFP3 | At5g11130/At5g11120 | Probable glycosyltransferase At5g11130 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MCASVKYNIR | GPALIPRMKT | KHRIYYITLF | SIVLLGLIAT | GMFQFWPHSI | ESSGDWSVEK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RTGRDVPLVR | LPADSPVPER | GDLSCRMHTC | FDVYRCGFNP | KNKIKVYIYP | LKKYVGEAGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PVSSTISREY | NELLTAISDS | DYYTDDVTRA | CLFVPSIDLL | NQNSLRVKET | AQALAQLSRW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DRGTNHLLFN | MLPGGPPDYN | TALDVPRDRA | LLAGGGFSTW | TYRQGYDVSI | PVYSPLSAEV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DLPEKGPGPR | RYFLLSSQVA | LHPEYREDLA | ALQARHGEAV | LVLDKCSNLS | EGVPAARRRC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HQQQAFDYPQ | VLQEATFCMV | LRGARLGQAV | LSDVLRAGCV | PVIIADSYVL | PFSEVLDWKR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASVVVPEEKM | SDVYSILQSI | PRRQIEEMQR | QARWFWEAYF | QSIKAIALAT | LQIINDRIYP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YAAISYEDWN | DPPAVKWGSV | SNPLFLPLIP | PQSQGFTAIV | LTYDRVESLF | RVITEVSKVP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SLSKLLVVWN | NQNKNPPEDS | LWPKIRVPLK | VVRTAENKLS | NRFFPYDEIE | TEAVLAIDDD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IIMLTSDELQ | FGYEVWREFP | DRLVGYPGRL | HLWDHEMNKW | KYESEWTNEV | SMVLTGAAFY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HKYFNYLYTY | KMPGDIKNWV | DAHMNCEDIA | MNFLVANVTG | KAVIKVTPRK | KFKCPECTAI |
| 670 | 680 | 690 | 700 | 710 | |
| DGLSLDQTHM | VERSECINKF | ASVFGTMPLK | VVEHRADPVL | YKDDFPEKLK | SFPNIGSL |