| UniProt ID | HS3SA_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y663 | |
| Protein Name | Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 | |
| Gene Name | HS3ST3A1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 406 | |
| Subcellular Localization |
Golgi apparatus membrane Single-pass type II membrane protein . |
|
| Protein Description | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.. | |
| Protein Sequence | MAPPGPASALSTSAEPLSRSIFRKFLLMLCSLLTSLYVFYCLAERCQTLSGPVVGLSGGGEEAGAPGGGVLAGGPRELAVWPAAAQRKRLLQLPQWRRRRPPAPRDDGEEAAWEEESPGLSGGPGGSGAGSTVAEAPPGTLALLLDEGSKQLPQAIIIGVKKGGTRALLEFLRVHPDVRAVGAEPHFFDRSYDKGLAWYRDLMPRTLDGQITMEKTPSYFVTREAPARISAMSKDTKLIVVVRDPVTRAISDYTQTLSKRPDIPTFESLTFKNRTAGLIDTSWSAIQIGIYAKHLEHWLRHFPIRQMLFVSGERLISDPAGELGRVQDFLGLKRIITDKHFYFNKTKGFPCLKKAEGSSRPHCLGKTKGRTHPEIDREVVRRLREFYRPFNLKFYQMTGHDFGWDG | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 40 | Phosphorylation | LTSLYVFYCLAERCQ HHHHHHHHHHHHHHH | 4.05 | - | |
| 127 | Phosphorylation | LSGGPGGSGAGSTVA CCCCCCCCCCCCCCC | 31.24 | 28787133 | |
| 140 | Phosphorylation | VAEAPPGTLALLLDE CCCCCCCCEEEEECC | 18.03 | 28787133 | |
| 206 | Phosphorylation | YRDLMPRTLDGQITM HHHHCCCCCCCCEEE | 24.27 | 27251275 | |
| 212 | Phosphorylation | RTLDGQITMEKTPSY CCCCCCEEEEECCCC | 16.05 | 27251275 | |
| 215 | Acetylation | DGQITMEKTPSYFVT CCCEEEEECCCCEEE | 55.72 | 30589377 | |
| 216 | Phosphorylation | GQITMEKTPSYFVTR CCEEEEECCCCEEEC | 12.26 | 27251275 | |
| 218 | Phosphorylation | ITMEKTPSYFVTREA EEEEECCCCEEECCC | 36.11 | 29116813 | |
| 222 | Phosphorylation | KTPSYFVTREAPARI ECCCCEEECCCCHHH | 16.94 | 29116813 | |
| 222 | O-linked_Glycosylation | KTPSYFVTREAPARI ECCCCEEECCCCHHH | 16.94 | OGP | |
| 247 | Phosphorylation | VVVRDPVTRAISDYT EEECCHHHHHHHHHH | 21.55 | 24670416 | |
| 273 | N-linked_Glycosylation | FESLTFKNRTAGLID CCCCCCCCCCCCCEE | 42.20 | UniProtKB CARBOHYD | |
| 281 | Phosphorylation | RTAGLIDTSWSAIQI CCCCCEECCCHHHHH | 25.71 | 28387310 | |
| 282 | Phosphorylation | TAGLIDTSWSAIQIG CCCCEECCCHHHHHH | 18.45 | 28387310 | |
| 284 | Phosphorylation | GLIDTSWSAIQIGIY CCEECCCHHHHHHHH | 18.43 | 22468782 | |
| 291 | Phosphorylation | SAIQIGIYAKHLEHW HHHHHHHHHHHHHHH | 12.37 | 22468782 | |
| 339 | Acetylation | LKRIITDKHFYFNKT CCEEEECCCCCCCCC | 27.28 | 7365187 | |
| 344 | N-linked_Glycosylation | TDKHFYFNKTKGFPC ECCCCCCCCCCCCCC | 39.44 | UniProtKB CARBOHYD |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HS3SA_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HS3SA_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HS3SA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HS3SA_HUMAN !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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