SPHK1_HUMAN - dbPTM
SPHK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* 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-45.7624719451
58 (in isoform 2)Acetylation-39.12-
193PhosphorylationRLGEMRFTLGTFLRL
HHHCHHHHHHHHHHH
17.5718669648
225PhosphorylationVGSKTPASPVVVQQG
CCCCCCCCCEEEEEC
21.3015623571
279 (in isoform 2)Phosphorylation-10.7227251275
295PhosphorylationFYVRAGVSRAMLLRL
HHHHHCCCHHHHHHH
17.2624719451
381 (in isoform 2)Phosphorylation-77.3824719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
225SPhosphorylationKinaseMAPK1P28482
GPS
225SPhosphorylationKinaseMAPK3P27361
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPHK1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
11777919
MBTP1_HUMANMBTPS1physical
17124500
BIRC3_HUMANBIRC3physical
24464131
DCXR_HUMANDCXRphysical
26186194
PPM1G_HUMANPPM1Gphysical
26186194
DHYS_HUMANDHPSphysical
26186194
CYLD_HUMANCYLDphysical
26186194
CYLD_HUMANCYLDphysical
28514442
DCXR_HUMANDCXRphysical
28514442
DHYS_HUMANDHPSphysical
28514442
BECN1_HUMANBECN1physical
28521610
TRAF2_HUMANTRAF2physical
28521610

Drug and Disease Associations
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
DB08868Fingolimod
Regulatory Network of SPHK1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP