UniProt ID | S13A5_HUMAN | |
---|---|---|
UniProt AC | Q86YT5 | |
Protein Name | Solute carrier family 13 member 5 | |
Gene Name | SLC13A5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 568 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. Cell membrane . |
|
Protein Description | High-affinity sodium/citrate cotransporter that mediates citrate entry into cells. The transport process is electrogenic; it is the trivalent form of citrate rather than the divalent form that is recognized as a substrate. May facilitate the utilization of circulating citrate for the generation of metabolic energy and for the synthesis of fatty acids and cholesterol.. | |
Protein Sequence | MASALSYVSKFKSFVILFVTPLLLLPLVILMPAKFVRCAYVIILMAIYWCTEVIPLAVTSLMPVLLFPLFQILDSRQVCVQYMKDTNMLFLGGLIVAVAVERWNLHKRIALRTLLWVGAKPARLMLGFMGVTALLSMWISNTATTAMMVPIVEAILQQMEATSAATEAGLELVDKGKAKELPGSQVIFEGPTLGQQEDQERKRLCKAMTLCICYAASIGGTATLTGTGPNVVLLGQMNELFPDSKDLVNFASWFAFAFPNMLVMLLFAWLWLQFVYMRFNFKKSWGCGLESKKNEKAALKVLQEEYRKLGPLSFAEINVLICFFLLVILWFSRDPGFMPGWLTVAWVEGETKYVSDATVAIFVATLLFIVPSQKPKFNFRSQTEEERKTPFYPPPLLDWKVTQEKVPWGIVLLLGGGFALAKGSEASGLSVWMGKQMEPLHAVPPAAITLILSLLVAVFTECTSNVATTTLFLPIFASMSRSIGLNPLYIMLPCTLSASFAFMLPVATPPNAIVFTYGHLKVADMVKTGVIMNIIGVFCVFLAVNTWGRAIFDLDHFPDWANVTHIET | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MASALSYVSK -----CCCHHHHHHH | 28.57 | 30001349 | |
6 | Phosphorylation | --MASALSYVSKFKS --CCCHHHHHHHCCH | 24.17 | 24043423 | |
7 | Phosphorylation | -MASALSYVSKFKSF -CCCHHHHHHHCCHH | 15.03 | 24043423 | |
9 | Phosphorylation | ASALSYVSKFKSFVI CCHHHHHHHCCHHHH | 24.92 | 24043423 | |
184 | Phosphorylation | KAKELPGSQVIFEGP CCCCCCCCEEEEECC | 21.23 | 28258704 | |
424 | Phosphorylation | GFALAKGSEASGLSV CCHHHCCCCCCCCEE | 29.32 | 22210691 | |
427 | Phosphorylation | LAKGSEASGLSVWMG HHCCCCCCCCEEECC | 35.89 | - | |
430 | Phosphorylation | GSEASGLSVWMGKQM CCCCCCCEEECCCCC | 19.77 | - | |
562 | N-linked_Glycosylation | DHFPDWANVTHIET- CCCCCCCCCCCCCC- | 34.66 | 19159218 |
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 S13A5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S13A5_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 S13A5_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EF1A2_HUMAN | EEF1A2 | physical | 28514442 |
Kegg Disease | ||||||
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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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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-562, AND MASSSPECTROMETRY. |