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O60602

- TLR5_HUMAN

UniProt

O60602 - TLR5_HUMAN

Protein

Toll-like receptor 5

Gene

TLR5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Participates in the innate immune response to microbial agents. Mediates detection of bacterial flagellins. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.1 Publication

    GO - Molecular functioni

    1. interleukin-1 receptor binding Source: UniProtKB
    2. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: Ensembl
    2. cellular response to mechanical stimulus Source: UniProtKB
    3. defense response to bacterium Source: InterPro
    4. inflammatory response Source: UniProtKB-KW
    5. innate immune response Source: Reactome
    6. male gonad development Source: Ensembl
    7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    8. positive regulation of interleukin-8 production Source: BHF-UCL
    9. positive regulation of toll-like receptor signaling pathway Source: BHF-UCL
    10. regulation of cytokine secretion Source: InterPro
    11. toll-like receptor 10 signaling pathway Source: Reactome
    12. toll-like receptor 5 signaling pathway Source: Reactome
    13. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_9061. Toll Like Receptor 5 (TLR5) Cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Toll-like receptor 5
    Alternative name(s):
    Toll/interleukin-1 receptor-like protein 3
    Gene namesi
    Name:TLR5
    Synonyms:TIL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11851. TLR5.

    Subcellular locationi

    Membrane By similarity; Single-pass type I membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Systemic lupus erythematosus 1 (SLEB1) [MIM:601744]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti392 – 858467Missing in 10% of the population; abolishes flagellin signaling; associated with resistance to SLEB1.
    VAR_018398Add
    BLAST

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    MIMi109100. phenotype.
    601744. phenotype.
    608556. phenotype.
    615557. phenotype.
    PharmGKBiPA36553.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 858838Toll-like receptor 5PRO_0000034729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)1 Publication
    Glycosylationi46 – 461N-linked (GlcNAc...)1 Publication
    Glycosylationi245 – 2451N-linked (GlcNAc...)1 Publication
    Glycosylationi342 – 3421N-linked (GlcNAc...)1 Publication
    Glycosylationi422 – 4221N-linked (GlcNAc...)1 Publication
    Disulfide bondi583 ↔ 6101 Publication
    Disulfide bondi585 ↔ 6291 Publication
    Glycosylationi595 – 5951N-linked (GlcNAc...)1 Publication
    Glycosylationi598 – 5981N-linked (GlcNAc...)1 Publication
    Modified residuei798 – 7981Phosphotyrosine1 Publication
    Modified residuei805 – 8051Phosphoserine; by PKD/PRKD11 Publication

    Post-translational modificationi

    Phosphorylated at Ser-805 by PKD/PRKD1; phosphorylation induces the production of inflammatory cytokines.2 Publications
    Phosphorylated at Tyr-798 upon flagellin binding; required for signaling.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO60602.
    PRIDEiO60602.

    PTM databases

    PhosphoSiteiO60602.

    Expressioni

    Tissue specificityi

    Highly expressed in ovary and in peripheral blood leukocytes, especially in monocytes, less in CD11c+ immature dendritic cells. Also detected in prostate and testis.

    Gene expression databases

    ArrayExpressiO60602.
    BgeeiO60602.
    CleanExiHS_TLR5.
    GenevestigatoriO60602.

    Organism-specific databases

    HPAiCAB009013.
    HPA015573.

    Interactioni

    Subunit structurei

    Binds MYD88 via their respective TIR domains By similarity. Homodimer both in the absence and presence of ligand.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi112955. 3 interactions.
    IntActiO60602. 2 interactions.
    MINTiMINT-4950390.
    STRINGi9606.ENSP00000340089.

    Structurei

    Secondary structure

    1
    858
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi552 – 5598

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P95model-B551-560[»]
    3J0Aelectron microscopy26.00A/B23-858[»]
    ProteinModelPortaliO60602.
    SMRiO60602. Positions 23-837.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 639619ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini661 – 858198CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei640 – 66021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati45 – 6824LRR 11 PublicationAdd
    BLAST
    Repeati71 – 9323LRR 21 PublicationAdd
    BLAST
    Repeati95 – 11723LRR 31 PublicationAdd
    BLAST
    Repeati120 – 14324LRR 41 PublicationAdd
    BLAST
    Repeati146 – 16621LRR 51 PublicationAdd
    BLAST
    Repeati171 – 19222LRR 61 PublicationAdd
    BLAST
    Repeati197 – 21115LRR 71 PublicationAdd
    BLAST
    Repeati214 – 22916LRR 81 PublicationAdd
    BLAST
    Repeati234 – 2352LRR 91 Publication
    Repeati260 – 28425LRR 111 PublicationAdd
    BLAST
    Repeati289 – 30113LRR 121 PublicationAdd
    BLAST
    Repeati313 – 33422LRR 131 PublicationAdd
    BLAST
    Repeati337 – 35519LRR 141 PublicationAdd
    BLAST
    Repeati385 – 40117LRR 161 PublicationAdd
    BLAST
    Repeati412 – 43120LRR 171 PublicationAdd
    BLAST
    Repeati449 – 47022LRR 181 PublicationAdd
    BLAST
    Repeati474 – 49522LRR 191 PublicationAdd
    BLAST
    Repeati503 – 52422LRR 201 PublicationAdd
    BLAST
    Repeati527 – 54620LRR 211 PublicationAdd
    BLAST
    Repeati549 – 56719LRR 221 PublicationAdd
    BLAST
    Domaini579 – 63153LRRCTAdd
    BLAST
    Domaini691 – 837147TIRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 22 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG271351.
    HOGENOMiHOG000008675.
    HOVERGENiHBG023182.
    InParanoidiO60602.
    KOiK10168.
    OMAiVSGNGWT.
    OrthoDBiEOG7HMS0B.
    PhylomeDBiO60602.
    TreeFamiTF351113.

    Family and domain databases

    Gene3Di3.40.50.10140. 1 hit.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027176. TLR5.
    [Graphical view]
    PANTHERiPTHR24365:SF221. PTHR24365:SF221. 1 hit.
    PfamiPF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 4 hits.
    PF01582. TIR. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS51450. LRR. 12 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O60602-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDHLDLLLG VVLMAGPVFG IPSCSFDGRI AFYRFCNLTQ VPQVLNTTER    50
    LLLSFNYIRT VTASSFPFLE QLQLLELGSQ YTPLTIDKEA FRNLPNLRIL 100
    DLGSSKIYFL HPDAFQGLFH LFELRLYFCG LSDAVLKDGY FRNLKALTRL 150
    DLSKNQIRSL YLHPSFGKLN SLKSIDFSSN QIFLVCEHEL EPLQGKTLSF 200
    FSLAANSLYS RVSVDWGKCM NPFRNMVLEI LDVSGNGWTV DITGNFSNAI 250
    SKSQAFSLIL AHHIMGAGFG FHNIKDPDQN TFAGLARSSV RHLDLSHGFV 300
    FSLNSRVFET LKDLKVLNLA YNKINKIADE AFYGLDNLQV LNLSYNLLGE 350
    LYSSNFYGLP KVAYIDLQKN HIAIIQDQTF KFLEKLQTLD LRDNALTTIH 400
    FIPSIPDIFL SGNKLVTLPK INLTANLIHL SENRLENLDI LYFLLRVPHL 450
    QILILNQNRF SSCSGDQTPS ENPSLEQLFL GENMLQLAWE TELCWDVFEG 500
    LSHLQVLYLN HNYLNSLPPG VFSHLTALRG LSLNSNRLTV LSHNDLPANL 550
    EILDISRNQL LAPNPDVFVS LSVLDITHNK FICECELSTF INWLNHTNVT 600
    IAGPPADIYC VYPDSFSGVS LFSLSTEGCD EEEVLKSLKF SLFIVCTVTL 650
    TLFLMTILTV TKFRGFCFIC YKTAQRLVFK DHPQGTEPDM YKYDAYLCFS 700
    SKDFTWVQNA LLKHLDTQYS DQNRFNLCFE ERDFVPGENR IANIQDAIWN 750
    SRKIVCLVSR HFLRDGWCLE AFSYAQGRCL SDLNSALIMV VVGSLSQYQL 800
    MKHQSIRGFV QKQQYLRWPE DFQDVGWFLH KLSQQILKKE KEKKKDNNIP 850
    LQTVATIS 858
    Length:858
    Mass (Da):97,834
    Last modified:November 25, 2008 - v4
    Checksum:i9EE0AB6EEFEA9051
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti231 – 2311L → V in AAC34376. (PubMed:9596645)Curated
    Sequence conflicti352 – 3521Y → C in AAC34376. (PubMed:9596645)Curated
    Sequence conflicti387 – 3871Q → R in AAI09120. (PubMed:15489334)Curated

    Polymorphismi

    Individuals with a common stop codon polymorphism in position 392 are unable to mediate flagellin signaling. This polymorphism acts in a dominant fashion and is associated with susceptibility to pneumonia caused by Legionella pneumophila [MIMi:608556]. It also provides protection against systemic lupus erythematosus.
    A nonsense TLR5 polymorphism, resulting in p.Arg392Ter, confers resistance to melioidosis [MIMi:615557], an infection caused by the Gram-negative, flagellated soil saprophyte Burkholderia pseudomallei. Carriers of this hypofunctional TLR5 variant may generate impaired inflammatory responses during melioidosis infection that result in reduced organ failure and lower mortality.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821T → I.
    Corresponds to variant rs764535 [ dbSNP | Ensembl ].
    VAR_032455
    Natural varianti112 – 1121P → A.
    Corresponds to variant rs5744166 [ dbSNP | Ensembl ].
    VAR_032456
    Natural varianti143 – 1431N → T.
    Corresponds to variant rs5744167 [ dbSNP | Ensembl ].
    VAR_061856
    Natural varianti181 – 1811Q → K.
    Corresponds to variant rs45528236 [ dbSNP | Ensembl ].
    VAR_061857
    Natural varianti392 – 858467Missing in 10% of the population; abolishes flagellin signaling; associated with resistance to SLEB1.
    VAR_018398Add
    BLAST
    Natural varianti592 – 5921N → S.2 Publications
    Corresponds to variant rs2072493 [ dbSNP | Ensembl ].
    VAR_018399
    Natural varianti616 – 6161F → L.3 Publications
    Corresponds to variant rs5744174 [ dbSNP | Ensembl ].
    VAR_018400
    Natural varianti644 – 6441I → F.1 Publication
    Corresponds to variant rs5744175 [ dbSNP | Ensembl ].
    VAR_070457
    Natural varianti769 – 7691L → F.
    Corresponds to variant rs56243703 [ dbSNP | Ensembl ].
    VAR_061858
    Natural varianti822 – 8221F → L.8 Publications
    Corresponds to variant rs7512943 [ dbSNP | Ensembl ].
    VAR_047454

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051151 mRNA. Translation: AAC34376.1.
    AB060695 mRNA. Translation: BAB43955.1.
    AB445645 mRNA. Translation: BAG55042.1.
    FJ556976 Genomic DNA. Translation: ACM69019.1.
    FJ556977 Genomic DNA. Translation: ACM69020.1.
    FJ556979 Genomic DNA. Translation: ACM69022.1.
    FJ556980 Genomic DNA. Translation: ACM69023.1.
    FJ556987 Genomic DNA. Translation: ACM69030.1.
    FJ556989 Genomic DNA. Translation: ACM69032.1.
    DQ026408 Genomic DNA. Translation: AAZ17463.1.
    DQ026409 Genomic DNA. Translation: AAZ17464.1.
    DQ026415 Genomic DNA. Translation: AAZ17469.1.
    AL929091 Genomic DNA. Translation: CAM28378.1.
    CH471100 Genomic DNA. Translation: EAW93262.1.
    CH471100 Genomic DNA. Translation: EAW93263.1.
    BC109118 mRNA. Translation: AAI09119.1.
    BC109119 mRNA. Translation: AAI09120.1.
    U88881 mRNA. Translation: AAC34136.1.
    CCDSiCCDS31033.1.
    RefSeqiNP_003259.2. NM_003268.5.
    XP_005273298.2. XM_005273241.2.
    XP_005273299.2. XM_005273242.2.
    XP_005273300.2. XM_005273243.2.
    XP_006711566.1. XM_006711503.1.
    XP_006711567.1. XM_006711504.1.
    XP_006711568.1. XM_006711505.1.
    XP_006711569.1. XM_006711506.1.
    XP_006711570.1. XM_006711507.1.
    UniGeneiHs.604542.

    Genome annotation databases

    EnsembliENST00000366881; ENSP00000355846; ENSG00000187554.
    ENST00000540964; ENSP00000440643; ENSG00000187554.
    GeneIDi7100.
    KEGGihsa:7100.
    UCSCiuc001hnv.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051151 mRNA. Translation: AAC34376.1 .
    AB060695 mRNA. Translation: BAB43955.1 .
    AB445645 mRNA. Translation: BAG55042.1 .
    FJ556976 Genomic DNA. Translation: ACM69019.1 .
    FJ556977 Genomic DNA. Translation: ACM69020.1 .
    FJ556979 Genomic DNA. Translation: ACM69022.1 .
    FJ556980 Genomic DNA. Translation: ACM69023.1 .
    FJ556987 Genomic DNA. Translation: ACM69030.1 .
    FJ556989 Genomic DNA. Translation: ACM69032.1 .
    DQ026408 Genomic DNA. Translation: AAZ17463.1 .
    DQ026409 Genomic DNA. Translation: AAZ17464.1 .
    DQ026415 Genomic DNA. Translation: AAZ17469.1 .
    AL929091 Genomic DNA. Translation: CAM28378.1 .
    CH471100 Genomic DNA. Translation: EAW93262.1 .
    CH471100 Genomic DNA. Translation: EAW93263.1 .
    BC109118 mRNA. Translation: AAI09119.1 .
    BC109119 mRNA. Translation: AAI09120.1 .
    U88881 mRNA. Translation: AAC34136.1 .
    CCDSi CCDS31033.1.
    RefSeqi NP_003259.2. NM_003268.5.
    XP_005273298.2. XM_005273241.2.
    XP_005273299.2. XM_005273242.2.
    XP_005273300.2. XM_005273243.2.
    XP_006711566.1. XM_006711503.1.
    XP_006711567.1. XM_006711504.1.
    XP_006711568.1. XM_006711505.1.
    XP_006711569.1. XM_006711506.1.
    XP_006711570.1. XM_006711507.1.
    UniGenei Hs.604542.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P95 model - B 551-560 [» ]
    3J0A electron microscopy 26.00 A/B 23-858 [» ]
    ProteinModelPortali O60602.
    SMRi O60602. Positions 23-837.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112955. 3 interactions.
    IntActi O60602. 2 interactions.
    MINTi MINT-4950390.
    STRINGi 9606.ENSP00000340089.

    Chemistry

    ChEMBLi CHEMBL2176839.
    GuidetoPHARMACOLOGYi 1755.

    PTM databases

    PhosphoSitei O60602.

    Proteomic databases

    PaxDbi O60602.
    PRIDEi O60602.

    Protocols and materials databases

    DNASUi 7100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366881 ; ENSP00000355846 ; ENSG00000187554 .
    ENST00000540964 ; ENSP00000440643 ; ENSG00000187554 .
    GeneIDi 7100.
    KEGGi hsa:7100.
    UCSCi uc001hnv.2. human.

    Organism-specific databases

    CTDi 7100.
    GeneCardsi GC01M223283.
    HGNCi HGNC:11851. TLR5.
    HPAi CAB009013.
    HPA015573.
    MIMi 109100. phenotype.
    601744. phenotype.
    603031. gene.
    608556. phenotype.
    615557. phenotype.
    neXtProti NX_O60602.
    PharmGKBi PA36553.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271351.
    HOGENOMi HOG000008675.
    HOVERGENi HBG023182.
    InParanoidi O60602.
    KOi K10168.
    OMAi VSGNGWT.
    OrthoDBi EOG7HMS0B.
    PhylomeDBi O60602.
    TreeFami TF351113.

    Enzyme and pathway databases

    Reactomei REACT_27215. MyD88 cascade initiated on plasma membrane.
    REACT_9061. Toll Like Receptor 5 (TLR5) Cascade.

    Miscellaneous databases

    GeneWikii TLR_5.
    GenomeRNAii 7100.
    NextBioi 13614062.
    PROi O60602.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60602.
    Bgeei O60602.
    CleanExi HS_TLR5.
    Genevestigatori O60602.

    Family and domain databases

    Gene3Di 3.40.50.10140. 1 hit.
    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000157. TIR_dom.
    IPR027176. TLR5.
    [Graphical view ]
    PANTHERi PTHR24365:SF221. PTHR24365:SF221. 1 hit.
    Pfami PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 4 hits.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS51450. LRR. 12 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of two Toll/Interleukin-1 receptor-like genes TIL3 and TIL4: evidence for a multi-gene receptor family in humans."
      Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M., Jasmin A., Trask B.J., Hood L., Nelson P.S.
      Blood 91:4020-4027(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-616 AND LEU-822.
      Tissue: Leukocyte and Prostate.
    2. "Homo sapiens TLR5."
      Seya T., Tsukada H.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-822.
      Tissue: Macrophage.
    3. "Natural selection in the TLR-related genes in the course of primate evolution."
      Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.
      Immunogenetics 60:727-735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-822.
    4. "A history of recurrent positive selection at the toll-like receptor 5 in primates."
      Wlasiuk G., Khan S., Switzer W.M., Nachman M.W.
      Mol. Biol. Evol. 26:937-949(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-822.
    5. "The heterogeneous allelic repertoire of human Toll-Like receptor (TLR) genes."
      Georgel P., Macquin C., Bahram S.
      PLoS ONE 4:E7803-E7803(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-644 AND LEU-822.
    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], VARIANT LEU-822.
    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], VARIANT LEU-822.
    9. "A family of human receptors structurally related to Drosophila Toll."
      Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.
      Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 494-858, VARIANT LEU-822.
      Tissue: CNS.
    10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-35.
    11. "The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5."
      Hayashi F., Smith K.D., Ozinsky A., Hawn T.R., Yi E.C., Goodlett D.R., Eng J.K., Akira S., Underhill D.M., Aderem A.
      Nature 410:1099-1103(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "A stop codon polymorphism of Toll-like receptor 5 is associated with resistance to systemic lupus erythematosus."
      Hawn T.R., Wu H., Grossman J.M., Hahn B.H., Tsao B.P., Aderem A.
      Proc. Natl. Acad. Sci. U.S.A. 102:10593-10597(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH RESISTANCE TO SLEB1, VARIANTS SER-592 AND LEU-616.
    13. "A phosphorylation site in the Toll-like receptor 5 TIR domain is required for inflammatory signalling in response to flagellin."
      Ivison S.M., Khan M.A., Graham N.R., Bernales C.Q., Kaleem A., Tirling C.O., Cherkasov A., Steiner T.S.
      Biochem. Biophys. Res. Commun. 352:936-941(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-798.
    14. "Protein kinase D interaction with TLR5 is required for inflammatory signaling in response to bacterial flagellin."
      Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N., Shobab L.A., Steiner T.S.
      J. Immunol. 178:5735-5743(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-805.
    15. Cited for: POLYMORPHISM, INVOLVEMENT IN RESISTANCE TO MELIOIDOSIS.
    16. "Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin."
      Zhou K., Kanai R., Lee P., Wang H.W., Modis Y.
      J. Struct. Biol. 177:402-409(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (26.0 ANGSTROMS) OF 23-858, GLYCOSYLATION AT ASN-37; ASN-46; ASN-245; ASN-342; ASN-422; ASN-595 AND ASN-598, DISULFIDE BONDS, LRR REPEATS, SUBUNIT.
    17. "A common dominant TLR5 stop codon polymorphism abolishes flagellin signaling and is associated with susceptibility to legionnaires' disease."
      Hawn T.R., Verbon A., Lettinga K.D., Zhao L.P., Li S.S., Laws R.J., Skerrett S.J., Beutler B., Schroeder L., Nachman A., Ozinsky A., Smith K.D., Aderem A.
      J. Exp. Med. 198:1563-1572(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS 392-ARG--SER-858 DEL; SER-592 AND LEU-616.

    Entry informationi

    Entry nameiTLR5_HUMAN
    AccessioniPrimary (citable) accession number: O60602
    Secondary accession number(s): B1AZ05
    , B3Y633, B9VJ63, D1CS80, D3DTB8, O15456, Q32MI2, Q32MI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 139 of the entry and version 4 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. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3