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Q8CI15 (SPHK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingosine kinase 1

Short name=SK 1
Short name=SPK 1
EC=2.7.1.91
Gene names
Name:Sphk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with CIB1, the interaction occurs in a calcium-dependent manner By similarity. Interacts with ACY1. Ref.6

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. Note: Translocated from the cytoplasm to the plasma membrane in a CIB1-dependent manner By similarity.

Miscellaneous

Sphingosine 1-phosphate stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling By similarity.

Sequence similarities

Contains 1 DAGKc domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel development

Inferred from genetic interaction PubMed 16314531. Source: MGI

brain development

Inferred from genetic interaction PubMed 16314531. Source: MGI

calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to starvation

Inferred from electronic annotation. Source: Ensembl

cyclooxygenase pathway

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from mutant phenotype PubMed 18305483. Source: MGI

lipid phosphorylation

Inferred from sequence alignment PubMed 12393916. Source: GOC

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 16314531. Source: MGI

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

regulation of interleukin-1 beta production

Inferred from mutant phenotype PubMed 18305483. Source: MGI

regulation of tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

response to ATP

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to magnesium ion

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

sphingosine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

D-erythro-sphingosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from sequence alignment PubMed 12393916. Source: MGI

NAD+ kinase activity

Inferred from electronic annotation. Source: InterPro

calmodulin binding

Inferred from sequence alignment PubMed 12393916. Source: MGI

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 sequence alignment PubMed 12393916. Source: MGI

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Sphingosine kinase 1
PRO_0000333032

Regions

Domain12 – 159148DAGKc
Nucleotide binding22 – 243ATP By similarity
Nucleotide binding54 – 585ATP By similarity
Nucleotide binding111 – 1133ATP By similarity
Nucleotide binding340 – 3423ATP By similarity
Region79 – 824Substrate binding By similarity
Motif147 – 1559Nuclear export signal 1 By similarity
Motif161 – 1699Nuclear export signal 2 By similarity

Sites

Active site811Proton donor/acceptor By similarity
Binding site861ATP By similarity
Binding site1781Substrate By similarity
Binding site1851ATP By similarity
Binding site1911ATP By similarity

Amino acid modifications

Modified residue1931Phosphothreonine By similarity
Modified residue2251Phosphoserine By similarity

Natural variations

Alternative sequence1 – 33MEP → MWWCCVLFV in isoform 2.
VSP_033448
Alternative sequence41Missing in isoform 3.
VSP_033449

Experimental info

Sequence conflict1461R → H in BAE33198. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B791FAA58FCE3D29

FASTA38242,443
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 01EB032322542CAD
Show »

FASTA38843,254
Isoform 3 [UniParc].

Checksum: 2F2C1F10D59EB129
Show »

FASTA38142,344

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Placenta.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACY1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001165943.1. NM_001172472.1.
NP_001165944.1. NM_001172473.1.
NP_001165946.1. NM_001172475.1.
NP_035581.1. NM_011451.3.
NP_079643.2. NM_025367.6.
XP_006532733.1. XM_006532670.1.
XP_006532734.1. XM_006532671.1.
XP_006532735.1. XM_006532672.1.
XP_006532736.1. XM_006532673.1.
UniGeneMm.20944.

3D structure databases

ProteinModelPortalQ8CI15.
SMRQ8CI15. Positions 9-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CI15. 3 interactions.

PTM databases

PhosphoSiteQ8CI15.

Proteomic databases

PaxDbQ8CI15.
PRIDEQ8CI15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063396; ENSMUSP00000064743; ENSMUSG00000061878. [Q8CI15-1]
ENSMUST00000063446; ENSMUSP00000067865; ENSMUSG00000061878. [Q8CI15-1]
ENSMUST00000100201; ENSMUSP00000097775; ENSMUSG00000061878. [Q8CI15-3]
ENSMUST00000106386; ENSMUSP00000101994; ENSMUSG00000061878. [Q8CI15-1]
ENSMUST00000106387; ENSMUSP00000101995; ENSMUSG00000061878. [Q8CI15-1]
ENSMUST00000106388; ENSMUSP00000101996; ENSMUSG00000061878. [Q8CI15-1]
ENSMUST00000141798; ENSMUSP00000131010; ENSMUSG00000061878. [Q8CI15-2]
GeneID20698.
KEGGmmu:20698.
UCSCuc007mlg.2. mouse. [Q8CI15-3]
uc007mlh.2. mouse. [Q8CI15-1]
uc007mll.2. mouse. [Q8CI15-2]

Organism-specific databases

CTD8877.
MGIMGI:1316649. Sphk1.

Phylogenomic databases

eggNOGCOG1597.
GeneTreeENSGT00690000101761.
HOGENOMHOG000111460.
HOVERGENHBG054796.
KOK04718.
OMASVNHYAG.
OrthoDBEOG7PCJGK.
PhylomeDBQ8CI15.
TreeFamTF354296.

Gene expression databases

ArrayExpressQ8CI15.
BgeeQ8CI15.
GenevestigatorQ8CI15.

Family and domain databases

InterProIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR001206. Diacylglycerol_kinase_cat_dom.
[Graphical view]
PfamPF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTSM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 2 hits.
PROSITEPS50146. DAGK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299241.
PROQ8CI15.
SOURCESearch...

Entry information

Entry nameSPHK1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot