| UniProt ID | SPHK1_HUMAN | |
|---|---|---|
| UniProt AC | Q9NYA1 | |
| Protein Name | Sphingosine kinase 1 | |
| Gene Name | SPHK1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 384 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cell membrane. Translocated from the cytoplasm to the plasma membrane in a CIB1-dependent manner. | |
| Protein Description | Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol.. | |
| Protein Sequence | MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL | |
| 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 |
|---|---|---|---|---|---|
| 36 (in isoform 2) | Phosphorylation | - | 22.22 | - | |
| 46 (in isoform 2) | Phosphorylation | - | 30.58 | - | |
| 55 (in isoform 2) | Phosphorylation | - | 45.76 | 24719451 | |
| 58 (in isoform 2) | Acetylation | - | 39.12 | - | |
| 193 | Phosphorylation | RLGEMRFTLGTFLRL HHHCHHHHHHHHHHH | 17.57 | 18669648 | |
| 225 | Phosphorylation | VGSKTPASPVVVQQG CCCCCCCCCEEEEEC | 21.30 | 15623571 | |
| 279 (in isoform 2) | Phosphorylation | - | 10.72 | 27251275 | |
| 295 | Phosphorylation | FYVRAGVSRAMLLRL HHHHHCCCHHHHHHH | 17.26 | 24719451 | |
| 381 (in isoform 2) | Phosphorylation | - | 77.38 | 24719451 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPHK1_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 SPHK1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TRAF2_HUMAN | TRAF2 | physical | 11777919 | |
| MBTP1_HUMAN | MBTPS1 | physical | 17124500 | |
| BIRC3_HUMAN | BIRC3 | physical | 24464131 | |
| DCXR_HUMAN | DCXR | physical | 26186194 | |
| PPM1G_HUMAN | PPM1G | physical | 26186194 | |
| DHYS_HUMAN | DHPS | physical | 26186194 | |
| CYLD_HUMAN | CYLD | physical | 26186194 | |
| CYLD_HUMAN | CYLD | physical | 28514442 | |
| DCXR_HUMAN | DCXR | physical | 28514442 | |
| DHYS_HUMAN | DHPS | physical | 28514442 | |
| BECN1_HUMAN | BECN1 | physical | 28521610 | |
| TRAF2_HUMAN | TRAF2 | physical | 28521610 |
| 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 | |
| DB08868 | Fingolimod |
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| Phosphorylation | |
| Reference | PubMed |
| "Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitinligase TRAF2."; Alvarez S.E., Harikumar K.B., Hait N.C., Allegood J., Strub G.M.,Kim E.Y., Maceyka M., Jiang H., Luo C., Kordula T., Milstien S.,Spiegel S.; Nature 465:1084-1088(2010). Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF GLY-82, ANDPHOSPHORYLATION AT SER-225. | |
| "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 THR-193, AND MASSSPECTROMETRY. | |