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Protein

Sphingosine 1-phosphate receptor 1

Gene

S1PR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (By similarity). 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.By similarity8 Publications

GO - Molecular functioni

  • G-protein coupled receptor activity Source: ProtInc
  • G-protein coupled receptor binding Source: UniProtKB
  • sphingolipid binding Source: Ensembl
  • sphingosine-1-phosphate receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Angiogenesis, Chemotaxis

Enzyme and pathway databases

ReactomeiR-HSA-418594. G alpha (i) signalling events.
R-HSA-419408. Lysosphingolipid and LPA receptors.
SignaLinkiP21453.
SIGNORiP21453.

Protein family/group databases

TCDBi9.A.14.2.1. the g-protein-coupled receptor (gpcr) family.

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
Sphingosine 1-phosphate receptor Edg-1
Short name:
S1P receptor Edg-1
CD_antigen: CD363
Gene namesi
Name:S1PR1
Synonyms:CHEDG1, EDG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3165. S1PR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4645Extracellular1 PublicationAdd
BLAST
Transmembranei47 – 6822Helical; Name=1Add
BLAST
Topological domaini69 – 8214Cytoplasmic1 PublicationAdd
BLAST
Transmembranei83 – 10422Helical; Name=2Add
BLAST
Topological domaini105 – 11612Extracellular1 PublicationAdd
BLAST
Transmembranei117 – 13822Helical; Name=3Add
BLAST
Topological domaini139 – 16022Cytoplasmic1 PublicationAdd
BLAST
Transmembranei161 – 18222Helical; Name=4Add
BLAST
Topological domaini183 – 19614Extracellular1 PublicationAdd
BLAST
Transmembranei197 – 22428Helical; Name=5Add
BLAST
Topological domaini225 – 25733Cytoplasmic1 PublicationAdd
BLAST
Transmembranei258 – 27821Helical; Name=6Add
BLAST
Topological domaini279 – 28911Extracellular1 PublicationAdd
BLAST
Transmembranei290 – 31021Helical; Name=7Add
BLAST
Topological domaini311 – 38272Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201R → A: Drastically reduced affinity for sphingosine 1-phosphate. 1 Publication
Mutagenesisi121 – 1211E → A: Drastically reduced affinity for sphingosine 1-phosphate. 1 Publication
Mutagenesisi121 – 1211E → Q: Slight activation of the receptor at maximal ligand concentration. 1 Publication
Mutagenesisi210 – 2101F → L: Impairs sphingosine 1-phosphate binding and signaling. 1 Publication
Mutagenesisi236 – 2361T → A: Acts as a dominant negative GPCR and inhibits S1P-induced Rac activation, chemotaxis, and angiogenesis. 1 Publication
Mutagenesisi265 – 2651F → L: Impairs sphingosine 1-phosphate binding and signaling. 1 Publication
Mutagenesisi269 – 2691W → F or L: Impairs sphingosine 1-phosphate binding and signaling. 1 Publication
Mutagenesisi292 – 2921R → A or V: Drastically reduced affinity for sphingosine 1-phosphate. 1 Publication

Organism-specific databases

PharmGKBiPA162402344.

Chemistry

ChEMBLiCHEMBL2363041.
GuidetoPHARMACOLOGYi275.

Polymorphism and mutation databases

BioMutaiS1PR1.
DMDMi205371820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 382381Sphingosine 1-phosphate receptor 1PRO_0000069412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101N6-acetyllysineBy similarity
Glycosylationi30 – 301N-linked (GlcNAc...)2 Publications
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi184 ↔ 191PROSITE-ProRule annotation1 Publication
Modified residuei236 – 2361Phosphothreonine; by PKB/AKT11 Publication
Disulfide bondi282 ↔ 287PROSITE-ProRule annotation1 Publication
Lipidationi328 – 3281S-palmitoyl cysteineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity
Modified residuei353 – 3531PhosphoserineSequence analysis

Post-translational modificationi

S1P-induced endothelial cell migration requires the PKB/AKT1-mediated phosphorylation of the third intracellular loop at the Thr-236 residue.2 Publications

Keywords - PTMi

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

Proteomic databases

EPDiP21453.
PaxDbiP21453.
PeptideAtlasiP21453.
PRIDEiP21453.

PTM databases

iPTMnetiP21453.
PhosphoSiteiP21453.
SwissPalmiP21453.

Expressioni

Tissue specificityi

Endothelial cells, and to a lesser extent, in vascular smooth muscle cells, fibroblasts, melanocytes, and cells of epithelioid origin.

Inductioni

By the tumor promoter phorbol 12-myristate 13-acetate (PMA) in the presence of cycloheximide.

Gene expression databases

BgeeiP21453.
CleanExiHS_S1PR1.
GenevisibleiP21453. HS.

Organism-specific databases

HPAiCAB010104.

Interactioni

Subunit structurei

Interacts with GNAI1 and GNAI3.2 Publications

GO - Molecular functioni

  • G-protein coupled receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108225. 29 interactions.
DIPiDIP-60427N.
IntActiP21453. 3 interactions.
STRINGi9606.ENSP00000305416.

Chemistry

BindingDBiP21453.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 319Combined sources
Helixi36 – 394Combined sources
Helixi42 – 7231Combined sources
Helixi74 – 763Combined sources
Helixi79 – 10426Combined sources
Helixi106 – 1094Combined sources
Helixi114 – 14633Combined sources
Helixi158 – 17619Combined sources
Turni177 – 1815Combined sources
Helixi188 – 1903Combined sources
Beta strandi193 – 1953Combined sources
Helixi200 – 23132Combined sources
Turni247 – 2493Combined sources
Helixi251 – 28030Combined sources
Turni284 – 2863Combined sources
Turni289 – 2913Combined sources
Helixi294 – 3029Combined sources
Helixi303 – 3053Combined sources
Helixi307 – 3148Combined sources
Helixi316 – 3227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V2WX-ray3.35A2-231[»]
A244-326[»]
3V2YX-ray2.80A2-231[»]
A244-326[»]
ProteinModelPortaliP21453.
SMRiP21453. Positions 16-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIA7. Eukaryota.
ENOG410XQD3. LUCA.
GeneTreeiENSGT00760000118804.
HOGENOMiHOG000233501.
HOVERGENiHBG103071.
InParanoidiP21453.
KOiK04288.
OMAiIGGMEFS.
OrthoDBiEOG708W0B.
PhylomeDBiP21453.
TreeFamiTF330052.

Family and domain databases

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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
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.

P21453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPTSVPLVK AHRSSVSDYV NYDIIVRHYN YTGKLNISAD KENSIKLTSV
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
LHNGSNNFRL FLLISACWVI SLILGGLPIM GWNCISALSS CSTVLPLYHK
210 220 230 240 250
HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN ISKASRSSEK
260 270 280 290 300
SLALLKTVII VLSVFIACWA PLFILLLLDV GCKVKTCDIL FRAEYFLVLA
310 320 330 340 350
VLNSGTNPII YTLTNKEMRR AFIRIMSCCK CPSGDSAGKF KRPIIAGMEF
360 370 380
SRSKSDNSSH PQKDEGDNPE TIMSSGNVNS SS
Length:382
Mass (Da):42,811
Last modified:September 2, 2008 - v2
Checksum:i0CCE8685A5E1BAD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2523KSL → NV in AAA52336 (PubMed:2160972).Curated
Sequence conflicti250 – 2523KSL → NV in AAC51905 (PubMed:9409733).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151S → L.
Corresponds to variant rs4987250 [ dbSNP | Ensembl ].
VAR_046158
Natural varianti115 – 1151A → T.
Corresponds to variant rs11542632 [ dbSNP | Ensembl ].
VAR_046159
Natural varianti332 – 3321P → R.
Corresponds to variant rs7549921 [ dbSNP | Ensembl ].
VAR_046160

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31210 mRNA. Translation: AAA52336.1.
AF022137 mRNA. Translation: AAC51905.1.
AF233365 mRNA. Translation: AAF43420.1.
AK312493 mRNA. Translation: BAG35395.1.
CR541786 mRNA. Translation: CAG46585.1.
CR542269 mRNA. Translation: CAG47065.1.
AL109741 Genomic DNA. Translation: CAI21861.1.
CH471097 Genomic DNA. Translation: EAW72927.1.
CH471097 Genomic DNA. Translation: EAW72928.1.
BC018650 mRNA. Translation: AAH18650.1.
CCDSiCCDS777.1.
PIRiA35300.
RefSeqiNP_001307659.1. NM_001320730.1.
NP_001391.2. NM_001400.4.
UniGeneiHs.154210.

Genome annotation databases

EnsembliENST00000305352; ENSP00000305416; ENSG00000170989.
GeneIDi1901.
KEGGihsa:1901.
UCSCiuc001dud.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31210 mRNA. Translation: AAA52336.1.
AF022137 mRNA. Translation: AAC51905.1.
AF233365 mRNA. Translation: AAF43420.1.
AK312493 mRNA. Translation: BAG35395.1.
CR541786 mRNA. Translation: CAG46585.1.
CR542269 mRNA. Translation: CAG47065.1.
AL109741 Genomic DNA. Translation: CAI21861.1.
CH471097 Genomic DNA. Translation: EAW72927.1.
CH471097 Genomic DNA. Translation: EAW72928.1.
BC018650 mRNA. Translation: AAH18650.1.
CCDSiCCDS777.1.
PIRiA35300.
RefSeqiNP_001307659.1. NM_001320730.1.
NP_001391.2. NM_001400.4.
UniGeneiHs.154210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V2WX-ray3.35A2-231[»]
A244-326[»]
3V2YX-ray2.80A2-231[»]
A244-326[»]
ProteinModelPortaliP21453.
SMRiP21453. Positions 16-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108225. 29 interactions.
DIPiDIP-60427N.
IntActiP21453. 3 interactions.
STRINGi9606.ENSP00000305416.

Chemistry

BindingDBiP21453.
ChEMBLiCHEMBL2363041.
GuidetoPHARMACOLOGYi275.

Protein family/group databases

TCDBi9.A.14.2.1. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

iPTMnetiP21453.
PhosphoSiteiP21453.
SwissPalmiP21453.

Polymorphism and mutation databases

BioMutaiS1PR1.
DMDMi205371820.

Proteomic databases

EPDiP21453.
PaxDbiP21453.
PeptideAtlasiP21453.
PRIDEiP21453.

Protocols and materials databases

DNASUi1901.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305352; ENSP00000305416; ENSG00000170989.
GeneIDi1901.
KEGGihsa:1901.
UCSCiuc001dud.3. human.

Organism-specific databases

CTDi1901.
GeneCardsiS1PR1.
HGNCiHGNC:3165. S1PR1.
HPAiCAB010104.
MIMi601974. gene.
neXtProtiNX_P21453.
PharmGKBiPA162402344.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIA7. Eukaryota.
ENOG410XQD3. LUCA.
GeneTreeiENSGT00760000118804.
HOGENOMiHOG000233501.
HOVERGENiHBG103071.
InParanoidiP21453.
KOiK04288.
OMAiIGGMEFS.
OrthoDBiEOG708W0B.
PhylomeDBiP21453.
TreeFamiTF330052.

Enzyme and pathway databases

ReactomeiR-HSA-418594. G alpha (i) signalling events.
R-HSA-419408. Lysosphingolipid and LPA receptors.
SignaLinkiP21453.
SIGNORiP21453.

Miscellaneous databases

GeneWikiiS1PR1.
GenomeRNAii1901.
PROiP21453.
SOURCEiSearch...

Gene expression databases

BgeeiP21453.
CleanExiHS_S1PR1.
GenevisibleiP21453. HS.

Family and domain databases

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.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors."
    Hla T., Maciag T.
    J. Biol. Chem. 265:9308-9313(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Umbilical vein endothelial cell.
  2. "Identification of cDNAs encoding two G protein-coupled receptors for lysosphingolipids."
    An S., Bleu T., Huang W., Hallmark O.G., Coughlin S.R., Goetzl E.J.
    FEBS Lett. 417:279-282(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-120; GLU-121 AND ARG-292.
  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].
    Tissue: Substantia nigra.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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].
    Tissue: Lung.
  9. "The inducible G protein-coupled receptor edg-1 signals via the G(i)/mitogen-activated protein kinase pathway."
    Lee M.-J., Evans M., Hla T.
    J. Biol. Chem. 271:11272-11279(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GNAI1 AND GNAI3.
  10. "Sphingosine-1-phosphate as a ligand for the G protein-coupled receptor EDG-1."
    Lee M.-J., Van Brocklyn J.R., Thangada S., Liu C.H., Hand A.R., Menzeleev R., Spiegel S., Hla T.
    Science 279:1552-1555(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Differential pharmacological properties and signal transduction of the sphingosine 1-phosphate receptors EDG-1, EDG-3, and EDG-5."
    Ancellin N., Hla T.
    J. Biol. Chem. 274:18997-19002(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHARMACOLOGICAL CHARACTERIZATION.
  12. "A single amino acid determines lysophospholipid specificity of the S1P1 (EDG1) and LPA1 (EDG2) phospholipid growth factor receptors."
    Wang D.A., Lorincz Z., Bautista D.L., Liliom K., Tigyi G., Parrill A.L.
    J. Biol. Chem. 276:49213-49220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Akt-mediated phosphorylation of the G protein-coupled receptor EDG-1 is required for endothelial cell chemotaxis."
    Lee M.-J., Thangada S., Paik J.-H., Sapkota G.P., Ancellin N., Chae S.-S., Wu M., Morales-Ruiz M., Sessa W.C., Alessi D.R., Hla T.
    Mol. Cell 8:693-704(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CHEMOTAXIS, PHOSPHORYLATION AT THR-236, MUTAGENESIS OF THR-236.
  14. "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.
  15. "Roles for N-glycosylation in the dynamics of Edg-1/S1P1 in sphingosine 1-phosphate-stimulated cells."
    Kohno T., Igarashi Y.
    Glycoconj. J. 21:497-501(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-30.
  16. "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, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-326 IN COMPLEX WITH SPHINGOLIPID ANALOG, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, MUTAGENESIS OF PHE-210; PHE-265 AND TRP-269, GLYCOSYLATION AT ASN-30, DISULFIDE BONDS.

Entry informationi

Entry nameiS1PR1_HUMAN
AccessioniPrimary (citable) accession number: P21453
Secondary accession number(s): D3DT66, Q9BYY4, Q9NYN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: September 2, 2008
Last modified: July 6, 2016
This is version 164 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.