| UniProt ID | S35A2_HUMAN | |
|---|---|---|
| UniProt AC | P78381 | |
| Protein Name | UDP-galactose translocator | |
| Gene Name | SLC35A2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 396 | |
| Subcellular Localization |
Golgi apparatus membrane Multi-pass membrane protein. |
|
| Protein Description | Transports nucleotide sugars from the cytosol into Golgi vesicles where glycosyltransferases function.. | |
| Protein Sequence | MAAVGAGGSTAAPGPGAVSAGALEPGTASAAHRRLKYISLAVLVVQNASLILSIRYARTLPGDRFFATTAVVMAEVLKGLTCLLLLFAQKRGNVKHLVLFLHEAVLVQYVDTLKLAVPSLIYTLQNNLQYVAISNLPAATFQVTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGGGPRPLDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWAEGTAVATRGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVASIRLFGFHVDPLFALGAGLVIGAVYLYSLPRGAAKAIASASASASGPCVHQQPPGQPPPPQLSSHRGDLITEPFLPKLLTKVKGS | |
| 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 |
|---|---|---|---|---|---|
| 9 | Phosphorylation | AAVGAGGSTAAPGPG CCCCCCCCCCCCCCC | 17.60 | 28857561 | |
| 10 | Phosphorylation | AVGAGGSTAAPGPGA CCCCCCCCCCCCCCC | 30.07 | 28857561 | |
| 19 | Phosphorylation | APGPGAVSAGALEPG CCCCCCCCCCCCCCC | 22.05 | 28857561 | |
| 27 | Phosphorylation | AGALEPGTASAAHRR CCCCCCCCCCHHHHH | 28.31 | 28857561 | |
| 29 | Phosphorylation | ALEPGTASAAHRRLK CCCCCCCCHHHHHHH | 26.31 | 28857561 | |
| 227 | Phosphorylation | FEKILKGSSGSVWLR HHHHHHCCCCCCHHH | 29.91 | 22817900 | |
| 228 | Phosphorylation | EKILKGSSGSVWLRN HHHHHCCCCCCHHHH | 43.70 | 22817900 | |
| 256 | Phosphorylation | GLWWAEGTAVATRGF HHHHHHCCEEEECCC | 14.95 | 22210691 | |
| 260 | Phosphorylation | AEGTAVATRGFFFGY HHCCEEEECCCCCCC | 25.40 | 22210691 | |
| 301 | Phosphorylation | NILKGFATSLSIVLS HHHHHHHHHHHHHHH | 28.12 | 25262027 | |
| 302 | Phosphorylation | ILKGFATSLSIVLST HHHHHHHHHHHHHHH | 19.38 | 28857561 | |
| 304 | Phosphorylation | KGFATSLSIVLSTVA HHHHHHHHHHHHHHH | 15.49 | 25262027 | |
| 308 | Phosphorylation | TSLSIVLSTVASIRL HHHHHHHHHHHHHHH | 15.22 | 25262027 | |
| 309 | Phosphorylation | SLSIVLSTVASIRLF HHHHHHHHHHHHHHH | 18.87 | 25262027 | |
| 312 | Phosphorylation | IVLSTVASIRLFGFH HHHHHHHHHHHHCCC | 12.14 | 25262027 | |
| 350 | Phosphorylation | GAAKAIASASASASG HHHHHHHHHHHCCCC | 19.35 | 28348404 | |
| 352 | Phosphorylation | AKAIASASASASGPC HHHHHHHHHCCCCCC | 21.91 | 28348404 | |
| 354 | Phosphorylation | AIASASASASGPCVH HHHHHHHCCCCCCCC | 22.07 | 28348404 | |
| 356 | Phosphorylation | ASASASASGPCVHQQ HHHHHCCCCCCCCCC | 40.55 | 28348404 |
| 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 S35A2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S35A2_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 S35A2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| KR103_HUMAN | KRTAP10-3 | physical | 25416956 | |
| TRY2_HUMAN | PRSS2 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 300896 | Congenital disorder of glycosylation 2M (CDG2M) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-228, ANDMASS SPECTROMETRY. | |