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Protein

Thromboxane A2 receptor

Gene

TBXA2R

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

Functioni

Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C. Isoform 1 activates adenylyl cyclase. Isoform 2 inhibits adenylyl cyclase.1 Publication

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: Reactome
  • thromboxane A2 receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_18425. Prostanoid ligand receptors.
REACT_20647. Thromboxane signalling through TP receptor.
SignaLinkiP21731.

Names & Taxonomyi

Protein namesi
Recommended name:
Thromboxane A2 receptor
Short name:
TXA2-R
Alternative name(s):
Prostanoid TP receptor
Gene namesi
Name:TBXA2R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11608. TBXA2R.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929ExtracellularSequence AnalysisAdd
BLAST
Transmembranei30 – 5223Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini53 – 6614CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei67 – 8721Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini88 – 10619ExtracellularSequence AnalysisAdd
BLAST
Transmembranei107 – 12822Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini129 – 14921CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei150 – 17223Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini173 – 19321ExtracellularSequence AnalysisAdd
BLAST
Transmembranei194 – 21926Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini220 – 24627CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei247 – 27024Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini271 – 28919ExtracellularSequence AnalysisAdd
BLAST
Transmembranei290 – 31122Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini312 – 34332CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • cytosol Source: GOC
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Bleeding disorder, platelet-type 13 (BDPLT13)1 Publication

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by reduced platelet aggregation and a tendency to mild mucocutaneous bleeding.

See also OMIM:614009
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → L in BDPLT13; does not affect TXA2 binding; defective interaction with G proteins; impairs phospholipase C and adenylyl cyclase activation; isoform 1; has no effect on adenylyl cyclase inhibition; isoform 2. 2 Publications
Corresponds to variant rs34377097 [ dbSNP | Ensembl ].
VAR_003515

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911L → R: Suppresses antagonist binding. 1 Publication
Mutagenesisi295 – 2951R → Q: Reduces antagonist binding. 1 Publication
Mutagenesisi299 – 2991W → L: Reduces antagonist binding. 1 Publication
Mutagenesisi299 – 2991W → R: Reduces antagonist binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614009. phenotype.
Orphaneti220443. Bleeding diathesis due to thromboxane synthesis deficiency.
PharmGKBiPA348.

Chemistry

DrugBankiDB01207. Ridogrel.

Polymorphism and mutation databases

BioMutaiTBXA2R.
DMDMi229463010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343Thromboxane A2 receptorPRO_0000070138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)
Glycosylationi16 – 161N-linked (GlcNAc...)
Disulfide bondi105 ↔ 183PROSITE-ProRule annotation
Modified residuei329 – 3291Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP21731.
PRIDEiP21731.

PTM databases

PhosphoSiteiP21731.

Expressioni

Gene expression databases

BgeeiP21731.
CleanExiHS_TBXA2R.
ExpressionAtlasiP21731. baseline and differential.
GenevisibleiP21731. HS.

Interactioni

Subunit structurei

Interacts with RPGRIP1L. Interacts with PSMA3. Interacts with GNB2L1/RACK1; the interaction regulates TBXA2R cell surface expression.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRDX4Q131623EBI-2625082,EBI-2211957

Protein-protein interaction databases

BioGridi112777. 35 interactions.
DIPiDIP-41465N.
IntActiP21731. 4 interactions.
MINTiMINT-1512445.
STRINGi9606.ENSP00000393333.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBNmodel-A100-265[»]
ProteinModelPortaliP21731.
SMRiP21731. Positions 66-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG263172.
GeneTreeiENSGT00760000119188.
HOGENOMiHOG000015238.
HOVERGENiHBG108543.
InParanoidiP21731.
KOiK04264.
OMAiLCHFMGV.
OrthoDBiEOG7TBC2R.
PhylomeDBiP21731.
TreeFamiTF324982.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR008365. Prostanoid_rcpt.
IPR001105. Thbox_rcpt.
[Graphical view]
PANTHERiPTHR11866. PTHR11866. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01788. PROSTANOIDR.
PR00429. THROMBOXANER.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P21731-3) [UniParc]FASTAAdd to basket

Also known as: Alpha

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
MWPNGSSLGP CFRPTNITLE ERRLIASPWF AASFCVVGLA SNLLALSVLA
60 70 80 90 100
GARQGGSHTR SSFLTFLCGL VLTDFLGLLV TGTIVVSQHA ALFEWHAVDP
110 120 130 140 150
GCRLCRFMGV VMIFFGLSPL LLGAAMASER YLGITRPFSR PAVASQRRAW
160 170 180 190 200
ATVGLVWAAA LALGLLPLLG VGRYTVQYPG SWCFLTLGAE SGDVAFGLLF
210 220 230 240 250
SMLGGLSVGL SFLLNTVSVA TLCHVYHGQE AAQQRPRDSE VEMMAQLLGI
260 270 280 290 300
MVVASVCWLP LLVFIAQTVL RNPPAMSPAG QLSRTTEKEL LIYLRVATWN
310 320 330 340
QILDPWVYIL FRRAVLRRLQ PRLSTRPRSL SLQPQLTQRS GLQ
Length:343
Mass (Da):37,431
Last modified:May 5, 2009 - v3
Checksum:i114A7C3F3F0D35F1
GO
Isoform 2 (identifier: P21731-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     329-343: SLSLQPQLTQRSGLQ → RSLTLWPSLE...PTGKALSRKD

Show »
Length:407
Mass (Da):44,205
Checksum:i461D60349704E7AB
GO

Sequence cautioni

The sequence AAA58957.1 differs from that shown. Reason: Frameshift at position 329. Curated
Isoform 2 : The sequence AAA58957.1 differs from that shown. Reason: Frameshift at positions 330 and 386. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti263 – 2631V → W AA sequence (PubMed:1825698).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → L in BDPLT13; does not affect TXA2 binding; defective interaction with G proteins; impairs phospholipase C and adenylyl cyclase activation; isoform 1; has no effect on adenylyl cyclase inhibition; isoform 2. 2 Publications
Corresponds to variant rs34377097 [ dbSNP | Ensembl ].
VAR_003515
Natural varianti68 – 681C → S.
Corresponds to variant rs5743 [ dbSNP | Ensembl ].
VAR_014688
Natural varianti80 – 801V → E.
Corresponds to variant rs5744 [ dbSNP | Ensembl ].
VAR_014689
Natural varianti94 – 941E → V.
Corresponds to variant rs5746 [ dbSNP | Ensembl ].
VAR_014690
Natural varianti160 – 1601A → T.
Corresponds to variant rs5749 [ dbSNP | Ensembl ].
VAR_014691
Natural varianti176 – 1761V → E.
Corresponds to variant rs5750 [ dbSNP | Ensembl ].
VAR_014692
Natural varianti217 – 2171V → I.
Corresponds to variant rs5751 [ dbSNP | Ensembl ].
VAR_014693

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei329 – 34315SLSLQ…RSGLQ → RSLTLWPSLEYSGTISAHCN LRLPGSSDSRASASRAAGIT GVSHCARPCMLFDPEFDLLA GVQLLPFEPPTGKALSRKD in isoform 2. 2 PublicationsVSP_001925Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38081 mRNA. Translation: BAA07274.1.
D15056 Genomic DNA. Translation: BAA03649.1.
U11271 mRNA. Translation: AAA58957.1. Frameshift.
U27325 mRNA. Translation: AAA68608.1.
AY429110 mRNA. Translation: AAR07905.1.
DQ268653 Genomic DNA. Translation: ABB72549.1.
AC005175 Genomic DNA. Translation: AAC24302.1.
AC005175 Genomic DNA. Translation: AAC24303.1.
CH471139 Genomic DNA. Translation: EAW69301.1.
BC074749 mRNA. Translation: AAH74749.1.
BC074750 mRNA. Translation: AAH74750.1.
CCDSiCCDS42467.1. [P21731-3]
CCDS54198.1. [P21731-2]
PIRiA49117.
A53959.
A56194.
T02670.
RefSeqiNP_001051.1. NM_001060.5. [P21731-3]
NP_963998.2. NM_201636.2. [P21731-2]
XP_011526516.1. XM_011528214.1. [P21731-3]
UniGeneiHs.442530.

Genome annotation databases

EnsembliENST00000375190; ENSP00000364336; ENSG00000006638.
ENST00000411851; ENSP00000393333; ENSG00000006638. [P21731-2]
GeneIDi6915.
KEGGihsa:6915.
UCSCiuc002lyg.2. human. [P21731-3]
uc021umv.1. human. [P21731-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38081 mRNA. Translation: BAA07274.1.
D15056 Genomic DNA. Translation: BAA03649.1.
U11271 mRNA. Translation: AAA58957.1. Frameshift.
U27325 mRNA. Translation: AAA68608.1.
AY429110 mRNA. Translation: AAR07905.1.
DQ268653 Genomic DNA. Translation: ABB72549.1.
AC005175 Genomic DNA. Translation: AAC24302.1.
AC005175 Genomic DNA. Translation: AAC24303.1.
CH471139 Genomic DNA. Translation: EAW69301.1.
BC074749 mRNA. Translation: AAH74749.1.
BC074750 mRNA. Translation: AAH74750.1.
CCDSiCCDS42467.1. [P21731-3]
CCDS54198.1. [P21731-2]
PIRiA49117.
A53959.
A56194.
T02670.
RefSeqiNP_001051.1. NM_001060.5. [P21731-3]
NP_963998.2. NM_201636.2. [P21731-2]
XP_011526516.1. XM_011528214.1. [P21731-3]
UniGeneiHs.442530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBNmodel-A100-265[»]
ProteinModelPortaliP21731.
SMRiP21731. Positions 66-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112777. 35 interactions.
DIPiDIP-41465N.
IntActiP21731. 4 interactions.
MINTiMINT-1512445.
STRINGi9606.ENSP00000393333.

Chemistry

BindingDBiP21731.
ChEMBLiCHEMBL2069.
DrugBankiDB01207. Ridogrel.
GuidetoPHARMACOLOGYi346.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP21731.

Polymorphism and mutation databases

BioMutaiTBXA2R.
DMDMi229463010.

Proteomic databases

PaxDbiP21731.
PRIDEiP21731.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375190; ENSP00000364336; ENSG00000006638.
ENST00000411851; ENSP00000393333; ENSG00000006638. [P21731-2]
GeneIDi6915.
KEGGihsa:6915.
UCSCiuc002lyg.2. human. [P21731-3]
uc021umv.1. human. [P21731-2]

Organism-specific databases

CTDi6915.
GeneCardsiGC19M003594.
H-InvDBHIX0202922.
HGNCiHGNC:11608. TBXA2R.
MIMi188070. gene.
614009. phenotype.
neXtProtiNX_P21731.
Orphaneti220443. Bleeding diathesis due to thromboxane synthesis deficiency.
PharmGKBiPA348.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263172.
GeneTreeiENSGT00760000119188.
HOGENOMiHOG000015238.
HOVERGENiHBG108543.
InParanoidiP21731.
KOiK04264.
OMAiLCHFMGV.
OrthoDBiEOG7TBC2R.
PhylomeDBiP21731.
TreeFamiTF324982.

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_18407. G alpha (12/13) signalling events.
REACT_18425. Prostanoid ligand receptors.
REACT_20647. Thromboxane signalling through TP receptor.
SignaLinkiP21731.

Miscellaneous databases

ChiTaRSiTBXA2R. human.
GeneWikiiThromboxane_receptor.
GenomeRNAii6915.
NextBioi27045.
PROiP21731.
SOURCEiSearch...

Gene expression databases

BgeeiP21731.
CleanExiHS_TBXA2R.
ExpressionAtlasiP21731. baseline and differential.
GenevisibleiP21731. HS.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR008365. Prostanoid_rcpt.
IPR001105. Thbox_rcpt.
[Graphical view]
PANTHERiPTHR11866. PTHR11866. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01788. PROSTANOIDR.
PR00429. THROMBOXANER.
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. "Cloning and expression of cDNA for a human thromboxane A2 receptor."
    Hirata M., Hayashi Y., Ushikubi F., Yokota Y., Kageyama R., Nakanishi S., Narumiya S.
    Nature 349:617-620(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Placenta.
  2. "Characterization and chromosomal mapping of the human thromboxane A2 receptor gene."
    Nuesing R.M., Hirata M., Kakizuka A., Eki T., Ozawa K., Narumiya S.
    J. Biol. Chem. 268:25253-25259(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "Alternative splicing produces a divergent cytoplasmic tail in the human endothelial thromboxane A2 receptor."
    Raychowdhury M.K., Yukawa M., Collins L.J., McGrail S.H., Kent K.C., Ware J.A.
    J. Biol. Chem. 269:19256-19261(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    Tissue: Endothelial cell and Placenta.
  4. "Cloning and pharmacologic characterization of a thromboxane A2 receptor from K562 (human chronic myelogenous leukemia) cells."
    D'Angelo D.D., Davis M.G., Ali S., Dorn G.W. II
    J. Pharmacol. Exp. Ther. 271:1034-1041(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  6. NIEHS SNPs program
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Lung.
  10. "Two thromboxane A2 receptor isoforms in human platelets. Opposite coupling to adenylyl cyclase with different sensitivity to Arg60 to Leu mutation."
    Hirata T., Ushikubi F., Kakizuka A., Okuma M., Narumiya S.
    J. Clin. Invest. 97:949-956(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 329-343 (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT BDPLT13 LEU-60.
    Tissue: Platelet.
  11. "Point mutation in the seventh hydrophobic domain of the human thromboxane A2 receptor allows discrimination between agonist and antagonist binding sites."
    Funk C.D., Furci L., Moran N., Fitzgerald G.A.
    Mol. Pharmacol. 44:934-939(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  12. "Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes."
    Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N.
    Prostaglandins Other Lipid Mediat. 83:237-249(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMA3.
  13. "RACK1 regulates the cell surface expression of the G protein-coupled receptor for thromboxane A(2)."
    Parent A., Laroche G., Hamelin E., Parent J.L.
    Traffic 9:394-407(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  14. "Thromboxane A2-induced signal transduction is negatively regulated by KIAA1005 that directly interacts with thromboxane A2 receptor."
    Tokue S., Sasaki M., Nakahata N.
    Prostaglandins Other Lipid Mediat. 89:8-15(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPGRIP1L.
  15. "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-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Arg60 to Leu mutation of the human thromboxane A2 receptor in a dominantly inherited bleeding disorder."
    Hirata T., Kakizuka A., Ushikubi F., Fuse I., Okuma M., Narumiya S.
    J. Clin. Invest. 94:1662-1667(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BDPLT13 LEU-60, CHARACTERIZATION OF VARIANT BDPLT13 LEU-60.

Entry informationi

Entry nameiTA2R_HUMAN
AccessioniPrimary (citable) accession number: P21731
Secondary accession number(s): O75228
, Q6DK52, Q9UCY1, Q9UCY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 5, 2009
Last modified: July 22, 2015
This is version 166 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.