dbPTM

SPHK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPHK2_HUMAN
UniProt AC	Q9NRA0
Protein Name	Sphingosine kinase 2
Gene Name	SPHK2
Organism	Homo sapiens (Human).
Sequence Length	654
Subcellular Localization	Isoform 1: Cytoplasm. Membrane. Isoform 2: Lysosome membrane.
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-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides..
Protein Sequence	MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRPPRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSVSDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVLMLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQLGYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
105	Phosphorylation	SGCCTLRSRSPSDSA ECCEEECCCCCCCCC	39.98	19276368
107	Phosphorylation	CCTLRSRSPSDSAAY CEEECCCCCCCCCEE	29.96	19276368
109	Phosphorylation	TLRSRSPSDSAAYFC EECCCCCCCCCEEEE	45.50	28464451
111	Phosphorylation	RSRSPSDSAAYFCIY CCCCCCCCCEEEEEE	21.09	28464451
114	Phosphorylation	SPSDSAAYFCIYTYP CCCCCCEEEEEEECC	9.94	28450419
262 (in isoform 3)	Phosphorylation	-	67.33	22210691
263 (in isoform 3)	Phosphorylation	-	14.17	25627689
264 (in isoform 3)	Phosphorylation	-	43.38	25627689
265 (in isoform 3)	Phosphorylation	-	55.28	25627689
266 (in isoform 3)	Phosphorylation	-	8.50	22210691
267 (in isoform 3)	Phosphorylation	-	6.54	22210691
273 (in isoform 3)	Phosphorylation	-	3.85	25627689
274 (in isoform 3)	Phosphorylation	-	2.06	25627689
355	Phosphorylation	ERFRALGSARFTLGT HHHHHHHCHHHHHHH	19.68	24043423
359	Phosphorylation	ALGSARFTLGTVLGL HHHCHHHHHHHHHHH	20.80	24043423
362	Phosphorylation	SARFTLGTVLGLATL CHHHHHHHHHHHHHH	18.70	24043423
363 (in isoform 3)	Phosphorylation	-	3.66	25159151
368	Phosphorylation	GTVLGLATLHTYRGR HHHHHHHHHHHHCCC	24.90	24043423
368 (in isoform 3)	Phosphorylation	-	24.90	25159151
371	Phosphorylation	LGLATLHTYRGRLSY HHHHHHHHHCCCCCC	20.30	24043423
372	Phosphorylation	GLATLHTYRGRLSYL HHHHHHHHCCCCCCC	10.58	24043423
377	Phosphorylation	HTYRGRLSYLPATVE HHHCCCCCCCCCCCC	24.22	23403867
378	Phosphorylation	TYRGRLSYLPATVEP HHCCCCCCCCCCCCC	22.69	23403867
382	Phosphorylation	RLSYLPATVEPASPT CCCCCCCCCCCCCCC	24.38	30266825
387	Phosphorylation	PATVEPASPTPAHSL CCCCCCCCCCCCHHC	39.77	29255136
389	Phosphorylation	TVEPASPTPAHSLPR CCCCCCCCCCHHCCC	30.52	30266825
393	Phosphorylation	ASPTPAHSLPRAKSE CCCCCCHHCCCCCCC	42.02	30266825
399	Phosphorylation	HSLPRAKSELTLTPD HHCCCCCCCCEECCC	36.53	23401153
402	Phosphorylation	PRAKSELTLTPDPAP CCCCCCCEECCCCCC	25.24	21712546
404	Phosphorylation	AKSELTLTPDPAPPM CCCCCEECCCCCCCC	22.02	25159151
414	Phosphorylation	PAPPMAHSPLHRSVS CCCCCCCCCCCCCHH	21.44	25159151
419	Phosphorylation	AHSPLHRSVSDLPLP CCCCCCCCHHCCCCC	18.41	17635916
421	Phosphorylation	SPLHRSVSDLPLPLP CCCCCCHHCCCCCCC	34.38	17635916
472	Phosphorylation	LSPDPLLSSPPGSPK CCCCCCCCCCCCCCC	48.78	26074081
473	Phosphorylation	SPDPLLSSPPGSPKA CCCCCCCCCCCCCCH	34.77	20363803
477	Phosphorylation	LLSSPPGSPKAALHS CCCCCCCCCCHHHCC	29.06	20363803
484	Phosphorylation	SPKAALHSPVSEGAP CCCHHHCCCCCCCCC	28.04	26055452
487	Phosphorylation	AALHSPVSEGAPVIP HHHCCCCCCCCCCCC	33.43	26055452
496	Phosphorylation	GAPVIPPSSGLPLPT CCCCCCCCCCCCCCC	31.51	26074081
497	Phosphorylation	APVIPPSSGLPLPTP CCCCCCCCCCCCCCC	50.55	26074081
503	Phosphorylation	SSGLPLPTPDARVGA CCCCCCCCCCCCCCC	41.29	26074081
614	Phosphorylation	AFRLEPLTPRGVLTV HHCCCCCCCCEEEEE	22.96	22817900
620	Phosphorylation	LTPRGVLTVDGEQVE CCCCEEEEECCEEEE	17.72	30257219
641	Phosphorylation	QMHPGIGTLLTGPPG EECCCCCCCCCCCCC	19.37	30257219

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
387	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
387	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
387	S	Phosphorylation	Kinase	MAPK	-	Uniprot
419	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
419	S	Phosphorylation	Kinase	PDPK1	Q9Z2A0	GPS
419	S	Phosphorylation	Kinase	PKD	-	Uniprot
421	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
421	S	Phosphorylation	Kinase	PDPK1	Q9Z2A0	GPS
421	S	Phosphorylation	Kinase	PKD	-	Uniprot
614	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
614	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
614	T	Phosphorylation	Kinase	MAPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
387	S	Phosphorylation	17311928
Phosphorylated by MAPK1 and MAPK2 at Ser-387 and Thr-614, phosphorylation is induced by agonists such as EGF and PMA and increases kinase activity.
419	S	Phosphorylation	17635916
Phosphorylated by PKD on Ser-419 and Ser-421 upon PMA treatment.
421	S	Phosphorylation	17635916
Phosphorylated by PKD on Ser-419 and Ser-421 upon PMA treatment.
614	T	Phosphorylation	17311928
Phosphorylated by MAPK1 and MAPK2 at Ser-387 and Thr-614, phosphorylation is induced by agonists such as EGF and PMA and increases kinase activity.

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 SPHK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
H31_HUMAN	HIST1H3A	physical	19729656

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
There are no disease associations of PTM sites.

Regulatory Network of SPHK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-387; THR-404 ANDSER-414, AND MASS SPECTROMETRY.	18691976 [Abstract]

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