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O08530

- S1PR1_MOUSE

UniProt

O08530 - S1PR1_MOUSE

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Protein

Sphingosine 1-phosphate receptor 1

Gene

S1pr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury.10 Publications

GO - Molecular functioni

  1. sphingolipid binding Source: Ensembl
  2. sphingosine-1-phosphate receptor activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: MGI
  3. angiogenesis Source: MGI
  4. blood vessel maturation Source: UniProtKB
  5. brain development Source: MGI
  6. cardiac muscle tissue growth involved in heart morphogenesis Source: UniProtKB
  7. cell migration Source: UniProtKB
  8. chemotaxis Source: UniProtKB
  9. endothelial cell differentiation Source: Ensembl
  10. heart trabecula morphogenesis Source: UniProtKB
  11. lamellipodium assembly Source: UniProtKB
  12. negative regulation of stress fiber assembly Source: Ensembl
  13. neuron differentiation Source: Ensembl
  14. positive regulation of cell migration Source: Ensembl
  15. positive regulation of cell proliferation Source: MGI
  16. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: Ensembl
  17. positive regulation of positive chemotaxis Source: Ensembl
  18. positive regulation of Ras GTPase activity Source: Ensembl
  19. positive regulation of smooth muscle cell proliferation Source: Ensembl
  20. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  21. regulation of bone mineralization Source: UniProtKB
  22. regulation of bone resorption Source: UniProtKB
  23. regulation of cell adhesion Source: MGI
  24. sphingosine-1-phosphate signaling pathway Source: UniProtKB
  25. T cell migration Source: UniProtKB
  26. transmission of nerve impulse Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Angiogenesis, Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingosine 1-phosphate receptor 1
Short name:
S1P receptor 1
Short name:
S1P1
Alternative name(s):
Endothelial differentiation G-protein coupled receptor 1
Lysophospholipid receptor B1
Sphingosine 1-phosphate receptor Edg-1
Short name:
S1P receptor Edg-1
CD_antigen: CD363
Gene namesi
Name:S1pr1
Synonyms:Edg1, Lpb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1096355. S1pr1.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Endosome By similarity. Membranecaveola By similarity
Note: Recruited to caveolin-enriched plasma membrane microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand binding leads to receptor internalization (By similarity).By similarity

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
  2. external side of plasma membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. intrinsic component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality, due to impaired vascular maturation and defects in heart development. Embryos appear normal up to 11.5 dpc, but after that they display massive hemorrhage. They have a normally arborized vascular network, but present excessive sprouting angiogenesis and severe aberrations in vessel size. Their aorta and other arteries are not properly enveloped by vascular smooth muscle cells, causing hemorrhage. Likewise, small blood vessels show a marked reduction in the number of vascular pericytes. In addition, mutants display defects in heart morphogenesis, with reduced myocardial tissue and altered morphology of the heart wall and the trabeculae. Conditional knockout in endothelial cells leads to the same vascular maturation defect as that seen in homozygous knockout mice. Conditional knockout in fibroblasts leads to defects in chemotaxis, probably due to defects in the activation of SRC and PTK2/FAK1, resulting in defects in the reorganization of the actin cytoskeleton and lamellipodia formation. A T-cell-specific knockout leads to a defect in the egress of mature T-cells from the thymus into the periphery. Conditional knockout in osteoclast precursors leads to osteoporosis, due to impaired migration of osteoclast precursors and increased osteoclast attachment to the bone.8 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 382381Sphingosine 1-phosphate receptor 1PRO_0000069413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylvaline1 Publication
Modified residuei10 – 101N6-acetyllysine1 Publication
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi184 ↔ 191PROSITE-ProRule annotation
Modified residuei236 – 2361PhosphothreonineBy similarity
Disulfide bondi282 ↔ 287PROSITE-ProRule annotation
Lipidationi328 – 3281S-palmitoyl cysteineBy similarity
Modified residuei353 – 3531PhosphoserineSequence Analysis

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiO08530.
PRIDEiO08530.

PTM databases

PhosphoSiteiO08530.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues with highest levels in brain, heart and spleen. Lower levels found in kidney, liver, lung, muscle, placenta, thymus, and uterus. Very low levels in intestine, stomach and testis. According to PubMed:9931453, expressed modestly in apparent endothelial cells surrounding some blood vessels (e.g. aortic trunk).2 Publications

Gene expression databases

BgeeiO08530.
ExpressionAtlasiO08530. baseline and differential.
GenevestigatoriO08530.

Interactioni

Subunit structurei

Interacts with GNAI1 and GNAI3.By similarity

Protein-protein interaction databases

BioGridi199373. 2 interactions.
DIPiDIP-32248N.
IntActiO08530. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO08530.
SMRiO08530. Positions 16-326.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4645ExtracellularBy similarityAdd
BLAST
Topological domaini69 – 8214CytoplasmicBy similarityAdd
BLAST
Topological domaini105 – 11612ExtracellularBy similarityAdd
BLAST
Topological domaini139 – 16022CytoplasmicBy similarityAdd
BLAST
Topological domaini183 – 19614ExtracellularBy similarityAdd
BLAST
Topological domaini225 – 25733CytoplasmicBy similarityAdd
BLAST
Topological domaini279 – 28911ExtracellularBy similarityAdd
BLAST
Topological domaini311 – 38272CytoplasmicBy similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6822Helical; Name=1By similarityAdd
BLAST
Transmembranei83 – 10422Helical; Name=2By similarityAdd
BLAST
Transmembranei117 – 13822Helical; Name=3By similarityAdd
BLAST
Transmembranei161 – 18222Helical; Name=4By similarityAdd
BLAST
Transmembranei197 – 22428Helical; Name=5By similarityAdd
BLAST
Transmembranei258 – 27821Helical; Name=6By similarityAdd
BLAST
Transmembranei290 – 31021Helical; Name=7By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1212Sphingosine 1-phosphate bindingBy similarity
Regioni265 – 2695Sphingosine 1-phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148018.
GeneTreeiENSGT00760000118804.
HOGENOMiHOG000233501.
HOVERGENiHBG103071.
InParanoidiO08530.
KOiK04288.
OMAiSAFIACW.
OrthoDBiEOG708W0B.
TreeFamiTF330052.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR000987. EDG1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004061. S1P_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00642. EDG1RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01523. S1PRECEPTOR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08530-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVSTSIPEVK ALRSSVSDYG NYDIIVRHYN YTGKLNIGAE KDHGIKLTSV
60 70 80 90 100
VFILICCFII LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA
110 120 130 140 150
NLLLSGATTY KLTPAQWFLR EGSMFVALSA SVFSLLAIAI ERYITMLKMK
160 170 180 190 200
LHNGSNSSRS FLLISACWVI SLILGGLPIM GWNCISSLSS CSTVLPLYHK
210 220 230 240 250
HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN ISKASRSSEK
260 270 280 290 300
SLALLKTVII VLSVFIACWA PLFILLLLDV GCKAKTCDIL YKAEYFLVLA
310 320 330 340 350
VLNSGTNPII YTLTNKEMRR AFIRIVSCCK CPNGDSAGKF KRPIIPGMEF
360 370 380
SRSKSDNSSH PQKDDGDNPE TIMSSGNVNS SS
Length:382
Mass (Da):42,639
Last modified:July 27, 2011 - v3
Checksum:i5FE4C9A2BD65CB2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791I → S in AAC53294. (PubMed:9226368)Curated
Sequence conflicti179 – 1791I → S in AAD16975. (PubMed:9931453)Curated
Sequence conflicti218 – 2181V → A in AAC53294. (PubMed:9226368)Curated
Sequence conflicti244 – 2441A → G in AAC53294. (PubMed:9226368)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40811 Genomic DNA. Translation: AAC53294.1.
AF108019 Genomic DNA. Translation: AAD16975.1.
AK004591 mRNA. Translation: BAB23393.1.
AK146501 mRNA. Translation: BAE27216.1.
CH466532 Genomic DNA. Translation: EDL12402.1.
BC049094 mRNA. Translation: AAH49094.1.
BC051023 mRNA. Translation: AAH51023.1.
CCDSiCCDS17781.1.
RefSeqiNP_031927.2. NM_007901.5.
UniGeneiMm.982.

Genome annotation databases

EnsembliENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
GeneIDi13609.
KEGGimmu:13609.
UCSCiuc008rbo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40811 Genomic DNA. Translation: AAC53294.1 .
AF108019 Genomic DNA. Translation: AAD16975.1 .
AK004591 mRNA. Translation: BAB23393.1 .
AK146501 mRNA. Translation: BAE27216.1 .
CH466532 Genomic DNA. Translation: EDL12402.1 .
BC049094 mRNA. Translation: AAH49094.1 .
BC051023 mRNA. Translation: AAH51023.1 .
CCDSi CCDS17781.1.
RefSeqi NP_031927.2. NM_007901.5.
UniGenei Mm.982.

3D structure databases

ProteinModelPortali O08530.
SMRi O08530. Positions 16-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199373. 2 interactions.
DIPi DIP-32248N.
IntActi O08530. 1 interaction.

Chemistry

BindingDBi O08530.
ChEMBLi CHEMBL1914262.
GuidetoPHARMACOLOGYi 275.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei O08530.

Proteomic databases

PaxDbi O08530.
PRIDEi O08530.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055676 ; ENSMUSP00000050897 ; ENSMUSG00000045092 .
GeneIDi 13609.
KEGGi mmu:13609.
UCSCi uc008rbo.2. mouse.

Organism-specific databases

CTDi 1901.
MGIi MGI:1096355. S1pr1.

Phylogenomic databases

eggNOGi NOG148018.
GeneTreei ENSGT00760000118804.
HOGENOMi HOG000233501.
HOVERGENi HBG103071.
InParanoidi O08530.
KOi K04288.
OMAi SAFIACW.
OrthoDBi EOG708W0B.
TreeFami TF330052.

Miscellaneous databases

NextBioi 284254.
PROi O08530.
SOURCEi Search...

Gene expression databases

Bgeei O08530.
ExpressionAtlasi O08530. baseline and differential.
Genevestigatori O08530.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR000987. EDG1_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004061. S1P_rcpt.
[Graphical view ]
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00642. EDG1RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01523. S1PRECEPTOR.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse gene for the inducible G-protein-coupled receptor edg-1."
    Liu C.H., Hla T.
    Genomics 43:15-24(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
    Tissue: Liver.
  2. "Comparative analysis of three murine G-protein coupled receptors activated by sphingosine-1-phosphate."
    Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.
    Gene 227:89-99(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart and Lung.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: C57BL/6.
    Tissue: Eye.
  6. "Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is essential for vascular maturation."
    Liu Y., Wada R., Yamashita T., Mi Y., Deng C.X., Hobson J.P., Rosenfeldt H.M., Nava V.E., Chae S.S., Lee M.J., Liu C.H., Hla T., Spiegel S., Proia R.L.
    J. Clin. Invest. 106:951-961(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION AND CHEMOTAXIS, TISSUE SPECIFICITY.
  7. "EDG-1 links the PDGF receptor to Src and focal adhesion kinase activation leading to lamellipodia formation and cell migration."
    Rosenfeldt H.M., Hobson J.P., Maceyka M., Olivera A., Nava V.E., Milstien S., Spiegel S.
    FASEB J. 15:2649-2659(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FIBROBLAST CHEMOTAXIS, DISRUPTION PHENOTYPE.
  8. "Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell motility."
    Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S., Caron M.G., Milstien S., Spiegel S.
    Science 291:1800-1803(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "G-protein-coupled receptor S1P1 acts within endothelial cells to regulate vascular maturation."
    Allende M.L., Yamashita T., Proia R.L.
    Blood 102:3665-3667(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION.
  10. "Expression of the sphingosine 1-phosphate receptor, S1P1, on T-cells controls thymic emigration."
    Allende M.L., Dreier J.L., Mandala S., Proia R.L.
    J. Biol. Chem. 279:15396-15401(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T CELL MIGRATION.
  11. "Lymphocyte egress from thymus and peripheral lymphoid organs is dependent on S1P receptor 1."
    Matloubian M., Lo C.G., Cinamon G., Lesneski M.J., Xu Y., Brinkmann V., Allende M.L., Proia R.L., Cyster J.G.
    Nature 427:355-360(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN T CELL MIGRATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Akt-mediated transactivation of the S1P1 receptor in caveolin-enriched microdomains regulates endothelial barrier enhancement by oxidized phospholipids."
    Singleton P.A., Chatchavalvanich S., Fu P., Xing J., Birukova A.A., Fortune J.A., Klibanov A.M., Garcia J.G., Birukov K.G.
    Circ. Res. 104:978-986(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Sphingosine-1-phosphate mobilizes osteoclast precursors and regulates bone homeostasis."
    Ishii M., Egen J.G., Klauschen F., Meier-Schellersheim M., Saeki Y., Vacher J., Proia R.L., Germain R.N.
    Nature 458:524-528(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN OSTEOCLAST MIGRATION AND BONE HOMEOSTASIS.
  15. "The Sphingosine-1-phospate receptor 1 mediates S1P action during cardiac development."
    Poulsen R.R., McClaskey C.M., Rivkees S.A., Wendler C.C.
    BMC Dev. Biol. 11:37-37(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN HEART MORPHOGENESIS AND DEVELOPMENT.
  16. "S1P1 inhibits sprouting angiogenesis during vascular development."
    Ben Shoham A., Malkinson G., Krief S., Shwartz Y., Ely Y., Ferrara N., Yaniv K., Zelzer E.
    Development 139:3859-3869(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN SPROUTING ANGIOGENESIS.
  17. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2 AND LYS-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiS1PR1_MOUSE
AccessioniPrimary (citable) accession number: O08530
Secondary accession number(s): Q9DC35, Q9R235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3