| UniProt ID | SO4A1_HUMAN | |
|---|---|---|
| UniProt AC | Q96BD0 | |
| Protein Name | Solute carrier organic anion transporter family member 4A1 | |
| Gene Name | SLCO4A1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 722 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein. |
|
| Protein Description | Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, and of estrone-3-sulfate and taurocholate.. | |
| Protein Sequence | MPLHQLGDKPLTFPSPNSAMENGLDHTPPSRRASPGTPLSPGSLRSAAHSPLDTSKQPLCQLWAEKHGARGTHEVRYVSAGQSVACGWWAFAPPCLQVLNTPKGILFFLCAAAFLQGMTVNGFINTVITSLERRYDLHSYQSGLIASSYDIAACLCLTFVSYFGGSGHKPRWLGWGVLLMGTGSLVFALPHFTAGRYEVELDAGVRTCPANPGAVCADSTSGLSRYQLVFMLGQFLHGVGATPLYTLGVTYLDENVKSSCSPVYIAIFYTAAILGPAAGYLIGGALLNIYTEMGRRTELTTESPLWVGAWWVGFLGSGAAAFFTAVPILGYPRQLPGSQRYAVMRAAEMHQLKDSSRGEASNPDFGKTIRDLPLSIWLLLKNPTFILLCLAGATEATLITGMSTFSPKFLESQFSLSASEAATLFGYLVVPAGGGGTFLGGFFVNKLRLRGSAVIKFCLFCTVVSLLGILVFSLHCPSVPMAGVTASYGGSLLPEGHLNLTAPCNAACSCQPEHYSPVCGSDGLMYFSLCHAGCPAATETNVDGQKVYRDCSCIPQNLSSGFGHATAGKCTSTCQRKPLLLVFIFVVIFFTFLSSIPALTATLRCVRDPQRSFALGIQWIVVRILGGIPGPIAFGWVIDKACLLWQDQCGQQGSCLVYQNSAMSRYILIMGLLYKVLGVLFFAIACFLYKPLSESSDGLETCLPSQSSAPDSATDSQLQSSV | |
| 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 | Ubiquitination | PLHQLGDKPLTFPSP CHHHCCCCCCCCCCC | 39.88 | 29967540 | |
| 12 | Phosphorylation | QLGDKPLTFPSPNSA HCCCCCCCCCCCCHH | 41.86 | 23186163 | |
| 15 | Phosphorylation | DKPLTFPSPNSAMEN CCCCCCCCCCHHHHC | 32.30 | 25159151 | |
| 18 | Phosphorylation | LTFPSPNSAMENGLD CCCCCCCHHHHCCCC | 32.17 | 25159151 | |
| 27 | Phosphorylation | MENGLDHTPPSRRAS HHCCCCCCCCCCCCC | 36.24 | 25159151 | |
| 30 | Phosphorylation | GLDHTPPSRRASPGT CCCCCCCCCCCCCCC | 35.29 | 25159151 | |
| 34 | Phosphorylation | TPPSRRASPGTPLSP CCCCCCCCCCCCCCC | 23.27 | 30266825 | |
| 37 | Phosphorylation | SRRASPGTPLSPGSL CCCCCCCCCCCCCCH | 25.17 | 23927012 | |
| 40 | Phosphorylation | ASPGTPLSPGSLRSA CCCCCCCCCCCHHHH | 28.55 | 23927012 | |
| 43 | Phosphorylation | GTPLSPGSLRSAAHS CCCCCCCCHHHHCCC | 24.80 | 25159151 | |
| 46 | Phosphorylation | LSPGSLRSAAHSPLD CCCCCHHHHCCCCCC | 34.79 | 25159151 | |
| 50 | Phosphorylation | SLRSAAHSPLDTSKQ CHHHHCCCCCCCCCC | 23.56 | 28355574 | |
| 54 | Phosphorylation | AAHSPLDTSKQPLCQ HCCCCCCCCCCCHHH | 45.57 | 29396449 | |
| 55 | Phosphorylation | AHSPLDTSKQPLCQL CCCCCCCCCCCHHHH | 29.03 | 30576142 | |
| 56 | Ubiquitination | HSPLDTSKQPLCQLW CCCCCCCCCCHHHHH | 59.01 | 21963094 | |
| 66 | Ubiquitination | LCQLWAEKHGARGTH HHHHHHHHHCCCCEE | 39.32 | 21963094 | |
| 197 | Phosphorylation | PHFTAGRYEVELDAG CCCCCCCEEEEEECC | 24.33 | - | |
| 300 | Phosphorylation | MGRRTELTTESPLWV CCCCCCCCCCCCCEE | 23.45 | 22210691 | |
| 353 (in isoform 3) | Ubiquitination | - | 49.33 | 21906983 | |
| 353 (in isoform 1) | Ubiquitination | - | 49.33 | 21906983 | |
| 353 (in isoform 4) | Ubiquitination | - | 49.33 | 21906983 | |
| 353 | Ubiquitination | AAEMHQLKDSSRGEA HHHHHHCCCCCCCCC | 49.33 | 21906983 | |
| 355 | Phosphorylation | EMHQLKDSSRGEASN HHHHCCCCCCCCCCC | 21.98 | 25159151 | |
| 356 | Phosphorylation | MHQLKDSSRGEASNP HHHCCCCCCCCCCCC | 55.21 | 25627689 | |
| 361 | Phosphorylation | DSSRGEASNPDFGKT CCCCCCCCCCCCCCH | 44.59 | 26657352 | |
| 367 (in isoform 1) | Ubiquitination | - | 40.55 | 21906983 | |
| 367 (in isoform 3) | Ubiquitination | - | 40.55 | 21906983 | |
| 367 (in isoform 4) | Ubiquitination | - | 40.55 | 21906983 | |
| 367 | Ubiquitination | ASNPDFGKTIRDLPL CCCCCCCCHHHHCCH | 40.55 | 21963094 | |
| 394 | Phosphorylation | LLCLAGATEATLITG HHHHCCCCHHHHHHC | 25.82 | - | |
| 406 | Phosphorylation | ITGMSTFSPKFLESQ HHCCCCCCHHHHHHC | 27.54 | 24719451 | |
| 499 | N-linked_Glycosylation | LLPEGHLNLTAPCNA CCCCCCCCCCCCCCC | 29.66 | UniProtKB CARBOHYD | |
| 557 | N-linked_Glycosylation | DCSCIPQNLSSGFGH CCCCCCCCCCCCCCC | 36.21 | UniProtKB CARBOHYD | |
| 569 | Ubiquitination | FGHATAGKCTSTCQR CCCCCCCCCCCHHCC | 31.69 | 21963094 | |
| 666 | Phosphorylation | QNSAMSRYILIMGLL CCCHHHHHHHHHHHH | 7.86 | 25072903 | |
| 674 | Phosphorylation | ILIMGLLYKVLGVLF HHHHHHHHHHHHHHH | 12.23 | 25072903 |
| 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 SO4A1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SO4A1_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 SO4A1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SO4A1_HUMAN !! | ||||
| 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 |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; THR-37; SER-40;SER-43; SER-46 AND SER-50, AND MASS SPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY. | |
| "Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY. | |