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Protein

Toll-like receptor 5

Gene

TLR5

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

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

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

GO - Biological processi

Complete GO annotation...

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_355363. MyD88 deficiency (TLR5).
REACT_355387. IRAK4 deficiency (TLR5).
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11851. TLR5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 639619ExtracellularSequence AnalysisAdd
BLAST
Transmembranei640 – 66021HelicalSequence AnalysisAdd
BLAST
Topological domaini661 – 858198CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Systemic lupus erythematosus 1 (SLEB1)

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

Disease descriptionA 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.

See also OMIM:601744
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti392 – 858467Missing in 10% of the population; abolishes flagellin signaling; associated with resistance to SLEB1. 1 Publication
VAR_018398Add
BLAST

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiTLR5.

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

BgeeiO60602.
CleanExiHS_TLR5.
ExpressionAtlasiO60602. baseline and differential.
GenevisibleiO60602. HS.

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

3D structure databases

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

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.
OMAiDAYLCYS.
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

        10         20         30         40         50
MGDHLDLLLG VVLMAGPVFG IPSCSFDGRI AFYRFCNLTQ VPQVLNTTER
60 70 80 90 100
LLLSFNYIRT VTASSFPFLE QLQLLELGSQ YTPLTIDKEA FRNLPNLRIL
110 120 130 140 150
DLGSSKIYFL HPDAFQGLFH LFELRLYFCG LSDAVLKDGY FRNLKALTRL
160 170 180 190 200
DLSKNQIRSL YLHPSFGKLN SLKSIDFSSN QIFLVCEHEL EPLQGKTLSF
210 220 230 240 250
FSLAANSLYS RVSVDWGKCM NPFRNMVLEI LDVSGNGWTV DITGNFSNAI
260 270 280 290 300
SKSQAFSLIL AHHIMGAGFG FHNIKDPDQN TFAGLARSSV RHLDLSHGFV
310 320 330 340 350
FSLNSRVFET LKDLKVLNLA YNKINKIADE AFYGLDNLQV LNLSYNLLGE
360 370 380 390 400
LYSSNFYGLP KVAYIDLQKN HIAIIQDQTF KFLEKLQTLD LRDNALTTIH
410 420 430 440 450
FIPSIPDIFL SGNKLVTLPK INLTANLIHL SENRLENLDI LYFLLRVPHL
460 470 480 490 500
QILILNQNRF SSCSGDQTPS ENPSLEQLFL GENMLQLAWE TELCWDVFEG
510 520 530 540 550
LSHLQVLYLN HNYLNSLPPG VFSHLTALRG LSLNSNRLTV LSHNDLPANL
560 570 580 590 600
EILDISRNQL LAPNPDVFVS LSVLDITHNK FICECELSTF INWLNHTNVT
610 620 630 640 650
IAGPPADIYC VYPDSFSGVS LFSLSTEGCD EEEVLKSLKF SLFIVCTVTL
660 670 680 690 700
TLFLMTILTV TKFRGFCFIC YKTAQRLVFK DHPQGTEPDM YKYDAYLCFS
710 720 730 740 750
SKDFTWVQNA LLKHLDTQYS DQNRFNLCFE ERDFVPGENR IANIQDAIWN
760 770 780 790 800
SRKIVCLVSR HFLRDGWCLE AFSYAQGRCL SDLNSALIMV VVGSLSQYQL
810 820 830 840 850
MKHQSIRGFV QKQQYLRWPE DFQDVGWFLH KLSQQILKKE KEKKKDNNIP

LQTVATIS
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. 1 Publication
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:
EMBLi
GenBanki
DDBJi
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_005273241.3.
XP_005273299.2. XM_005273242.3.
XP_005273300.2. XM_005273243.3.
XP_006711567.1. XM_006711504.2.
XP_006711568.1. XM_006711505.2.
XP_006711569.1. XM_006711506.2.
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:
EMBLi
GenBanki
DDBJi
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_005273241.3.
XP_005273299.2. XM_005273242.3.
XP_005273300.2. XM_005273243.3.
XP_006711567.1. XM_006711504.2.
XP_006711568.1. XM_006711505.2.
XP_006711569.1. XM_006711506.2.
UniGeneiHs.604542.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2176839.
GuidetoPHARMACOLOGYi1755.

PTM databases

PhosphoSiteiO60602.

Polymorphism and mutation databases

BioMutaiTLR5.

Proteomic databases

PaxDbiO60602.
PRIDEiO60602.

Protocols and materials databases

DNASUi7100.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7100.
GeneCardsiGC01M223283.
HGNCiHGNC:11851. TLR5.
HPAiCAB009013.
HPA015573.
MIMi109100. phenotype.
601744. phenotype.
603031. gene.
608556. phenotype.
615557. phenotype.
neXtProtiNX_O60602.
PharmGKBiPA36553.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_27215. MyD88 cascade initiated on plasma membrane.
REACT_355363. MyD88 deficiency (TLR5).
REACT_355387. IRAK4 deficiency (TLR5).
REACT_9061. Toll Like Receptor 5 (TLR5) Cascade.

Miscellaneous databases

GeneWikiiTLR_5.
GenomeRNAii7100.
NextBioi13614062.
PROiO60602.
SOURCEiSearch...

Gene expression databases

BgeeiO60602.
CleanExiHS_TLR5.
ExpressionAtlasiO60602. baseline and differential.
GenevisibleiO60602. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 146 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

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.