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Q9NYA1

- SPHK1_HUMAN

UniProt

Q9NYA1 - SPHK1_HUMAN

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Protein
Sphingosine kinase 1
Gene
SPHK1, SPHK, SPK
Organism
Homo sapiens (Human)
Status
Reviewed - 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-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.3 Publications
ATP + sphingosine = ADP + sphingosine 1-phosphate.3 Publications

Cofactori

Magnesium.1 Publication

Kineticsi

  1. KM=14 µM for sphingosine1 Publication
  2. KM=20 µM for dihydrosphingosine
  3. KM=77 µM for ATP

pH dependencei

Optimum pH is 7.4.

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. D-erythro-sphingosine kinase activity Source: UniProtKB
  3. DNA binding Source: MGI
  4. NAD+ kinase activity Source: InterPro
  5. calmodulin binding Source: UniProtKB
  6. diacylglycerol kinase activity Source: InterPro
  7. magnesium ion binding Source: UniProtKB
  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 NF-kappaB import into nucleus Source: UniProtKB
  16. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  17. positive regulation of angiogenesis Source: UniProtKB
  18. positive regulation of cell growth Source: UniProtKB
  19. positive regulation of cell migration Source: UniProtKB
  20. positive regulation of fibroblast proliferation Source: MGI
  21. positive regulation of mitotic cell cycle Source: UniProtKB
  22. positive regulation of neuron projection development Source: Ensembl
  23. positive regulation of neurotransmitter secretion Source: Ensembl
  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 ATP Source: Ensembl
  32. response to amine 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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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 1
PRO_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.2 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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 159148DAGKc
Add
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.

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

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.
VSP_035453
Alternative sequencei3 – 31P → PVVGCGRGLFGFVFS in isoform 3.
VSP_047078

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 126 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

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