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Protein

Sphingosine kinase 2

Gene

Sphk2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

ATP + sphinganine = ADP + sphinganine 1-phosphate.
ATP + sphingosine = ADP + sphingosine 1-phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei212 – 2121Proton donor/acceptorBy similarity
Binding sitei217 – 2171ATPPROSITE-ProRule annotation
Binding sitei309 – 3091SubstrateBy similarity
Binding sitei316 – 3161ATPPROSITE-ProRule annotation
Binding sitei322 – 3221ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi153 – 1553ATPPROSITE-ProRule annotation
Nucleotide bindingi185 – 1895ATPPROSITE-ProRule annotation
Nucleotide bindingi242 – 2443ATPPROSITE-ProRule annotation
Nucleotide bindingi586 – 5883ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • D-erythro-sphingosine kinase activity Source: MGI
  • sphinganine kinase activity Source: UniProtKB
  • sphingosine-1-phosphate receptor activity Source: MGI

GO - Biological processi

  • blood vessel development Source: MGI
  • brain development Source: MGI
  • cell proliferation Source: UniProtKB
  • female pregnancy Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • positive regulation of cell proliferation Source: MGI
  • sphinganine-1-phosphate biosynthetic process Source: UniProtKB
  • sphingosine-1-phosphate signaling pathway Source: MGI
  • sphingosine biosynthetic process Source: MGI
  • sphingosine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.91. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Chemistry

SwissLipidsiSLP:000000113.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine kinase 2 (EC:2.7.1.91)
Short name:
SK 2
Short name:
SPK 2
Gene namesi
Name:Sphk2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1861380. Sphk2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • lysosomal membrane Source: MGI
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Sphingosine kinase 2PRO_0000181359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei364 – 3641PhosphoserineCombined sources
Modified residuei377 – 3771PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JIA7.
MaxQBiQ9JIA7.
PaxDbiQ9JIA7.
PRIDEiQ9JIA7.

PTM databases

iPTMnetiQ9JIA7.
PhosphoSiteiQ9JIA7.

Expressioni

Gene expression databases

BgeeiQ9JIA7.
CleanExiMM_SPHK2.
ExpressionAtlasiQ9JIA7. baseline and differential.
GenevisibleiQ9JIA7. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
FynP396882EBI-985434,EBI-524514

Protein-protein interaction databases

IntActiQ9JIA7. 6 interactions.
MINTiMINT-4135335.
STRINGi10090.ENSMUSP00000072615.

Chemistry

BindingDBiQ9JIA7.

Structurei

3D structure databases

ProteinModelPortaliQ9JIA7.
SMRiQ9JIA7. Positions 141-360, 472-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 290148DAGKcPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 140140Required for binding to sulfatide and phosphoinositides and for membrane localizationBy similarityAdd
BLAST
Regioni210 – 2134Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 DAGKc domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1116. Eukaryota.
COG1597. LUCA.
GeneTreeiENSGT00690000101761.
HOGENOMiHOG000111460.
HOVERGENiHBG054796.
InParanoidiQ9JIA7.
KOiK04718.
OMAiPTHGLPR.
OrthoDBiEOG7PCJGK.
PhylomeDBiQ9JIA7.
TreeFamiTF354296.

Family and domain databases

InterProiIPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
[Graphical view]
PfamiPF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JIA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPPLLPVA ASTPILHGEF GSYPANGPRF ALTLTTQALH IQRLRPKPEA
60 70 80 90 100
RPRDGLVSLD EVSGCGTLQS RSPEDTAAYF CIYTYPRGRR GGRRRATRTF
110 120 130 140 150
RADGATTYEE NRAEAQRWAT ALTCLLRGVP LSGDQEITPE LLPRKPRLLI
160 170 180 190 200
LVNPFGGRGL AWQRCMDHVV PMISEAGLSF NLIQTERQNH ARELVQGLSL
210 220 230 240 250
SEWEGIVTVS GDGLLYEVLN GLLDRPDWED AVRMPIGVLP CGSGNALAGA
260 270 280 290 300
VNHHGGFEQV VGVDLLLNCS LLLCRGGSHP LDLLSVTLAS GSRCFSFLSV
310 320 330 340 350
AWGFLSDVDI HSERFRALGS ARFTLGAVLG LASLHTYRGR LSYLPATTEP
360 370 380 390 400
ALPIPGHSLP RAKSELVLAP APAPAATHSP LHRSVSDLPL PLPQPALVSP
410 420 430 440 450
GSPEPLPDLS LNGGGPELTG DWGGAGDAPL SPDPLLPSSP NALKTAQLSP
460 470 480 490 500
IAEGPPEMPA SSGFLPPTHS APEASTWGPV DHLLPPLGSP LPQDWVTIEG
510 520 530 540 550
EFVLMLGILP SHLCADLMAA PHARFDDGVV HLCWVRSGIS RAALLRILLA
560 570 580 590 600
MEHGNHFSLG CPHLGYAAAR AFRLEPLTPR GLLTVDGELV EYGPIQAQVH
610
PGLATLLTGP AGQKPQA
Length:617
Mass (Da):65,618
Last modified:March 27, 2002 - v2
Checksum:i40EE2C2C288BE26A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521N → S in AAF74125 (PubMed:10751414).Curated
Sequence conflicti510 – 5101P → T in AAF74125 (PubMed:10751414).Curated
Sequence conflicti548 – 5481L → F in AAF74125 (PubMed:10751414).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF245448 mRNA. Translation: AAF74125.1.
AF415214 mRNA. Translation: AAL07500.1.
AK004951 mRNA. Translation: BAB23694.1.
BC006941 mRNA. Translation: AAH06941.1.
BC053737 mRNA. Translation: AAH53737.1.
CCDSiCCDS21261.1.
RefSeqiNP_001166032.1. NM_001172561.1.
NP_064395.2. NM_020011.5.
NP_975009.1. NM_203280.3.
XP_006541075.1. XM_006541012.2.
XP_006541076.1. XM_006541013.2.
UniGeneiMm.24222.
Mm.378235.

Genome annotation databases

EnsembliENSMUST00000072836; ENSMUSP00000072615; ENSMUSG00000057342.
ENSMUST00000107737; ENSMUSP00000103366; ENSMUSG00000057342.
GeneIDi56632.
KEGGimmu:56632.
UCSCiuc009gwt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF245448 mRNA. Translation: AAF74125.1.
AF415214 mRNA. Translation: AAL07500.1.
AK004951 mRNA. Translation: BAB23694.1.
BC006941 mRNA. Translation: AAH06941.1.
BC053737 mRNA. Translation: AAH53737.1.
CCDSiCCDS21261.1.
RefSeqiNP_001166032.1. NM_001172561.1.
NP_064395.2. NM_020011.5.
NP_975009.1. NM_203280.3.
XP_006541075.1. XM_006541012.2.
XP_006541076.1. XM_006541013.2.
UniGeneiMm.24222.
Mm.378235.

3D structure databases

ProteinModelPortaliQ9JIA7.
SMRiQ9JIA7. Positions 141-360, 472-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JIA7. 6 interactions.
MINTiMINT-4135335.
STRINGi10090.ENSMUSP00000072615.

Chemistry

BindingDBiQ9JIA7.
ChEMBLiCHEMBL1075305.
SwissLipidsiSLP:000000113.

PTM databases

iPTMnetiQ9JIA7.
PhosphoSiteiQ9JIA7.

Proteomic databases

EPDiQ9JIA7.
MaxQBiQ9JIA7.
PaxDbiQ9JIA7.
PRIDEiQ9JIA7.

Protocols and materials databases

DNASUi56632.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072836; ENSMUSP00000072615; ENSMUSG00000057342.
ENSMUST00000107737; ENSMUSP00000103366; ENSMUSG00000057342.
GeneIDi56632.
KEGGimmu:56632.
UCSCiuc009gwt.2. mouse.

Organism-specific databases

CTDi56848.
MGIiMGI:1861380. Sphk2.

Phylogenomic databases

eggNOGiKOG1116. Eukaryota.
COG1597. LUCA.
GeneTreeiENSGT00690000101761.
HOGENOMiHOG000111460.
HOVERGENiHBG054796.
InParanoidiQ9JIA7.
KOiK04718.
OMAiPTHGLPR.
OrthoDBiEOG7PCJGK.
PhylomeDBiQ9JIA7.
TreeFamiTF354296.

Enzyme and pathway databases

BRENDAi2.7.1.91. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiSphk2. mouse.
PROiQ9JIA7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIA7.
CleanExiMM_SPHK2.
ExpressionAtlasiQ9JIA7. baseline and differential.
GenevisibleiQ9JIA7. MM.

Family and domain databases

InterProiIPR001206. Diacylglycerol_kinase_cat_dom.
IPR016064. NAD/diacylglycerol_kinase.
[Graphical view]
PfamiPF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform."
    Liu H., Sugiura M., Nava V.E., Edsall L.C., Kono K., Poulton S., Milstien S., Kohama T., Spiegel S.
    J. Biol. Chem. 275:19513-19520(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: ICR.
    Tissue: Brain.
  2. Thompson D., Pyne S.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. "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].
    Tissue: Limb and Mammary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-364 AND THR-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiSPHK2_MOUSE
AccessioniPrimary (citable) accession number: Q9JIA7
Secondary accession number(s): Q91VA9, Q9DBH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: March 27, 2002
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.