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Q9NYA1 (SPHK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:SPHK, SPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length384 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. Ref.13 Ref.14

Catalytic activity

ATP + sphinganine = ADP + sphinganine 1-phosphate. Ref.2 Ref.13 Ref.14

ATP + sphingosine = ADP + sphingosine 1-phosphate. Ref.2 Ref.13 Ref.14

Cofactor

Magnesium. Ref.3

Subunit structure

Interacts with ACY1 By similarity. Binds to calmodulin. Interacts with SPHKAP. Interacts with CIB1, the interaction occurs in a calcium-dependent manner. Ref.9 Ref.12

Subcellular location

Cytoplasm. Nucleus. Cell membrane. Note: Translocated from the cytoplasm to the plasma membrane in a CIB1-dependent manner. Ref.10 Ref.12

Tissue specificity

Widely expressed with highest levels in adult liver, kidney, heart and skeletal muscle. Ref.2

Miscellaneous

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

Sequence similarities

Contains 1 DAGKc domain.

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for sphingosine Ref.3

KM=20 µM for dihydrosphingosine

KM=77 µM for ATP

pH dependence:

Optimum pH is 7.4.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

blood vessel development

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

calcium-mediated signaling

Inferred from direct assay Ref.3. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

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 electronic annotation. Source: Ensembl

intracellular signal transduction

Traceable author statement Ref.3. Source: UniProtKB

lipid phosphorylation

Inferred from direct assay PubMed 12393916PubMed 15623571. Source: GOC

negative regulation of apoptotic process

Traceable author statement Ref.3. Source: UniProtKB

positive regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay PubMed 12441135. Source: UniProtKB

positive regulation of cell growth

Inferred from direct assay PubMed 12441135. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 12441135. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 15623571. Source: MGI

positive regulation of mitotic cell cycle

Inferred from direct assay PubMed 12441135. Source: UniProtKB

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 direct assay Ref.13. Source: UniProtKB

positive regulation of smooth muscle contraction

Inferred from direct assay PubMed 12847068. Source: UniProtKB

protein folding

Traceable author statement. Source: Reactome

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

Inferred from electronic annotation. Source: InterPro

regulation of interleukin-1 beta production

Inferred from electronic annotation. Source: Ensembl

regulation of tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.13. 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

signal transduction

Traceable author statement PubMed 10751414. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingoid catabolic process

Non-traceable author statement Ref.1. Source: UniProtKB

sphingolipid biosynthetic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

sphingosine metabolic process

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Traceable author statement Ref.1. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay PubMed 12393916. Source: UniProtKB

D-erythro-sphingosine kinase activity

Inferred from direct assay Ref.1Ref.13. Source: UniProtKB

DNA binding

Inferred from direct assay PubMed 12393916. Source: MGI

NAD+ kinase activity

Inferred from electronic annotation. Source: InterPro

calmodulin binding

Inferred from direct assay Ref.3. Source: UniProtKB

diacylglycerol kinase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from direct assay Ref.3. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein phosphatase 2A binding

Inferred from physical interaction PubMed 21075214. Source: BHF-UCL

sphinganine kinase activity

Inferred from direct assay PubMed 12393916PubMed 15623571. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYA1-1)

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: Q9NYA1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSAQVLGFLR...WQREPRVEVM
Isoform 3 (identifier: Q9NYA1-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Sphingosine kinase 1
PRO_0000181357

Regions

Domain12 – 159148DAGKc
Nucleotide binding22 – 243ATP
Nucleotide binding54 – 585ATP
Nucleotide binding111 – 1133ATP
Nucleotide binding341 – 3433ATP
Region79 – 824Substrate binding
Motif147 – 1559Nuclear export signal 1
Motif161 – 1699Nuclear export signal 2

Sites

Active site811Proton donor/acceptor Ref.14
Binding site861ATP
Binding site1781Substrate
Binding site1851ATP
Binding site1911ATP

Amino acid modifications

Modified residue1931Phosphothreonine Ref.11
Modified residue2251Phosphoserine Ref.13

Natural variations

Alternative sequence11M → MSAQVLGFLRSWTPLPLAAP RGPAAAGNDAGAPAATAPGG EGEPHSRPCDARLGSTDKEL KAGAAATGSAPTAPGTPWQR EPRVEVM in isoform 2.
VSP_035453
Alternative sequence31P → PVVGCGRGLFGFVFS in isoform 3.
VSP_047078
Isoform 2:
Natural variant341A → T.
Corresponds to variant rs346803 [ dbSNP | Ensembl ].

Experimental info

Mutagenesis811D → A: Loss of enzyme activity. Ref.12 Ref.14
Mutagenesis811D → N: Strongly reduced enzyme activity. Ref.12 Ref.14
Mutagenesis821G → D: Loss of enzyme activity. Ref.12 Ref.13
Mutagenesis1971F → A: Abolishes interaction with CIB1; when associated with A-198. Ref.12
Mutagenesis1981L → A: Abolishes interaction with CIB1; when associated with A-197. Ref.12
Sequence conflict61Missing in CAB92131. Ref.4
Sequence conflict11 – 155LPRPC → ARL in CAB92131. Ref.4
Sequence conflict114 – 1152NA → KP in CAB92131. Ref.4
Sequence conflict2511V → M in AAF73423. Ref.2
Sequence conflict2601V → I in AAF73423. Ref.2
Sequence conflict3021L → F in AAF73423. Ref.2
Sequence conflict3251V → G in CAB92131. Ref.4
Sequence conflict3371V → M in AAG01980. Ref.3

Secondary structure

.......................................................... 384
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: EB04A7F2034C2DB0

FASTA38442,518
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F6BF2D324E12CFC0
Show »

FASTA47051,054
Isoform 3 [UniParc].

Checksum: 7F2C9B26C030E560
Show »

FASTA39843,944

References

« Hide 'large scale' references
[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]"Functional characterization of human sphingosine kinase-1."
Nava V.E., Lacana' E., Poulton S., Liu H., Sugiura M., Kono K., Milstien S., Kohama T., Spiegel S.
FEBS Lett. 473:81-84(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11744.1. [Q9NYA1-2]
CCDS45785.1. [Q9NYA1-1]
CCDS59297.1. [Q9NYA1-3]
RefSeqNP_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]
UniGeneHs.68061.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9NYA1.
SMRQ9NYA1. Positions 9-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114396. 7 interactions.
IntActQ9NYA1. 7 interactions.
MINTMINT-226199.
STRING9606.ENSP00000313681.

Chemistry

BindingDBQ9NYA1.
ChEMBLCHEMBL4394.
GuidetoPHARMACOLOGY2204.

PTM databases

PhosphoSiteQ9NYA1.

Polymorphism databases

DMDM17369329.

Proteomic databases

MaxQBQ9NYA1.
PaxDbQ9NYA1.
PRIDEQ9NYA1.

Protocols and materials databases

DNASU8877.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323374; ENSP00000313681; ENSG00000176170. [Q9NYA1-2]
ENST00000392496; ENSP00000376285; ENSG00000176170. [Q9NYA1-1]
ENST00000545180; ENSP00000440970; ENSG00000176170. [Q9NYA1-1]
ENST00000590959; ENSP00000468547; ENSG00000176170. [Q9NYA1-3]
ENST00000592299; ENSP00000465726; ENSG00000176170. [Q9NYA1-1]
GeneID8877.
KEGGhsa:8877.
UCSCuc002jrf.1. human. [Q9NYA1-1]
uc002jrh.2. human.
uc002jrj.2. human. [Q9NYA1-2]

Organism-specific databases

CTD8877.
GeneCardsGC17P074380.
HGNCHGNC:11240. SPHK1.
HPAHPA022829.
HPA028761.
MIM603730. gene.
neXtProtNX_Q9NYA1.
PharmGKBPA36070.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1597.
HOVERGENHBG054796.
InParanoidQ9NYA1.
KOK04718.
OMADCPYLVY.
PhylomeDBQ9NYA1.
TreeFamTF354296.

Enzyme and pathway databases

BRENDA2.7.1.91. 2681.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
SABIO-RKQ9NYA1.
SignaLinkQ9NYA1.

Gene expression databases

ArrayExpressQ9NYA1.
BgeeQ9NYA1.
CleanExHS_SPHK1.
GenevestigatorQ9NYA1.

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

GeneWikiSphingosine_kinase_1.
GenomeRNAi8877.
NextBio33329.
PROQ9NYA1.
SOURCESearch...

Entry information

Entry nameSPHK1_HUMAN
AccessionPrimary (citable) accession number: Q9NYA1
Secondary accession number(s): Q8N632 expand/collapse secondary AC list , Q96GK1, Q9HD92, Q9NY70, Q9NYL3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM