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P25116

- PAR1_HUMAN

UniProt

P25116 - PAR1_HUMAN

Protein

Proteinase-activated receptor 1

Gene

F2R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei41 – 422Cleavage; by thrombin

    GO - Molecular functioni

    1. G-protein alpha-subunit binding Source: UniProtKB
    2. G-protein beta-subunit binding Source: UniProtKB
    3. G-protein coupled receptor activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. receptor binding Source: BHF-UCL
    6. thrombin receptor activity Source: BHF-UCL

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    2. activation of MAPKK activity Source: UniProtKB
    3. anatomical structure morphogenesis Source: ProtInc
    4. blood coagulation Source: Reactome
    5. connective tissue replacement involved in inflammatory response wound healing Source: BHF-UCL
    6. establishment of synaptic specificity at neuromuscular junction Source: UniProtKB
    7. G-protein coupled receptor signaling pathway Source: UniProtKB
    8. homeostasis of number of cells within a tissue Source: UniProtKB
    9. inflammatory response Source: UniProtKB
    10. negative regulation of cell proliferation Source: BHF-UCL
    11. negative regulation of glomerular filtration Source: UniProtKB
    12. negative regulation of neuron apoptotic process Source: UniProtKB
    13. negative regulation of renin secretion into blood stream Source: UniProtKB
    14. phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
    15. platelet activation Source: BHF-UCL
    16. platelet dense granule organization Source: BHF-UCL
    17. positive regulation of blood coagulation Source: BHF-UCL
    18. positive regulation of calcium ion transport Source: UniProtKB
    19. positive regulation of cell migration Source: BHF-UCL
    20. positive regulation of cell proliferation Source: UniProtKB
    21. positive regulation of collagen biosynthetic process Source: BHF-UCL
    22. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    23. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    24. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
    25. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    26. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    27. positive regulation of interleukin-6 secretion Source: UniProtKB
    28. positive regulation of interleukin-8 secretion Source: UniProtKB
    29. positive regulation of JAK-STAT cascade Source: BHF-UCL
    30. positive regulation of MAPK cascade Source: BHF-UCL
    31. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    32. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
    33. positive regulation of Rho protein signal transduction Source: UniProtKB
    34. positive regulation of smooth muscle contraction Source: UniProtKB
    35. positive regulation of transcription, DNA-templated Source: BHF-UCL
    36. positive regulation of vasoconstriction Source: UniProtKB
    37. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    38. regulation of blood coagulation Source: BHF-UCL
    39. regulation of interleukin-1 beta production Source: UniProtKB
    40. regulation of sensory perception of pain Source: UniProtKB
    41. release of sequestered calcium ion into cytosol Source: UniProtKB
    42. response to lipopolysaccharide Source: UniProtKB
    43. response to wounding Source: BHF-UCL
    44. STAT protein import into nucleus Source: BHF-UCL
    45. tyrosine phosphorylation of STAT protein Source: BHF-UCL

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteinase-activated receptor 1
    Short name:
    PAR-1
    Alternative name(s):
    Coagulation factor II receptor
    Thrombin receptor
    Gene namesi
    Name:F2R
    Synonyms:CF2R, PAR1, TR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3537. F2R.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: BHF-UCL
    2. extracellular region Source: Reactome
    3. Golgi apparatus Source: ProtInc
    4. integral component of plasma membrane Source: ProtInc
    5. neuromuscular junction Source: UniProtKB
    6. plasma membrane Source: BHF-UCL
    7. platelet dense tubular network Source: BHF-UCL
    8. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27946.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Propeptidei22 – 4120PRO_0000012740Add
    BLAST
    Chaini42 – 425384Proteinase-activated receptor 1PRO_0000012741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi175 ↔ 254PROSITE-ProRule annotation
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
    Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP25116.
    PaxDbiP25116.
    PRIDEiP25116.

    PTM databases

    PhosphoSiteiP25116.

    Miscellaneous databases

    PMAP-CutDBP25116.

    Expressioni

    Tissue specificityi

    Platelets and vascular endothelial cells.

    Gene expression databases

    ArrayExpressiP25116.
    BgeeiP25116.
    CleanExiHS_F2R.
    GenevestigatoriP25116.

    Organism-specific databases

    HPAiCAB008973.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAV1Q031353EBI-2803960,EBI-603614
    PROCRQ9UNN83EBI-2803960,EBI-719705

    Protein-protein interaction databases

    BioGridi108448. 14 interactions.
    DIPiDIP-29703N.
    IntActiP25116. 9 interactions.
    STRINGi9606.ENSP00000321326.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 413
    Turni47 – 504
    Helixi92 – 965
    Helixi99 – 1024
    Helixi104 – 13027
    Helixi131 – 1333
    Helixi136 – 15217
    Helixi155 – 1639
    Helixi172 – 20534
    Helixi216 – 23823
    Beta strandi243 – 2464
    Turni247 – 2504
    Beta strandi251 – 2577
    Helixi265 – 29632
    Helixi305 – 32420
    Helixi327 – 33812
    Helixi347 – 36014
    Helixi363 – 37311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NRNX-ray3.10R38-60[»]
    1NROX-ray3.10R38-64[»]
    1NRPX-ray3.00R38-60[»]
    1NRQX-ray3.50R40-60[»]
    1NRRX-ray2.40R43-60[»]
    3BEFX-ray2.20C/F49-57[»]
    3HKIX-ray2.20C/F42-62[»]
    3HKJX-ray2.60C/F42-62[»]
    3LU9X-ray1.80C/F33-57[»]
    3VW7X-ray2.20A86-395[»]
    ProteinModelPortaliP25116.
    SMRiP25116. Positions 62-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25116.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 10261ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini129 – 1379CytoplasmicSequence Analysis
    Topological domaini158 – 17619ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini199 – 21820CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini240 – 26829ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini289 – 31123CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini335 – 35016ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini375 – 42551CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei103 – 12826Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei138 – 15720Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei177 – 19822Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei219 – 23921Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei269 – 28820Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei312 – 33423Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei351 – 37424Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi57 – 604Asp/Glu-rich (acidic)

    Domaini

    The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin.

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG150457.
    HOGENOMiHOG000232200.
    HOVERGENiHBG108233.
    InParanoidiP25116.
    KOiK03914.
    OMAiASKMDTC.
    OrthoDBiEOG7V49ZD.
    PhylomeDBiP25116.
    TreeFamiTF330775.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR003912. Protea_act_rcpt.
    IPR000935. Thrmbn_rcpt.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR01428. PROTEASEAR.
    PR00908. THROMBINR.
    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.

    P25116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPRRLLLVA ACFSLCGPLL SARTRARRPE SKATNATLDP RSFLLRNPND    50
    KYEPFWEDEE KNESGLTEYR LVSINKSSPL QKQLPAFISE DASGYLTSSW 100
    LTLFVPSVYT GVFVVSLPLN IMAIVVFILK MKVKKPAVVY MLHLATADVL 150
    FVSVLPFKIS YYFSGSDWQF GSELCRFVTA AFYCNMYASI LLMTVISIDR 200
    FLAVVYPMQS LSWRTLGRAS FTCLAIWALA IAGVVPLLLK EQTIQVPGLN 250
    ITTCHDVLNE TLLEGYYAYY FSAFSAVFFF VPLIISTVCY VSIIRCLSSS 300
    AVANRSKKSR ALFLSAAVFC IFIICFGPTN VLLIAHYSFL SHTSTTEAAY 350
    FAYLLCVCVS SISCCIDPLI YYYASSECQR YVYSILCCKE SSDPSSYNSS 400
    GQLMASKMDT CSSNLNNSIY KKLLT 425
    Length:425
    Mass (Da):47,441
    Last modified:April 16, 2002 - v2
    Checksum:i41B742A99EEC96AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381L → V in AAA36743. (PubMed:1672265)Curated
    Sequence conflicti364 – 3641C → S in AAA36743. (PubMed:1672265)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661S → G.1 Publication
    Corresponds to variant rs5893 [ dbSNP | Ensembl ].
    VAR_014167
    Natural varianti187 – 1871Y → N.
    Corresponds to variant rs2230849 [ dbSNP | Ensembl ].
    VAR_049432
    Natural varianti257 – 2571V → L.
    Corresponds to variant rs2227832 [ dbSNP | Ensembl ].
    VAR_049433
    Natural varianti268 – 2681A → P.
    Corresponds to variant rs1055103 [ dbSNP | Ensembl ].
    VAR_060680
    Natural varianti335 – 3351A → V.2 Publications
    Corresponds to variant rs17849599 [ dbSNP | Ensembl ].
    VAR_060681
    Natural varianti412 – 4121S → Y.
    Corresponds to variant rs2227799 [ dbSNP | Ensembl ].
    VAR_049434

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62424 mRNA. Translation: AAA36743.1.
    AF391809 Genomic DNA. Translation: AAK69768.1.
    BT007279 mRNA. Translation: AAP35943.1.
    BC002464 mRNA. Translation: AAH02464.1.
    BC051909 mRNA. Translation: AAH51909.1.
    CCDSiCCDS4032.1.
    PIRiA37912.
    RefSeqiNP_001983.2. NM_001992.3.
    UniGeneiHs.482562.

    Genome annotation databases

    EnsembliENST00000319211; ENSP00000321326; ENSG00000181104.
    GeneIDi2149.
    KEGGihsa:2149.
    UCSCiuc003ken.4. human.

    Polymorphism databases

    DMDMi20178318.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62424 mRNA. Translation: AAA36743.1 .
    AF391809 Genomic DNA. Translation: AAK69768.1 .
    BT007279 mRNA. Translation: AAP35943.1 .
    BC002464 mRNA. Translation: AAH02464.1 .
    BC051909 mRNA. Translation: AAH51909.1 .
    CCDSi CCDS4032.1.
    PIRi A37912.
    RefSeqi NP_001983.2. NM_001992.3.
    UniGenei Hs.482562.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NRN X-ray 3.10 R 38-60 [» ]
    1NRO X-ray 3.10 R 38-64 [» ]
    1NRP X-ray 3.00 R 38-60 [» ]
    1NRQ X-ray 3.50 R 40-60 [» ]
    1NRR X-ray 2.40 R 43-60 [» ]
    3BEF X-ray 2.20 C/F 49-57 [» ]
    3HKI X-ray 2.20 C/F 42-62 [» ]
    3HKJ X-ray 2.60 C/F 42-62 [» ]
    3LU9 X-ray 1.80 C/F 33-57 [» ]
    3VW7 X-ray 2.20 A 86-395 [» ]
    ProteinModelPortali P25116.
    SMRi P25116. Positions 62-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108448. 14 interactions.
    DIPi DIP-29703N.
    IntActi P25116. 9 interactions.
    STRINGi 9606.ENSP00000321326.

    Chemistry

    BindingDBi P25116.
    ChEMBLi CHEMBL3974.
    DrugBanki DB00086. Streptokinase.
    GuidetoPHARMACOLOGYi 347.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P25116.

    Polymorphism databases

    DMDMi 20178318.

    Proteomic databases

    MaxQBi P25116.
    PaxDbi P25116.
    PRIDEi P25116.

    Protocols and materials databases

    DNASUi 2149.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319211 ; ENSP00000321326 ; ENSG00000181104 .
    GeneIDi 2149.
    KEGGi hsa:2149.
    UCSCi uc003ken.4. human.

    Organism-specific databases

    CTDi 2149.
    GeneCardsi GC05P076047.
    H-InvDB HIX0004960.
    HGNCi HGNC:3537. F2R.
    HPAi CAB008973.
    MIMi 187930. gene.
    neXtProti NX_P25116.
    PharmGKBi PA27946.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150457.
    HOGENOMi HOG000232200.
    HOVERGENi HBG108233.
    InParanoidi P25116.
    KOi K03914.
    OMAi ASKMDTC.
    OrthoDBi EOG7V49ZD.
    PhylomeDBi P25116.
    TreeFami TF330775.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_18283. G alpha (q) signalling events.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).

    Miscellaneous databases

    ChiTaRSi F2R. human.
    EvolutionaryTracei P25116.
    GeneWikii Coagulation_factor_II_receptor.
    GenomeRNAii 2149.
    NextBioi 8685.
    PMAP-CutDB P25116.
    PROi P25116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25116.
    Bgeei P25116.
    CleanExi HS_F2R.
    Genevestigatori P25116.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR003912. Protea_act_rcpt.
    IPR000935. Thrmbn_rcpt.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PR01428. PROTEASEAR.
    PR00908. THROMBINR.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation."
      Vu T.-K.H., Hung D.T., Wheaton V.I., Coughlin S.R.
      Cell 64:1057-1068(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. SeattleSNPs variation discovery resource
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-335.
    4. "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], VARIANT VAL-335.
      Tissue: Eye.
    5. "Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization."
      Shapiro M.J., Trejo J., Zeng D., Coughlin S.R.
      J. Biol. Chem. 271:32874-32880(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    6. "Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin."
      Kahn M.L., Nakanishi-Matsui M., Shapiro M.J., Ishihara H., Coughlin S.R.
      J. Clin. Invest. 103:879-887(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Parstatin, the cleaved peptide on proteinase-activated receptor 1 activation, is a potent inhibitor of angiogenesis."
      Zania P., Gourni D., Aplin A.C., Nicosia R.F., Flordellis C.S., Maragoudakis M.E., Tsopanoglou N.E.
      J. Pharmacol. Exp. Ther. 328:378-389(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANGIOGENESIS INHIBITION PROPERTIES OF PARSTATIN.
    8. "The protease-activated receptor 1 possesses a functional and cleavable signal peptide which is necessary for receptor expression."
      Zampatis D.E., Rutz C., Furkert J., Schmidt A., Wustenhagen D., Kubick S., Tsopanoglou N.E., Schulein R.
      FEBS Lett. 586:2351-2359(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIGNAL SEQUENCE CLEAVAGE SITE.
    9. Cited for: VARIANT GLY-166.
    10. "Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes."
      Mathews I.I., Padmanabhan K.P., Ganesh V., Tulinsky A., Ishii M., Chen J., Turck C.W., Coughlin S.R., Fenton J.W. II
      Biochemistry 33:3266-3279(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 38-64 IN COMPLEX WITH THROMBIN.

    Entry informationi

    Entry nameiPAR1_HUMAN
    AccessioniPrimary (citable) accession number: P25116
    Secondary accession number(s): Q53XV0, Q96RF7, Q9BUN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 166 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 chromosome 5
      Human chromosome 5: 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