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Q9BX95

- SGPP1_HUMAN

UniProt

Q9BX95 - SGPP1_HUMAN

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Protein

Sphingosine-1-phosphate phosphatase 1

Gene

SGPP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Has enzymatic activity against both sphingosine 1-phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels.1 Publication

GO - Molecular functioni

  1. sphingosine-1-phosphate phosphatase activity Source: Ensembl

GO - Biological processi

  1. extrinsic apoptotic signaling pathway Source: Ensembl
  2. intrinsic apoptotic signaling pathway Source: Ensembl
  3. small molecule metabolic process Source: Reactome
  4. sphinganine-1-phosphate metabolic process Source: Ensembl
  5. sphingolipid biosynthetic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
  7. sphingosine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine-1-phosphate phosphatase 1 (EC:3.1.3.-)
Short name:
SPPase1
Short name:
Spp1
Short name:
hSPP1
Short name:
hSPPase1
Alternative name(s):
Sphingosine-1-phosphatase 1
Gene namesi
Name:SGPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:17720. SGPP1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei132 – 15221HelicalSequence AnalysisAdd
BLAST
Transmembranei163 – 18321HelicalSequence AnalysisAdd
BLAST
Transmembranei204 – 22421HelicalSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Transmembranei257 – 27721HelicalSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST
Transmembranei322 – 34221HelicalSequence AnalysisAdd
BLAST
Transmembranei359 – 37921HelicalSequence AnalysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134884424.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Sphingosine-1-phosphate phosphatase 1PRO_0000114477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011Phosphoserine2 Publications
Modified residuei112 – 1121Phosphoserine3 Publications
Modified residuei114 – 1141Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BX95.
PaxDbiQ9BX95.
PeptideAtlasiQ9BX95.
PRIDEiQ9BX95.

PTM databases

PhosphoSiteiQ9BX95.

Expressioni

Tissue specificityi

Ubiquitous, with the strongest level in placenta and kidney.1 Publication

Gene expression databases

BgeeiQ9BX95.
CleanExiHS_SGPP1.
GenevestigatoriQ9BX95.

Organism-specific databases

HPAiHPA053149.

Interactioni

Protein-protein interaction databases

BioGridi123508. 11 interactions.
STRINGi9606.ENSP00000247225.

Structurei

3D structure databases

ProteinModelPortaliQ9BX95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0671.
GeneTreeiENSGT00390000017322.
HOGENOMiHOG000234228.
HOVERGENiHBG079185.
InParanoidiQ9BX95.
KOiK04716.
OMAiQCTKDII.
OrthoDBiEOG72VH66.
PhylomeDBiQ9BX95.
TreeFamiTF323419.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9BX95-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLRQRLAQL VGRLQDPQKV ARFQRLCGVE APPRRSADRR EDEKAEAPLA
60 70 80 90 100
GDPRLRGRQP GAPGGPQPPG SDRNQCPAKP DGGGAPNGVR NGLAAELGPA
110 120 130 140 150
SPRRAGALRR NSLTGEEGQL ARVSNWPLYC LFCFGTELGN ELFYILFFPF
160 170 180 190 200
WIWNLDPLVG RRLVVIWVLV MYLGQCTKDI IRWPRPASPP VVKLEVFYNS
210 220 230 240 250
EYSMPSTHAM SGTAIPISMV LLTYGRWQYP LIYGLILIPC WCSLVCLSRI
260 270 280 290 300
YMGMHSILDI IAGFLYTILI LAVFYPFVDL IDNFNQTHKY APFIIIGLHL
310 320 330 340 350
ALGIFSFTLD TWSTSRGDTA EILGSGAGIA CGSHVTYNMG LVLDPSLDTL
360 370 380 390 400
PLAGPPITVT LFGKAILRIL IGMVFVLIIR DVMKKITIPL ACKIFNIPCD
410 420 430 440
DIRKARQHME VELPYRYITY GMVGFSITFF VPYIFFFIGI S
Length:441
Mass (Da):49,108
Last modified:April 26, 2004 - v2
Checksum:i86A018DDDA3A3019
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461L → P in AAK26660. (PubMed:12815058)Curated
Sequence conflicti191 – 1911V → A in AAK26660. (PubMed:12815058)Curated
Sequence conflicti282 – 2821D → G in AAK26660. (PubMed:12815058)Curated
Sequence conflicti320 – 3201A → T in AAK26660. (PubMed:12815058)Curated
Sequence conflicti371 – 3711I → V in AAK26660. (PubMed:12815058)Curated
Sequence conflicti375 – 3751F → S in AAK26660. (PubMed:12815058)Curated
Sequence conflicti410 – 4101E → G in AAK26660. (PubMed:12815058)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF349315 mRNA. Translation: AAK26660.1.
AJ293294 mRNA. Translation: CAC17772.1.
AK314188 mRNA. Translation: BAG36867.1.
AL161670 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80834.1.
BC063839 mRNA. Translation: AAH63839.1.
BC070060 mRNA. Translation: AAH70060.1.
CCDSiCCDS9760.1.
RefSeqiNP_110418.1. NM_030791.2.
UniGeneiHs.24678.

Genome annotation databases

EnsembliENST00000247225; ENSP00000247225; ENSG00000126821.
GeneIDi81537.
KEGGihsa:81537.
UCSCiuc001xgj.3. human.

Polymorphism databases

DMDMi46577706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF349315 mRNA. Translation: AAK26660.1 .
AJ293294 mRNA. Translation: CAC17772.1 .
AK314188 mRNA. Translation: BAG36867.1 .
AL161670 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80834.1 .
BC063839 mRNA. Translation: AAH63839.1 .
BC070060 mRNA. Translation: AAH70060.1 .
CCDSi CCDS9760.1.
RefSeqi NP_110418.1. NM_030791.2.
UniGenei Hs.24678.

3D structure databases

ProteinModelPortali Q9BX95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123508. 11 interactions.
STRINGi 9606.ENSP00000247225.

PTM databases

PhosphoSitei Q9BX95.

Polymorphism databases

DMDMi 46577706.

Proteomic databases

MaxQBi Q9BX95.
PaxDbi Q9BX95.
PeptideAtlasi Q9BX95.
PRIDEi Q9BX95.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247225 ; ENSP00000247225 ; ENSG00000126821 .
GeneIDi 81537.
KEGGi hsa:81537.
UCSCi uc001xgj.3. human.

Organism-specific databases

CTDi 81537.
GeneCardsi GC14M064150.
HGNCi HGNC:17720. SGPP1.
HPAi HPA053149.
MIMi 612826. gene.
neXtProti NX_Q9BX95.
PharmGKBi PA134884424.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0671.
GeneTreei ENSGT00390000017322.
HOGENOMi HOG000234228.
HOVERGENi HBG079185.
InParanoidi Q9BX95.
KOi K04716.
OMAi QCTKDII.
OrthoDBi EOG72VH66.
PhylomeDBi Q9BX95.
TreeFami TF323419.

Enzyme and pathway databases

Reactomei REACT_115810. Sphingolipid de novo biosynthesis.

Miscellaneous databases

GeneWikii SGPP1.
GenomeRNAii 81537.
NextBioi 71763.
PROi Q9BX95.
SOURCEi Search...

Gene expression databases

Bgeei Q9BX95.
CleanExi HS_SGPP1.
Genevestigatori Q9BX95.

Family and domain databases

Gene3Di 1.20.144.10. 1 hit.
InterProi IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view ]
Pfami PF01569. PAP2. 1 hit.
[Graphical view ]
SMARTi SM00014. acidPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF48317. SSF48317. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Role of human sphingosine-1-phosphate phosphatase 1 in the regulation of intra- and extracellular sphingosine-1-phosphate levels and cell viability."
    Johnson K.R., Johnson K.Y., Becker K.P., Bielawski J., Mao C., Obeid L.M.
    J. Biol. Chem. 278:34541-34547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    Tissue: Fetal kidney.
  2. "Cloning of human sphingosine-1-phosphatase."
    Van Veldhoven P.P.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Thalamus.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Placenta and PNS.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND THR-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSGPP1_HUMAN
AccessioniPrimary (citable) accession number: Q9BX95
Secondary accession number(s): B2RAH0, Q9H189
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: April 26, 2004
Last modified: October 29, 2014
This is version 102 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 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3