Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NRA0

- SPHK2_HUMAN

UniProt

Q9NRA0 - SPHK2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Sphingosine kinase 2

Gene

SPHK2

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-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

Mg2+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. Ras GTPase binding Source: UniProtKB
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9NRA0.
ExpressionAtlasiQ9NRA0. baseline and differential.
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.
GeneTreeiENSGT00690000101761.
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

        10         20         30         40         50
MNGHLEAEEQ QDQRPDQELT GSWGHGPRST LVRAKAMAPP PPPLAASTPL
60 70 80 90 100
LHGEFGSYPA RGPRFALTLT SQALHIQRLR PKPEARPRGG LVPLAEVSGC
110 120 130 140 150
CTLRSRSPSD SAAYFCIYTY PRGRRGARRR ATRTFRADGA ATYEENRAEA
160 170 180 190 200
QRWATALTCL LRGLPLPGDG EITPDLLPRP PRLLLLVNPF GGRGLAWQWC
210 220 230 240 250
KNHVLPMISE AGLSFNLIQT ERQNHARELV QGLSLSEWDG IVTVSGDGLL
260 270 280 290 300
HEVLNGLLDR PDWEEAVKMP VGILPCGSGN ALAGAVNQHG GFEPALGLDL
310 320 330 340 350
LLNCSLLLCR GGGHPLDLLS VTLASGSRCF SFLSVAWGFV SDVDIQSERF
360 370 380 390 400
RALGSARFTL GTVLGLATLH TYRGRLSYLP ATVEPASPTP AHSLPRAKSE
410 420 430 440 450
LTLTPDPAPP MAHSPLHRSV SDLPLPLPQP ALASPGSPEP LPILSLNGGG
460 470 480 490 500
PELAGDWGGA GDAPLSPDPL LSSPPGSPKA ALHSPVSEGA PVIPPSSGLP
510 520 530 540 550
LPTPDARVGA STCGPPDHLL PPLGTPLPPD WVTLEGDFVL MLAISPSHLG
560 570 580 590 600
ADLVAAPHAR FDDGLVHLCW VRSGISRAAL LRLFLAMERG SHFSLGCPQL
610 620 630 640 650
GYAAARAFRL EPLTPRGVLT VDGEQVEYGP LQAQMHPGIG TLLTGPPGCP

GREP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00690000101761.
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

Bgeei Q9NRA0.
ExpressionAtlasi Q9NRA0. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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