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UniProtKB/Swiss-Prot entry Q9NYA1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SPHK1_HUMAN
Primary accession number Q9NYA1
Secondary accession numbers Q8N632 Q9HD92 Q9NY70 Q9NYL3
Integrated into Swiss-Prot on October 24, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Sphingosine kinase 1
Synonyms SPK 1
SK 1
EC 2.7.1.91
Gene name
Name: SPHK1
Synonyms: SPHK, SPK
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/S0378-1119(00)00205-5; PubMed=10863092 [NCBI, ExPASy, EBI, Israel, Japan]
Melendez A.J., Carlos-Dias E., Gosink M., Allen J.M., Takacs L.;
"Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution.";
Gene 251:19-26(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND TISSUE SPECIFICITY.
DOI=10.1016/S0014-5793(00)01510-6; PubMed=10802064 [NCBI, ExPASy, EBI, Israel, Japan]
Nava V.E., Lacana' E., Poulton S., Liu H., Sugiura M., Kono K., Milstien S., Kohama T., Spiegel S.;
"Functional characterization of human sphingosine kinase-1.";
FEBS Lett. 473:81-84(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
DOI=10.1042/0264-6021:3500429; PubMed=10947957 [NCBI, ExPASy, EBI, Israel, Japan]
Pitson S.M., D'Andrea R.J., Vandeleur L., Moretti P.A.B., Xia P., Gamble J.R., Vadas M.A., Wattenberg B.W.;
"Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes.";
Biochem. J. 350:429-441(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Van Veldhoven P.P., Gijsbers S.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Mammary gland, Ovary, and Testis;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Blood, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH SPHKAP.
DOI=10.1074/jbc.M202841200; PubMed=12080051 [NCBI, ExPASy, EBI, Israel, Japan]
Lacana E., Maceyka M., Milstien S., Spiegel S.;
"Cloning and characterization of a protein kinase A anchoring protein (AKAP)-related protein that interacts with and regulates sphingosine kinase 1 activity.";
J. Biol. Chem. 277:32947-32953(2002).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF266756; AAF73470.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF238083; AAF73423.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200328; AAG01980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK023393; BAB14558.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292294; BAF84983.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022402; BAB14028.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ245504; CAB92131.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471099; EAW89392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014439; AAH14439.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030553; AAH30553.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_892010.1; -.
UniGene Hs.68061
3D structure databases
ModBase Q9NYA1.
PTM databases
PhosphoSite Q9NYA1; -.
Organism-specific databases
H-InvDB HIX0022906; -.
HGNC HGNC:11240; SPHK1.
GenAtlas SPHK1.
MIM 603730; gene. [NCBI / EBI]
PharmGKB PA36070; -.
GeneCards Q9NYA1.
Gene expression databases
ArrayExpress Q9NYA1; -.
CleanEx HS_SPHK1; -.
GermOnline ENSG00000176170; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0005624; Cellular component: membrane fraction (traceable author statement from UniProtKB).
GO:0005625; Cellular component: soluble fraction (inferred from direct assay from MGI).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from UniProtKB).
GO:0005516; Molecular function: calmodulin binding (inferred from direct assay from UniProtKB).
GO:0017050; Molecular function: D-erythro-sphingosine kinase activity (inferred from direct assay from UniProtKB).
GO:0004143; Molecular function: diacylglycerol kinase activity (inferred from electronic annotation from InterPro).
GO:0003677; Molecular function: DNA binding (inferred from direct assay from MGI).
GO:0000287; Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0008481; Molecular function: sphinganine kinase activity (inferred from direct assay from MGI).
GO:0007205; Biological process: activation of protein kinase C activity (inferred from electronic annotation from InterPro).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0019722; Biological process: calcium-mediated signaling (inferred from direct assay from UniProtKB).
GO:0045766; Biological process: positive regulation of angiogenesis (inferred from direct assay from UniProtKB).
GO:0030307; Biological process: positive regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0030335; Biological process: positive regulation of cell migration (inferred from direct assay from UniProtKB).
GO:0048146; Biological process: positive regulation of fibroblast proliferation (inferred from direct assay from MGI).
GO:0045931; Biological process: positive regulation of mitotic cell cycle (inferred from direct assay from UniProtKB).
GO:0045987; Biological process: positive regulation of smooth muscle contraction (inferred from direct assay from UniProtKB).
GO:0046521; Biological process: sphingoid catabolic process (non-traceable author statement from UniProtKB).
GO:0006670; Biological process: sphingosine metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001206; DAGKc.
Graphical view of domain structure.
Pfam PF00781; DAGK_cat; 1.
Pfam graphical view of domain structure.
ProDom PD005043; DAGKc; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00046; DAGKc; 1.
SMART graphical view of domain structure.
ProtoNet Q9NYA1.
Genome annotation databases
Ensembl ENSG00000176170; Homo sapiens. [Contig view]
GeneID 8877; -.
Phylogenomic databases
HOVERGEN Q9NYA1; -.
Other
SOURCE SPHK1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   384  384     Sphingosine kinase 1. PRO_0000181357
DOMAIN   16   153  138     DAGKc. 
MOD_RES   193   193        Phosphothreonine. 
VAR_SEQ   1     1        M -> MSAQVLGFLRSWTPLPLAAPRGPAAAGNDAGAPTATAPGG EGEPHSRPCDARLGSTDKELKAGAAATGSAPTAPGTPWQR EPRVEVM (in isoform 2). VSP_035453
CONFLICT   6     6        Missing (in Ref. 4; CAB92131). 
CONFLICT   11    15        LPRPC -> ARL (in Ref. 4; CAB92131). 
CONFLICT   114   115        NA -> KP (in Ref. 4; CAB92131). 
CONFLICT   251   251        V -> M (in Ref. 2; AAF73423). 
CONFLICT   260   260        V -> I (in Ref. 2; AAF73423). 
CONFLICT   302   302        L -> F (in Ref. 2; AAF73423). 
CONFLICT   325   325        V -> G (in Ref. 4; CAB92131). 
CONFLICT   337   337        V -> M (in Ref. 3; AAG01980). 
Sequence information
Length: 384 AA [This is the length of the unprocessed precursor] Molecular weight: 42518 Da [This is the MW of the unprocessed precursor] CRC64: EB04A7F2034C2DB0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPAGGPRGV LPRPCRVLVL LNPRGGKGKA LQLFRSHVQP LLAEAEISFT LMLTERRNHA 

        70         80         90        100        110        120 
RELVRSEELG RWDALVVMSG DGLMHEVVNG LMERPDWETA IQKPLCSLPA GSGNALAASL 

       130        140        150        160        170        180 
NHYAGYEQVT NEDLLTNCTL LLCRRLLSPM NLLSLHTASG LRLFSVLSLA WGFIADVDLE 

       190        200        210        220        230        240 
SEKYRRLGEM RFTLGTFLRL AALRTYRGRL AYLPVGRVGS KTPASPVVVQ QGPVDAHLVP 

       250        260        270        280        290        300 
LEEPVPSHWT VVPDEDFVLV LALLHSHLGS EMFAAPMGRC AAGVMHLFYV RAGVSRAMLL 

       310        320        330        340        350        360 
RLFLAMEKGR HMEYECPYLV YVPVVAFRLE PKDGKGVFAV DGELMVSEAV QGQVHPNYFW 

       370        380 
MVSGCVEPPP SWKPQQMPPP EEPL 

Q9NYA1 in FASTA format

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