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P21731

- TA2R_HUMAN

UniProt

P21731 - TA2R_HUMAN

Protein

Thromboxane A2 receptor

Gene

TBXA2R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (05 May 2009)
      Previous versions | rss
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    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

    1. guanyl-nucleotide exchange factor activity Source: Reactome
    2. protein binding Source: UniProtKB
    3. thromboxane A2 receptor activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. G-protein coupled receptor signaling pathway Source: ProtInc
    3. inflammatory response Source: Ensembl
    4. platelet activation Source: Reactome
    5. positive regulation of angiogenesis Source: Ensembl
    6. positive regulation of blood pressure Source: Ensembl
    7. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    8. positive regulation of GTPase activity Source: GOC
    9. positive regulation of smooth muscle contraction Source: Ensembl
    10. positive regulation of vasoconstriction Source: Ensembl
    11. response to drug Source: Ensembl
    12. response to lipopolysaccharide Source: Ensembl
    13. response to nutrient Source: Ensembl
    14. second-messenger-mediated signaling Source: Ensembl
    15. thromboxane A2 signaling pathway Source: GOC

    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: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:11608. TBXA2R.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Bleeding disorder, platelet-type 13 (BDPLT13) [MIM:614009]: A disorder characterized by reduced platelet aggregation and a tendency to mild mucocutaneous bleeding.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    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. 1 Publication
    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.

    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

    ArrayExpressiP21731.
    BgeeiP21731.
    CleanExiHS_TBXA2R.
    GenevestigatoriP21731.

    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.ENSP00000364336.

    Structurei

    Secondary structure

    1
    343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi101 – 13434
    Beta strandi138 – 1403
    Turni145 – 1473
    Helixi148 – 16417
    Helixi166 – 1683
    Beta strandi174 – 1774
    Turni178 – 1814
    Beta strandi182 – 1854
    Helixi192 – 1943
    Helixi196 – 20611
    Helixi209 – 22214
    Beta strandi223 – 2286
    Turni236 – 2383
    Helixi239 – 25517
    Helixi256 – 2583
    Helixi259 – 2646

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2929ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini53 – 6614CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini88 – 10619ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini129 – 14921CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini173 – 19321ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini220 – 24627CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini271 – 28919ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini312 – 34332CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei30 – 5223Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei67 – 8721Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei107 – 12822Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei150 – 17223Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei194 – 21926Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei247 – 27024Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei290 – 31122Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG263172.
    HOGENOMiHOG000015238.
    HOVERGENiHBG108543.
    KOiK04264.
    OMAiATLCRVY.
    OrthoDBiEOG7TBC2R.
    PhylomeDBiP21731.
    TreeFamiTF324982.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    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. Align

    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

    MWPNGSSLGP CFRPTNITLE ERRLIASPWF AASFCVVGLA SNLLALSVLA    50
    GARQGGSHTR SSFLTFLCGL VLTDFLGLLV TGTIVVSQHA ALFEWHAVDP 100
    GCRLCRFMGV VMIFFGLSPL LLGAAMASER YLGITRPFSR PAVASQRRAW 150
    ATVGLVWAAA LALGLLPLLG VGRYTVQYPG SWCFLTLGAE SGDVAFGLLF 200
    SMLGGLSVGL SFLLNTVSVA TLCHVYHGQE AAQQRPRDSE VEMMAQLLGI 250
    MVVASVCWLP LLVFIAQTVL RNPPAMSPAG QLSRTTEKEL LIYLRVATWN 300
    QILDPWVYIL FRRAVLRRLQ PRLSTRPRSL SLQPQLTQRS GLQ 343
    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.
    Isoform 2 : The sequence AAA58957.1 differs from that shown. Reason: Frameshift at positions 330 and 386.

    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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.442530.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi229463010.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS42467.1. [P21731-3 ]
    CCDS54198.1. [P21731-2 ]
    PIRi A49117.
    A53959.
    A56194.
    T02670.
    RefSeqi NP_001051.1. NM_001060.5. [P21731-3 ]
    NP_963998.2. NM_201636.2. [P21731-2 ]
    UniGenei Hs.442530.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LBN model - A 100-265 [» ]
    ProteinModelPortali P21731.
    SMRi P21731. Positions 66-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112777. 35 interactions.
    DIPi DIP-41465N.
    IntActi P21731. 4 interactions.
    MINTi MINT-1512445.
    STRINGi 9606.ENSP00000364336.

    Chemistry

    BindingDBi P21731.
    ChEMBLi CHEMBL2069.
    DrugBanki DB01207. Ridogrel.
    GuidetoPHARMACOLOGYi 346.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P21731.

    Polymorphism databases

    DMDMi 229463010.

    Proteomic databases

    PaxDbi P21731.
    PRIDEi P21731.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375190 ; ENSP00000364336 ; ENSG00000006638 . [P21731-3 ]
    ENST00000411851 ; ENSP00000393333 ; ENSG00000006638 . [P21731-2 ]
    GeneIDi 6915.
    KEGGi hsa:6915.
    UCSCi uc002lyg.2. human. [P21731-3 ]
    uc021umv.1. human. [P21731-2 ]

    Organism-specific databases

    CTDi 6915.
    GeneCardsi GC19M003594.
    H-InvDB HIX0202922.
    HGNCi HGNC:11608. TBXA2R.
    MIMi 188070. gene.
    614009. phenotype.
    neXtProti NX_P21731.
    Orphaneti 220443. Bleeding diathesis due to thromboxane synthesis deficiency.
    PharmGKBi PA348.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263172.
    HOGENOMi HOG000015238.
    HOVERGENi HBG108543.
    KOi K04264.
    OMAi ATLCRVY.
    OrthoDBi EOG7TBC2R.
    PhylomeDBi P21731.
    TreeFami TF324982.

    Enzyme and pathway databases

    Reactomei REACT_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.
    SignaLinki P21731.

    Miscellaneous databases

    ChiTaRSi TBXA2R. human.
    GeneWikii Thromboxane_receptor.
    GenomeRNAii 6915.
    NextBioi 27045.
    PROi P21731.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21731.
    Bgeei P21731.
    CleanExi HS_TBXA2R.
    Genevestigatori P21731.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR008365. Prostanoid_rcpt.
    IPR001105. Thbox_rcpt.
    [Graphical view ]
    PANTHERi PTHR11866. PTHR11866. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR01788. PROSTANOIDR.
    PR00429. THROMBOXANER.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 156 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