Reviewed, UniProtKB/Swiss-Prot Q8CI15 (SPHK1_MOUSE)

Names and origin

Protein names

Recommended name:
    Sphingosine kinase 1
      Short name=SPK 1
      Short name=SK 1
    EC=2.7.1.91

Gene names

Name:

Sphk1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	ATP + sphinganine = ADP + sphinganine 1-phosphate. ATP + sphingosine = ADP + sphingosine 1-phosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Binds to calmodulin. Interacts with SPHKAP By similarity. Interacts with ACY1.
Sequence similarities	Contains 1 DAGKc domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: InterPro blood vessel development Inferred from genetic interaction. Source: MGI brain development Inferred from genetic interaction. Source: MGI inflammatory response Inferred from mutant phenotype. Source: MGI positive regulation of cell proliferation Inferred from genetic interaction. Source: MGI regulation of interleukin-1 beta production Inferred from mutant phenotype. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW D-erythro-sphingosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol kinase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB sphinganine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fhl2	O70433	1	EBI-985291,EBI-299379
FYN	P06241	1	EBI-985291,EBI-515315	From a different organism.
LYN	P07948	1	EBI-985291,EBI-79452	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8CI15-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8CI15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MEP → MWWCCVLFV

Isoform 3 (identifier: Q8CI15-3)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Sphingosine kinase 1		PRO_0000333032
Regions
	Domain	16 – 153	138	DAGKc
Amino acid modifications
	Modified residue	193	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	1 – 3	3	MEP → MWWCCVLFV in isoform 2.		VSP_033448
	Alternative sequence	4	1	Missing in isoform 3.		VSP_033449
Experimental info
	Sequence conflict	146	1	R → H in BAE33198. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B791FAA58FCE3D29	FASTA	382	42,443
	10 20 30 40 50 60 MEPVECPRGL LPRPCRVLVL LNPQGGKGKA LQLFQSRVQP FLEEAEITFK LILTERKNHA 70 80 90 100 110 120 RELVCAEELG HWDALAVMSG DGLMHEVVNG LMERPDWETA IQKPLCSLPG GSGNALAASV 130 140 150 160 170 180 NHYAGYEQVT NEDLLINCTL LLCRRRLSPM NLLSLHTASG LRLYSVLSLS WGFVADVDLE 190 200 210 220 230 240 SEKYRRLGEI RFTVGTFFRL ASLRIYQGQL AYLPVGTVAS KRPASTLVQK GPVDTHLVPL 250 260 270 280 290 300 EEPVPSHWTV VPEQDFVLVL VLLHTHLSSE LFAAPMGRCE AGVMHLFYVR AGVSRAALLR 310 320 330 340 350 360 LFLAMQKGKH MELDCPYLVH VPVVAFRLEP RSQRGVFSVD GELMVCEAVQ GQVHPNYLWM 370 380 VCGSRDAPSG RDSRRGPPPE EP
	Isoform 2. Checksum: 01EB032322542CAD	FASTA	388	43,254
	10 20 30 40 50 60 MWWCCVLFVV ECPRGLLPRP CRVLVLLNPQ GGKGKALQLF QSRVQPFLEE AEITFKLILT 70 80 90 100 110 120 ERKNHARELV CAEELGHWDA LAVMSGDGLM HEVVNGLMER PDWETAIQKP LCSLPGGSGN 130 140 150 160 170 180 ALAASVNHYA GYEQVTNEDL LINCTLLLCR RRLSPMNLLS LHTASGLRLY SVLSLSWGFV 190 200 210 220 230 240 ADVDLESEKY RRLGEIRFTV GTFFRLASLR IYQGQLAYLP VGTVASKRPA STLVQKGPVD 250 260 270 280 290 300 THLVPLEEPV PSHWTVVPEQ DFVLVLVLLH THLSSELFAA PMGRCEAGVM HLFYVRAGVS 310 320 330 340 350 360 RAALLRLFLA MQKGKHMELD CPYLVHVPVV AFRLEPRSQR GVFSVDGELM VCEAVQGQVH 370 380 PNYLWMVCGS RDAPSGRDSR RGPPPEEP
	Isoform 3. Checksum: 2F2C1F10D59EB129	FASTA	381	42,344
	10 20 30 40 50 60 MEPECPRGLL PRPCRVLVLL NPQGGKGKAL QLFQSRVQPF LEEAEITFKL ILTERKNHAR 70 80 90 100 110 120 ELVCAEELGH WDALAVMSGD GLMHEVVNGL MERPDWETAI QKPLCSLPGG SGNALAASVN 130 140 150 160 170 180 HYAGYEQVTN EDLLINCTLL LCRRRLSPMN LLSLHTASGL RLYSVLSLSW GFVADVDLES 190 200 210 220 230 240 EKYRRLGEIR FTVGTFFRLA SLRIYQGQLA YLPVGTVASK RPASTLVQKG PVDTHLVPLE 250 260 270 280 290 300 EPVPSHWTVV PEQDFVLVLV LLHTHLSSEL FAAPMGRCEA GVMHLFYVRA GVSRAALLRL 310 320 330 340 350 360 FLAMQKGKHM ELDCPYLVHV PVVAFRLEPR SQRGVFSVDG ELMVCEAVQG QVHPNYLWMV 370 380 CGSRDAPSGR DSRRGPPPEE P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional characterization of murine sphingosine kinase." Kohama T., Olivera A., Edsall L., Nagiec M.M., Dickson R., Spiegel S. J. Biol. Chem. 273:23722-23728(1998) [PubMed: 9726979] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	Thompson D., Pyne S. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Placenta.
[4]	The mouse genome sequencing consortium Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Kidney.
[6]	"Aminoacylase 1 is a sphingosine kinase 1-interacting protein." Maceyka M., Nava V.E., Milstien S., Spiegel S. FEBS Lett. 568:30-34(2004) [PubMed: 15196915] [Abstract] Cited for: INTERACTION WITH ACY1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF068749 mRNA. Translation: AAC61698.1. AF415213 mRNA. Translation: AAL07499.1. AK155332 mRNA. Translation: BAE33198.1. AK160900 mRNA. Translation: BAE36079.1. AL645851 Genomic DNA. Translation: CAM17116.1. AL645851 Genomic DNA. Translation: CAM17117.1. BC037710 mRNA. Translation: AAH37710.1.
IPI	IPI00407664. IPI00649112. IPI00762556.
RefSeq	NP_079643.2.
UniGene	Mm.20944
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CI15. 3 interactions.
PTM databases
PhosphoSite	Q8CI15.
Proteomic databases
PRIDE	Q8CI15.
Genome annotation databases
Ensembl	ENSMUSG00000061878. Mus musculus. [Contig view]
GeneID	20698.
Organism-specific databases
MGI	MGI:1316649. Sphk1.
Phylogenomic databases
HOVERGEN	Q8CI15.
OMA	Q8CI15. AIQKPLC.
Gene expression databases
Bgee	Q8CI15.
Family and domain databases
InterPro	IPR001206. Diacylglycerol_kinase_cat. [Graphical view]
Pfam	PF00781. DAGK_cat. 1 hit. [Graphical view]
ProDom	PD005043. DAGKc. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00046. DAGKc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	299241.
SOURCE	Search...

Entry information

Entry name

SPHK1_MOUSE

Accession

Primary (citable) accession number: Q8CI15
Secondary accession number(s): O88886, Q3U2E3, Q91ZN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 1, 2003
Last modified:	May 5, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)