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Q9NRA0

- SPHK2_HUMAN

UniProt

Q9NRA0 - SPHK2_HUMAN

Protein

Sphingosine kinase 2

Gene

SPHK2

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 2 (26 Jul 2002)
      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-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides.1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Inhibited by sulfatide.1 Publication

    Kineticsi

    1. KM=3.4 µM for sphingosine1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei247 – 2471Proton donor/acceptorBy similarity
    Binding sitei252 – 2521ATPPROSITE-ProRule annotation
    Binding sitei344 – 3441SubstrateBy similarity
    Binding sitei351 – 3511ATPPROSITE-ProRule annotation
    Binding sitei357 – 3571ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1903ATPPROSITE-ProRule annotation
    Nucleotide bindingi220 – 2245ATPPROSITE-ProRule annotation
    Nucleotide bindingi277 – 2793ATPPROSITE-ProRule annotation
    Nucleotide bindingi622 – 6243ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. D-erythro-sphingosine kinase activity Source: Ensembl
    3. diacylglycerol kinase activity Source: InterPro
    4. NAD+ kinase activity Source: InterPro
    5. protein binding Source: UniProtKB
    6. Ras GTPase binding Source: UniProtKB
    7. sphinganine kinase activity Source: UniProtKB

    GO - Biological processi

    1. blood vessel development Source: Ensembl
    2. brain development Source: Ensembl
    3. cell proliferation Source: UniProtKB
    4. lipid phosphorylation Source: GOC
    5. negative regulation of apoptotic process Source: UniProtKB
    6. positive regulation of cell proliferation Source: Ensembl
    7. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
    8. small molecule metabolic process Source: Reactome
    9. sphinganine-1-phosphate biosynthetic process Source: UniProtKB
    10. sphingolipid biosynthetic process Source: Reactome
    11. sphingolipid metabolic process Source: Reactome
    12. sphingosine metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.91. 2681.
    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:18859. SPHK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. lysosomal membrane Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Lysosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38719.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 654654Sphingosine kinase 2PRO_0000181358Add
    BLAST

    Proteomic databases

    MaxQBiQ9NRA0.
    PaxDbiQ9NRA0.
    PRIDEiQ9NRA0.

    PTM databases

    PhosphoSiteiQ9NRA0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NRA0.
    BgeeiQ9NRA0.
    GenevestigatoriQ9NRA0.

    Interactioni

    Protein-protein interaction databases

    BioGridi121208. 2 interactions.
    IntActiQ9NRA0. 5 interactions.
    STRINGi9606.ENSP00000245222.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRA0.
    SMRiQ9NRA0. Positions 176-406, 514-637.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 325148DAGKcPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 175175Required for binding to sulfatide and phosphoinositides and for membrane localizationAdd
    BLAST
    Regioni245 – 2484Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 DAGKc domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1597.
    HOGENOMiHOG000111460.
    HOVERGENiHBG054796.
    InParanoidiQ9NRA0.
    KOiK04718.
    OrthoDBiEOG7PCJGK.
    PhylomeDBiQ9NRA0.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9NRA0-1) [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

    MNGHLEAEEQ QDQRPDQELT GSWGHGPRST LVRAKAMAPP PPPLAASTPL    50
    LHGEFGSYPA RGPRFALTLT SQALHIQRLR PKPEARPRGG LVPLAEVSGC 100
    CTLRSRSPSD SAAYFCIYTY PRGRRGARRR ATRTFRADGA ATYEENRAEA 150
    QRWATALTCL LRGLPLPGDG EITPDLLPRP PRLLLLVNPF GGRGLAWQWC 200
    KNHVLPMISE AGLSFNLIQT ERQNHARELV QGLSLSEWDG IVTVSGDGLL 250
    HEVLNGLLDR PDWEEAVKMP VGILPCGSGN ALAGAVNQHG GFEPALGLDL 300
    LLNCSLLLCR GGGHPLDLLS VTLASGSRCF SFLSVAWGFV SDVDIQSERF 350
    RALGSARFTL GTVLGLATLH TYRGRLSYLP ATVEPASPTP AHSLPRAKSE 400
    LTLTPDPAPP MAHSPLHRSV SDLPLPLPQP ALASPGSPEP LPILSLNGGG 450
    PELAGDWGGA GDAPLSPDPL LSSPPGSPKA ALHSPVSEGA PVIPPSSGLP 500
    LPTPDARVGA STCGPPDHLL PPLGTPLPPD WVTLEGDFVL MLAISPSHLG 550
    ADLVAAPHAR FDDGLVHLCW VRSGISRAAL LRLFLAMERG SHFSLGCPQL 600
    GYAAARAFRL EPLTPRGVLT VDGEQVEYGP LQAQMHPGIG TLLTGPPGCP 650
    GREP 654
    Length:654
    Mass (Da):69,217
    Last modified:July 26, 2002 - v2
    Checksum:iF73FFCEC930DA50F
    GO
    Isoform 2 (identifier: Q9NRA0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.

    Show »
    Length:618
    Mass (Da):65,205
    Checksum:i1A5B06BCB6F93F1F
    GO
    Isoform 3 (identifier: Q9NRA0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.
         292-390: FEPALGLDLL...ATVEPASPTP → PREDSDSSTS...NVFICKKKKK

    Show »
    Length:618
    Mass (Da):65,170
    Checksum:iD934F61C0A69EDAE
    GO
    Isoform 4 (identifier: Q9NRA0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         13-71: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:595
    Mass (Da):62,986
    Checksum:iC24AC949EEEA059B
    GO
    Isoform 5 (identifier: Q9NRA0-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: MNGHLEAEEQQD → MIGCLHARVS...NSHPFSPPFP
         640-654: GTLLTGPPGCPGREP → ARGRTQTPALPAAPALYGRQPGAAHGLQPVCQGAALFFHNSWLWGSQDLFRIVLTEAVGG

    Show »
    Length:761
    Mass (Da):80,205
    Checksum:iA52BF3441102A3D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491P → S in CAB66636. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti652 – 6521R → Q.
    Corresponds to variant rs11881285 [ dbSNP | Ensembl ].
    VAR_060112

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636Missing in isoform 2 and isoform 3. 4 PublicationsVSP_006217Add
    BLAST
    Alternative sequencei1 – 1212MNGHL…EEQQD → MIGCLHARVSGPLWDAGLCP ASSRSAHTCLSLSVSDAPVS PATAPHCLLLSTAPAPPCPC HGVLNSHPFSPPFP in isoform 5. 1 PublicationVSP_047721Add
    BLAST
    Alternative sequencei13 – 7159Missing in isoform 4. 1 PublicationVSP_046910Add
    BLAST
    Alternative sequencei292 – 39099FEPAL…ASPTP → PREDSDSSTSSSACPLWTTA RSCPRAAASMPGSCPLLPQQ LALGFSRFIQDRVNGGGGRI GSLTCRGHTQRTLPAPAREG GGSLFLKNINVFICKKKKK in isoform 3. 1 PublicationVSP_006218Add
    BLAST
    Alternative sequencei640 – 65415GTLLT…PGREP → ARGRTQTPALPAAPALYGRQ PGAAHGLQPVCQGAALFFHN SWLWGSQDLFRIVLTEAVGG in isoform 5. 1 PublicationVSP_047722Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF245447 mRNA. Translation: AAF74124.1.
    EF107108 mRNA. Translation: ABK81123.1.
    AL136701 mRNA. Translation: CAB66636.1.
    AK000599 mRNA. Translation: BAA91280.1.
    AK300541 mRNA. Translation: BAG62249.1.
    AC022154 Genomic DNA. No translation available.
    BC006161 mRNA. Translation: AAH06161.1.
    BC010671 mRNA. Translation: AAH10671.1.
    CCDSiCCDS12727.1. [Q9NRA0-1]
    CCDS59404.1. [Q9NRA0-4]
    CCDS59405.1. [Q9NRA0-2]
    RefSeqiNP_001191087.1. NM_001204158.2. [Q9NRA0-4]
    NP_001191088.1. NM_001204159.2. [Q9NRA0-1]
    NP_001191089.1. NM_001204160.2. [Q9NRA0-2]
    NP_064511.2. NM_020126.4. [Q9NRA0-1]
    XP_006723354.1. XM_006723291.1. [Q9NRA0-1]
    XP_006723355.1. XM_006723292.1. [Q9NRA0-2]
    XP_006723356.1. XM_006723293.1. [Q9NRA0-4]
    UniGeneiHs.528006.

    Genome annotation databases

    EnsembliENST00000245222; ENSP00000245222; ENSG00000063176. [Q9NRA0-1]
    ENST00000598088; ENSP00000469158; ENSG00000063176. [Q9NRA0-1]
    ENST00000599748; ENSP00000471205; ENSG00000063176. [Q9NRA0-2]
    ENST00000600537; ENSP00000470092; ENSG00000063176. [Q9NRA0-4]
    GeneIDi56848.
    KEGGihsa:56848.
    UCSCiuc002pjr.3. human. [Q9NRA0-1]
    uc002pju.3. human. [Q9NRA0-3]

    Polymorphism databases

    DMDMi22001996.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF245447 mRNA. Translation: AAF74124.1 .
    EF107108 mRNA. Translation: ABK81123.1 .
    AL136701 mRNA. Translation: CAB66636.1 .
    AK000599 mRNA. Translation: BAA91280.1 .
    AK300541 mRNA. Translation: BAG62249.1 .
    AC022154 Genomic DNA. No translation available.
    BC006161 mRNA. Translation: AAH06161.1 .
    BC010671 mRNA. Translation: AAH10671.1 .
    CCDSi CCDS12727.1. [Q9NRA0-1 ]
    CCDS59404.1. [Q9NRA0-4 ]
    CCDS59405.1. [Q9NRA0-2 ]
    RefSeqi NP_001191087.1. NM_001204158.2. [Q9NRA0-4 ]
    NP_001191088.1. NM_001204159.2. [Q9NRA0-1 ]
    NP_001191089.1. NM_001204160.2. [Q9NRA0-2 ]
    NP_064511.2. NM_020126.4. [Q9NRA0-1 ]
    XP_006723354.1. XM_006723291.1. [Q9NRA0-1 ]
    XP_006723355.1. XM_006723292.1. [Q9NRA0-2 ]
    XP_006723356.1. XM_006723293.1. [Q9NRA0-4 ]
    UniGenei Hs.528006.

    3D structure databases

    ProteinModelPortali Q9NRA0.
    SMRi Q9NRA0. Positions 176-406, 514-637.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121208. 2 interactions.
    IntActi Q9NRA0. 5 interactions.
    STRINGi 9606.ENSP00000245222.

    Chemistry

    BindingDBi Q9NRA0.
    ChEMBLi CHEMBL3023.
    GuidetoPHARMACOLOGYi 2205.

    PTM databases

    PhosphoSitei Q9NRA0.

    Polymorphism databases

    DMDMi 22001996.

    Proteomic databases

    MaxQBi Q9NRA0.
    PaxDbi Q9NRA0.
    PRIDEi Q9NRA0.

    Protocols and materials databases

    DNASUi 56848.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000245222 ; ENSP00000245222 ; ENSG00000063176 . [Q9NRA0-1 ]
    ENST00000598088 ; ENSP00000469158 ; ENSG00000063176 . [Q9NRA0-1 ]
    ENST00000599748 ; ENSP00000471205 ; ENSG00000063176 . [Q9NRA0-2 ]
    ENST00000600537 ; ENSP00000470092 ; ENSG00000063176 . [Q9NRA0-4 ]
    GeneIDi 56848.
    KEGGi hsa:56848.
    UCSCi uc002pjr.3. human. [Q9NRA0-1 ]
    uc002pju.3. human. [Q9NRA0-3 ]

    Organism-specific databases

    CTDi 56848.
    GeneCardsi GC19P049122.
    HGNCi HGNC:18859. SPHK2.
    MIMi 607092. gene.
    neXtProti NX_Q9NRA0.
    PharmGKBi PA38719.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1597.
    HOGENOMi HOG000111460.
    HOVERGENi HBG054796.
    InParanoidi Q9NRA0.
    KOi K04718.
    OrthoDBi EOG7PCJGK.
    PhylomeDBi Q9NRA0.
    TreeFami TF354296.

    Enzyme and pathway databases

    BRENDAi 2.7.1.91. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    ChiTaRSi SPHK2. human.
    GeneWikii SPHK2.
    GenomeRNAii 56848.
    NextBioi 35460299.
    PROi Q9NRA0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRA0.
    Bgeei Q9NRA0.
    Genevestigatori Q9NRA0.

    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. "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] (ISOFORM 2), CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    2. "Variant of human sphingosine kinase-2 (SPHK2)."
      Alemany R., Ruemenapp U., van Koppen C.J., Danneberg K., Meyer zu Heringdorf D., Jakobs K.H.
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-354 (ISOFORM 3).
      Tissue: Carcinoma and Prostate.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1 AND 2).
      Tissue: Eye and Lymph.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A lipid binding domain in sphingosine kinase 2."
      Don A.S., Rosen H.
      Biochem. Biophys. Res. Commun. 380:87-92(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, REGION.

    Entry informationi

    Entry nameiSPHK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRA0
    Secondary accession number(s): A0T4C8
    , B4DU87, Q9BRN1, Q9H0Q2, Q9NWU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: July 26, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3