| UniProt ID | S23A2_HUMAN | |
|---|---|---|
| UniProt AC | Q9UGH3 | |
| Protein Name | Solute carrier family 23 member 2 | |
| Gene Name | SLC23A2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 650 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
| Protein Description | Sodium/ascorbate cotransporter. Mediates electrogenic uptake of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.. | |
| Protein Sequence | MMGIGKNTTSKSMEAGSSTEGKYEDEAKHPAFFTLPVVINGGATSSGEQDNEDTELMAIYTTENGIAEKSSLAETLDSTGSLDPQRSDMIYTIEDVPPWYLCIFLGLQHYLTCFSGTIAVPFLLADAMCVGYDQWATSQLIGTIFFCVGITTLLQTTFGCRLPLFQASAFAFLAPARAILSLDKWKCNTTDVSVANGTAELLHTEHIWYPRIREIQGAIIMSSLIEVVIGLLGLPGALLKYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAMLTIFLVLLFSQYARNVKFPLPIYKSKKGWTAYKLQLFKMFPIILAILVSWLLCFIFTVTDVFPPDSTKYGFYARTDARQGVLLVAPWFKVPYPFQWGLPTVSAAGVIGMLSAVVASIIESIGDYYACARLSCAPPPPIHAINRGIFVEGLSCVLDGIFGTGNGSTSSSPNIGVLGITKVGSRRVIQCGAALMLALGMIGKFSALFASLPDPVLGALFCTLFGMITAVGLSNLQFIDLNSSRNLFVLGFSIFFGLVLPSYLRQNPLVTGITGIDQVLNVLLTTAMFVGGCVAFILDNTIPGTPEERGIRKWKKGVGKGNKSLDGMESYNLPFGMNIIKKYRCFSYLPISPTFVGYTWKGLRKSDNSRSSDEDSQATG | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MMGIGKNTTSKSMEA CCCCCCCCCCCCCCC | 35.61 | 22210691 | |
| 10 | O-linked_Glycosylation | GIGKNTTSKSMEAGS CCCCCCCCCCCCCCC | 22.24 | 30379171 | |
| 11 | Ubiquitination | IGKNTTSKSMEAGSS CCCCCCCCCCCCCCC | 52.29 | 21906983 | |
| 11 | Ubiquitination | IGKNTTSKSMEAGSS CCCCCCCCCCCCCCC | 52.29 | - | |
| 17 | Phosphorylation | SKSMEAGSSTEGKYE CCCCCCCCCCCCCCC | 40.93 | 21945579 | |
| 18 | Phosphorylation | KSMEAGSSTEGKYED CCCCCCCCCCCCCCC | 29.56 | 21945579 | |
| 19 | Phosphorylation | SMEAGSSTEGKYEDE CCCCCCCCCCCCCCH | 50.91 | 21945579 | |
| 22 | Ubiquitination | AGSSTEGKYEDEAKH CCCCCCCCCCCHHCC | 38.95 | 21906983 | |
| 22 | Ubiquitination | AGSSTEGKYEDEAKH CCCCCCCCCCCHHCC | 38.95 | - | |
| 23 | Phosphorylation | GSSTEGKYEDEAKHP CCCCCCCCCCHHCCC | 39.20 | 21945579 | |
| 60 | Phosphorylation | DTELMAIYTTENGIA CCEEEEEEECCCCCC | 9.70 | 25884760 | |
| 70 | Phosphorylation | ENGIAEKSSLAETLD CCCCCCCCHHHHHHH | 23.30 | 20201521 | |
| 71 | Phosphorylation | NGIAEKSSLAETLDS CCCCCCCHHHHHHHC | 42.54 | 23927012 | |
| 75 | Phosphorylation | EKSSLAETLDSTGSL CCCHHHHHHHCCCCC | 30.20 | 23927012 | |
| 78 | Phosphorylation | SLAETLDSTGSLDPQ HHHHHHHCCCCCCCC | 37.47 | 30266825 | |
| 79 | Phosphorylation | LAETLDSTGSLDPQR HHHHHHCCCCCCCCC | 30.38 | 30266825 | |
| 81 | Phosphorylation | ETLDSTGSLDPQRSD HHHHCCCCCCCCCCC | 29.68 | 29255136 | |
| 184 | Ubiquitination | RAILSLDKWKCNTTD HHHHCCCCCCCCCCC | 54.57 | - | |
| 188 | N-linked_Glycosylation | SLDKWKCNTTDVSVA CCCCCCCCCCCEEEC | 42.14 | UniProtKB CARBOHYD | |
| 196 | N-linked_Glycosylation | TTDVSVANGTAELLH CCCEEECCCCEEEEE | 46.31 | UniProtKB CARBOHYD | |
| 298 | Ubiquitination | KFPLPIYKSKKGWTA CCCCCEECCCCCCEE | 57.42 | - | |
| 498 | Ubiquitination | FCTLFGMITAVGLSN HHHHHHHHHHHCCCC | 1.98 | - | |
| 593 | Ubiquitination | KGVGKGNKSLDGMES CCCCCCCCCCCCHHH | 62.15 | - | |
| 594 | Phosphorylation | GVGKGNKSLDGMESY CCCCCCCCCCCHHHC | 35.37 | - | |
| 612 | Ubiquitination | FGMNIIKKYRCFSYL CCHHHHHHHCCCEEC | 27.76 | - | |
| 613 | Phosphorylation | GMNIIKKYRCFSYLP CHHHHHHHCCCEECC | 13.96 | - | |
| 617 | Phosphorylation | IKKYRCFSYLPISPT HHHHCCCEECCCCCC | 29.41 | 18491316 | |
| 624 | Phosphorylation | SYLPISPTFVGYTWK EECCCCCCCCCCEEC | 24.94 | - | |
| 629 | Phosphorylation | SPTFVGYTWKGLRKS CCCCCCCEECCCCCC | 18.12 | 18491316 | |
| 641 | Phosphorylation | RKSDNSRSSDEDSQA CCCCCCCCCCHHHHC | 41.80 | 24719451 | |
| 646 | Phosphorylation | SRSSDEDSQATG--- CCCCCHHHHCCC--- | 21.48 | - | |
| 649 | Phosphorylation | SDEDSQATG------ CCHHHHCCC------ | 35.47 | 26853621 |
| 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 S23A2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S23A2_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 S23A2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| COA1_HUMAN | COA1 | physical | 26186194 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| 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 |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASSSPECTROMETRY. | |