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Q9NYA1

- SPHK1_HUMAN

UniProt

Q9NYA1 - SPHK1_HUMAN

Protein

Sphingosine kinase 1

Gene

SPHK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol.2 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication

    Kineticsi

    1. KM=14 µM for sphingosine1 Publication
    2. KM=20 µM for dihydrosphingosine1 Publication
    3. KM=77 µM for ATP1 Publication

    pH dependencei

    Optimum pH is 7.4.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei81 – 811Proton donor/acceptor1 Publication
    Binding sitei86 – 861ATP
    Binding sitei178 – 1781Substrate
    Binding sitei185 – 1851ATP
    Binding sitei191 – 1911ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 243ATP
    Nucleotide bindingi54 – 585ATP
    Nucleotide bindingi111 – 1133ATP
    Nucleotide bindingi341 – 3433ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. D-erythro-sphingosine kinase activity Source: UniProtKB
    4. diacylglycerol kinase activity Source: InterPro
    5. DNA binding Source: MGI
    6. magnesium ion binding Source: UniProtKB
    7. NAD+ kinase activity Source: InterPro
    8. protein binding Source: UniProtKB
    9. protein phosphatase 2A binding Source: BHF-UCL
    10. sphinganine kinase activity Source: MGI

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. blood vessel development Source: Ensembl
    3. brain development Source: Ensembl
    4. calcium-mediated signaling Source: UniProtKB
    5. cellular protein metabolic process Source: Reactome
    6. cellular response to growth factor stimulus Source: Ensembl
    7. cellular response to hydrogen peroxide Source: Ensembl
    8. cellular response to starvation Source: Ensembl
    9. cyclooxygenase pathway Source: Ensembl
    10. female pregnancy Source: Ensembl
    11. inflammatory response Source: Ensembl
    12. intracellular signal transduction Source: UniProtKB
    13. lipid phosphorylation Source: GOC
    14. negative regulation of apoptotic process Source: UniProtKB
    15. positive regulation of angiogenesis Source: UniProtKB
    16. positive regulation of cell growth Source: UniProtKB
    17. positive regulation of cell migration Source: UniProtKB
    18. positive regulation of fibroblast proliferation Source: MGI
    19. positive regulation of mitotic cell cycle Source: UniProtKB
    20. positive regulation of neuron projection development Source: Ensembl
    21. positive regulation of neurotransmitter secretion Source: Ensembl
    22. positive regulation of NF-kappaB import into nucleus Source: UniProtKB
    23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    24. positive regulation of protein phosphorylation Source: Ensembl
    25. positive regulation of protein ubiquitination Source: UniProtKB
    26. positive regulation of smooth muscle contraction Source: UniProtKB
    27. protein folding Source: Reactome
    28. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
    29. regulation of interleukin-1 beta production Source: Ensembl
    30. regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    31. response to amine Source: Ensembl
    32. response to ATP Source: Ensembl
    33. response to interleukin-1 Source: Ensembl
    34. response to magnesium ion Source: Ensembl
    35. response to progesterone Source: Ensembl
    36. signal transduction Source: ProtInc
    37. small molecule metabolic process Source: Reactome
    38. sphingoid catabolic process Source: UniProtKB
    39. sphingolipid biosynthetic process Source: Reactome
    40. sphingolipid metabolic process Source: Reactome
    41. sphingosine metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.91. 2681.
    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
    REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    SABIO-RKQ9NYA1.
    SignaLinkiQ9NYA1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sphingosine kinase 1 (EC:2.7.1.91)
    Short name:
    SK 1
    Short name:
    SPK 1
    Gene namesi
    Name:SPHK1
    Synonyms:SPHK, SPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11240. SPHK1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. synaptic vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi81 – 811D → A: Loss of enzyme activity. 2 Publications
    Mutagenesisi81 – 811D → N: Strongly reduced enzyme activity. 2 Publications
    Mutagenesisi82 – 821G → D: Loss of enzyme activity. 2 Publications
    Mutagenesisi197 – 1971F → A: Abolishes interaction with CIB1; when associated with A-198. 1 Publication
    Mutagenesisi198 – 1981L → A: Abolishes interaction with CIB1; when associated with A-197. 1 Publication

    Organism-specific databases

    PharmGKBiPA36070.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Sphingosine kinase 1PRO_0000181357Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931Phosphothreonine1 Publication
    Modified residuei225 – 2251Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYA1.
    PaxDbiQ9NYA1.
    PRIDEiQ9NYA1.

    PTM databases

    PhosphoSiteiQ9NYA1.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in adult liver, kidney, heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9NYA1.
    BgeeiQ9NYA1.
    CleanExiHS_SPHK1.
    GenevestigatoriQ9NYA1.

    Organism-specific databases

    HPAiHPA022829.
    HPA028761.

    Interactioni

    Subunit structurei

    Interacts with ACY1 By similarity. Binds to calmodulin. Interacts with SPHKAP. Interacts with CIB1, the interaction occurs in a calcium-dependent manner.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTSBP078584EBI-985303,EBI-715062
    EEF1A1P681042EBI-985303,EBI-352162
    FHL2Q141927EBI-985303,EBI-701903
    SPHKAPQ2M3C74EBI-985303,EBI-1803914
    TRAF6Q9Y4K32EBI-985303,EBI-359276

    Protein-protein interaction databases

    BioGridi114396. 8 interactions.
    IntActiQ9NYA1. 7 interactions.
    MINTiMINT-226199.
    STRINGi9606.ENSP00000313681.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 219
    Helixi25 – 284
    Helixi30 – 378
    Helixi39 – 446
    Beta strandi47 – 537
    Helixi59 – 668
    Helixi69 – 713
    Beta strandi73 – 797
    Helixi81 – 9313
    Helixi97 – 1004
    Beta strandi105 – 1095
    Helixi115 – 1239
    Helixi131 – 14414
    Beta strandi146 – 15712
    Beta strandi162 – 17211
    Helixi173 – 18210
    Helixi183 – 1908
    Helixi191 – 20111
    Beta strandi206 – 2149
    Helixi215 – 2173
    Beta strandi230 – 2323
    Beta strandi249 – 2513
    Beta strandi256 – 26611
    Beta strandi285 – 2917
    Helixi296 – 30611
    Turni307 – 3093
    Helixi311 – 3144
    Beta strandi319 – 33416
    Beta strandi336 – 3405
    Beta strandi343 – 3486
    Beta strandi350 – 36213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VZBX-ray2.00A/B/C9-364[»]
    3VZCX-ray2.30A/B/C/D/E/F9-364[»]
    3VZDX-ray2.30A/B/C/D/E/F9-364[»]
    4L02X-ray2.75A/B/C9-364[»]
    ProteinModelPortaliQ9NYA1.
    SMRiQ9NYA1. Positions 9-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 159148DAGKcPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 824Substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi147 – 1559Nuclear export signal 1
    Motifi161 – 1699Nuclear export signal 2

    Sequence similaritiesi

    Contains 1 DAGKc domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1597.
    HOVERGENiHBG054796.
    InParanoidiQ9NYA1.
    KOiK04718.
    OMAiDCPYLVY.
    PhylomeDBiQ9NYA1.
    TreeFamiTF354296.

    Family and domain databases

    InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NYA1-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDPAGGPRGV LPRPCRVLVL LNPRGGKGKA LQLFRSHVQP LLAEAEISFT    50
    LMLTERRNHA RELVRSEELG RWDALVVMSG DGLMHEVVNG LMERPDWETA 100
    IQKPLCSLPA GSGNALAASL NHYAGYEQVT NEDLLTNCTL LLCRRLLSPM 150
    NLLSLHTASG LRLFSVLSLA WGFIADVDLE SEKYRRLGEM RFTLGTFLRL 200
    AALRTYRGRL AYLPVGRVGS KTPASPVVVQ QGPVDAHLVP LEEPVPSHWT 250
    VVPDEDFVLV LALLHSHLGS EMFAAPMGRC AAGVMHLFYV RAGVSRAMLL 300
    RLFLAMEKGR HMEYECPYLV YVPVVAFRLE PKDGKGVFAV DGELMVSEAV 350
    QGQVHPNYFW MVSGCVEPPP SWKPQQMPPP EEPL 384
    Length:384
    Mass (Da):42,518
    Last modified:October 1, 2000 - v1
    Checksum:iEB04A7F2034C2DB0
    GO
    Isoform 2 (identifier: Q9NYA1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSAQVLGFLR...WQREPRVEVM

    Show »
    Length:470
    Mass (Da):51,054
    Checksum:iF6BF2D324E12CFC0
    GO
    Isoform 3 (identifier: Q9NYA1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3-3: P → PVVGCGRGLFGFVFS

    Show »
    Length:398
    Mass (Da):43,944
    Checksum:i7F2C9B26C030E560
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61Missing in CAB92131. 1 PublicationCurated
    Sequence conflicti11 – 155LPRPC → ARL in CAB92131. 1 PublicationCurated
    Sequence conflicti114 – 1152NA → KP in CAB92131. 1 PublicationCurated
    Sequence conflicti251 – 2511V → M in AAF73423. (PubMed:10802064)Curated
    Sequence conflicti260 – 2601V → I in AAF73423. (PubMed:10802064)Curated
    Sequence conflicti302 – 3021L → F in AAF73423. (PubMed:10802064)Curated
    Sequence conflicti325 – 3251V → G in CAB92131. 1 PublicationCurated
    Sequence conflicti337 – 3371V → M in AAG01980. (PubMed:10947957)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q9NYA1-2)
    Natural varianti34 – 341A → T.
    Corresponds to variant rs346803 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSAQVLGFLRSWTPLPLAAP RGPAAAGNDAGAPAATAPGG EGEPHSRPCDARLGSTDKEL KAGAAATGSAPTAPGTPWQR EPRVEVM in isoform 2. 2 PublicationsVSP_035453
    Alternative sequencei3 – 31P → PVVGCGRGLFGFVFS in isoform 3. 1 PublicationVSP_047078

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF266756 mRNA. Translation: AAF73470.1.
    AF238083 mRNA. Translation: AAF73423.1.
    AF200328 mRNA. Translation: AAG01980.1.
    AK023393 mRNA. Translation: BAB14558.1.
    AK292294 mRNA. Translation: BAF84983.1.
    AK022402 mRNA. Translation: BAB14028.1.
    AJ245504 mRNA. Translation: CAB92131.1.
    AC090699 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89392.1.
    CH471099 Genomic DNA. Translation: EAW89393.1.
    BC009419 mRNA. Translation: AAH09419.1.
    BC014439 mRNA. Translation: AAH14439.1.
    BC030553 mRNA. Translation: AAH30553.1.
    CCDSiCCDS11744.1. [Q9NYA1-2]
    CCDS45785.1. [Q9NYA1-1]
    CCDS59297.1. [Q9NYA1-3]
    RefSeqiNP_001136073.1. NM_001142601.1. [Q9NYA1-1]
    NP_001136074.1. NM_001142602.1. [Q9NYA1-1]
    NP_068807.2. NM_021972.3. [Q9NYA1-3]
    NP_892010.2. NM_182965.2. [Q9NYA1-2]
    XP_005257823.1. XM_005257766.1. [Q9NYA1-1]
    UniGeneiHs.68061.

    Genome annotation databases

    EnsembliENST00000323374; ENSP00000313681; ENSG00000176170. [Q9NYA1-2]
    ENST00000392496; ENSP00000376285; ENSG00000176170. [Q9NYA1-1]
    ENST00000545180; ENSP00000440970; ENSG00000176170. [Q9NYA1-1]
    ENST00000590959; ENSP00000468547; ENSG00000176170. [Q9NYA1-3]
    ENST00000592299; ENSP00000465726; ENSG00000176170. [Q9NYA1-1]
    GeneIDi8877.
    KEGGihsa:8877.
    UCSCiuc002jrf.1. human. [Q9NYA1-1]
    uc002jrh.2. human.
    uc002jrj.2. human. [Q9NYA1-2]

    Polymorphism databases

    DMDMi17369329.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF266756 mRNA. Translation: AAF73470.1 .
    AF238083 mRNA. Translation: AAF73423.1 .
    AF200328 mRNA. Translation: AAG01980.1 .
    AK023393 mRNA. Translation: BAB14558.1 .
    AK292294 mRNA. Translation: BAF84983.1 .
    AK022402 mRNA. Translation: BAB14028.1 .
    AJ245504 mRNA. Translation: CAB92131.1 .
    AC090699 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89392.1 .
    CH471099 Genomic DNA. Translation: EAW89393.1 .
    BC009419 mRNA. Translation: AAH09419.1 .
    BC014439 mRNA. Translation: AAH14439.1 .
    BC030553 mRNA. Translation: AAH30553.1 .
    CCDSi CCDS11744.1. [Q9NYA1-2 ]
    CCDS45785.1. [Q9NYA1-1 ]
    CCDS59297.1. [Q9NYA1-3 ]
    RefSeqi NP_001136073.1. NM_001142601.1. [Q9NYA1-1 ]
    NP_001136074.1. NM_001142602.1. [Q9NYA1-1 ]
    NP_068807.2. NM_021972.3. [Q9NYA1-3 ]
    NP_892010.2. NM_182965.2. [Q9NYA1-2 ]
    XP_005257823.1. XM_005257766.1. [Q9NYA1-1 ]
    UniGenei Hs.68061.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VZB X-ray 2.00 A/B/C 9-364 [» ]
    3VZC X-ray 2.30 A/B/C/D/E/F 9-364 [» ]
    3VZD X-ray 2.30 A/B/C/D/E/F 9-364 [» ]
    4L02 X-ray 2.75 A/B/C 9-364 [» ]
    ProteinModelPortali Q9NYA1.
    SMRi Q9NYA1. Positions 9-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114396. 8 interactions.
    IntActi Q9NYA1. 7 interactions.
    MINTi MINT-226199.
    STRINGi 9606.ENSP00000313681.

    Chemistry

    BindingDBi Q9NYA1.
    ChEMBLi CHEMBL4394.
    GuidetoPHARMACOLOGYi 2204.

    PTM databases

    PhosphoSitei Q9NYA1.

    Polymorphism databases

    DMDMi 17369329.

    Proteomic databases

    MaxQBi Q9NYA1.
    PaxDbi Q9NYA1.
    PRIDEi Q9NYA1.

    Protocols and materials databases

    DNASUi 8877.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323374 ; ENSP00000313681 ; ENSG00000176170 . [Q9NYA1-2 ]
    ENST00000392496 ; ENSP00000376285 ; ENSG00000176170 . [Q9NYA1-1 ]
    ENST00000545180 ; ENSP00000440970 ; ENSG00000176170 . [Q9NYA1-1 ]
    ENST00000590959 ; ENSP00000468547 ; ENSG00000176170 . [Q9NYA1-3 ]
    ENST00000592299 ; ENSP00000465726 ; ENSG00000176170 . [Q9NYA1-1 ]
    GeneIDi 8877.
    KEGGi hsa:8877.
    UCSCi uc002jrf.1. human. [Q9NYA1-1 ]
    uc002jrh.2. human.
    uc002jrj.2. human. [Q9NYA1-2 ]

    Organism-specific databases

    CTDi 8877.
    GeneCardsi GC17P074380.
    HGNCi HGNC:11240. SPHK1.
    HPAi HPA022829.
    HPA028761.
    MIMi 603730. gene.
    neXtProti NX_Q9NYA1.
    PharmGKBi PA36070.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1597.
    HOVERGENi HBG054796.
    InParanoidi Q9NYA1.
    KOi K04718.
    OMAi DCPYLVY.
    PhylomeDBi Q9NYA1.
    TreeFami TF354296.

    Enzyme and pathway databases

    BRENDAi 2.7.1.91. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
    REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    SABIO-RK Q9NYA1.
    SignaLinki Q9NYA1.

    Miscellaneous databases

    GeneWikii Sphingosine_kinase_1.
    GenomeRNAii 8877.
    NextBioi 33329.
    PROi Q9NYA1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYA1.
    Bgeei Q9NYA1.
    CleanExi HS_SPHK1.
    Genevestigatori Q9NYA1.

    Family and domain databases

    InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00781. DAGK_cat. 1 hit.
    [Graphical view ]
    SMARTi SM00046. DAGKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 2 hits.
    PROSITEi PS50146. DAGK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution."
      Melendez A.J., Carlos-Dias E., Gosink M., Allen J.M., Takacs L.
      Gene 251:19-26(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY.
    3. "Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes."
      Pitson S.M., D'Andrea R.J., Vandeleur L., Moretti P.A.B., Xia P., Gamble J.R., Vadas M.A., Wattenberg B.W.
      Biochem. J. 350:429-441(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    4. Van Veldhoven P.P., Gijsbers S.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Mammary gland, Ovary and Testis.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 2 AND 3).
      Tissue: Blood, Kidney and Skin.
    9. "Cloning and characterization of a protein kinase A anchoring protein (AKAP)-related protein that interacts with and regulates sphingosine kinase 1 activity."
      Lacana E., Maceyka M., Milstien S., Spiegel S.
      J. Biol. Chem. 277:32947-32953(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPHKAP.
    10. "Identification of functional nuclear export sequences in human sphingosine kinase 1."
      Inagaki Y., Li P.Y., Wada A., Mitsutake S., Igarashi Y.
      Biochem. Biophys. Res. Commun. 311:168-173(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Translocation of sphingosine kinase 1 to the plasma membrane is mediated by calcium- and integrin-binding protein 1."
      Jarman K.E., Moretti P.A., Zebol J.R., Pitson S.M.
      J. Biol. Chem. 285:483-492(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIB1, SUBCELLULAR LOCATION, MUTAGENESIS OF 197-PHE-LEU-198.
    13. "Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF GLY-82, PHOSPHORYLATION AT SER-225.
    14. "Molecular basis of sphingosine kinase 1 substrate recognition and catalysis."
      Wang Z., Min X., Xiao S.H., Johnstone S., Romanow W., Meininger D., Xu H., Liu J., Dai J., An S., Thibault S., Walker N.
      Structure 21:798-809(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-364 IN COMPLEXES WITH SUBSTRATE ANALOGS AND ADP, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF ASP-81.

    Entry informationi

    Entry nameiSPHK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYA1
    Secondary accession number(s): Q8N632
    , Q96GK1, Q9HD92, Q9NY70, Q9NYL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3