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O60602 (TLR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toll-like receptor 5
Alternative name(s):
Toll/interleukin-1 receptor-like protein 3
Gene names
Name:TLR5
Synonyms:TIL3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

Binds MYD88 via their respective TIR domains By similarity. Homodimer both in the absence and presence of ligand. Ref.15

Subcellular location

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

Tissue specificity

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

Post-translational modification

Phosphorylated at Ser-805 by PKD/PRKD1; phosphorylation induces the production of inflammatory cytokines. Ref.13 Ref.14

Phosphorylated at Tyr-798 upon flagellin binding; required for signaling. Ref.13 Ref.14

Polymorphism

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 [MIM:608556]. It also provides protection against systemic lupus erythematosus.

Involvement in disease

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. Ref.12

Sequence similarities

Belongs to the Toll-like receptor family.

Contains 15 LRR (leucine-rich) repeats.

Contains 1 TIR domain.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseSystemic lupus erythematosus
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

male gonad development

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-8 production

Inferred from direct assay PubMed 17128265. Source: BHF-UCL

positive regulation of toll-like receptor signaling pathway

Inferred from direct assay PubMed 17128265. Source: BHF-UCL

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioninterleukin-1 receptor binding

Inferred from physical interaction PubMed 12925853. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.10
Chain21 – 858838Toll-like receptor 5
PRO_0000034729

Regions

Topological domain21 – 639619Extracellular Potential
Transmembrane640 – 66021Helical; Potential
Topological domain661 – 858198Cytoplasmic Potential
Repeat45 – 6824LRR 1
Repeat94 – 11724LRR 2
Repeat144 – 16825LRR 3
Repeat170 – 19223LRR 4
Repeat287 – 31024LRR 5
Repeat311 – 33424LRR 6
Repeat336 – 35823LRR 7
Repeat359 – 38224LRR 8
Repeat383 – 40725LRR 9
Repeat415 – 43723LRR 10
Repeat447 – 47024LRR 11
Repeat472 – 49625LRR 12
Repeat501 – 52424LRR 13
Repeat526 – 54823LRR 14
Repeat550 – 57021LRR 15
Domain691 – 837147TIR

Amino acid modifications

Modified residue7981Phosphotyrosine Ref.13
Modified residue8051Phosphoserine; by PKD/PRKD1 Ref.14
Glycosylation371N-linked (GlcNAc...) Ref.15
Glycosylation461N-linked (GlcNAc...) Ref.15
Glycosylation2451N-linked (GlcNAc...) Ref.15
Glycosylation3421N-linked (GlcNAc...) Ref.15
Glycosylation4221N-linked (GlcNAc...) Ref.15
Glycosylation5951N-linked (GlcNAc...) Ref.15
Glycosylation5981N-linked (GlcNAc...) Ref.15
Disulfide bond583 ↔ 610 Ref.15
Disulfide bond585 ↔ 629 Ref.15

Natural variations

Natural variant821T → I.
Corresponds to variant rs764535 [ dbSNP | Ensembl ].
VAR_032455
Natural variant1121P → A.
Corresponds to variant rs5744166 [ dbSNP | Ensembl ].
VAR_032456
Natural variant1431N → T.
Corresponds to variant rs5744167 [ dbSNP | Ensembl ].
VAR_061856
Natural variant1811Q → K.
Corresponds to variant rs45528236 [ dbSNP | Ensembl ].
VAR_061857
Natural variant392 – 858467Missing in 10% of the population; abolishes flagellin signaling; associated with resistance to SLEB1.
VAR_018398
Natural variant5921N → S. Ref.12 Ref.16
Corresponds to variant rs2072493 [ dbSNP | Ensembl ].
VAR_018399
Natural variant6161F → L. Ref.1 Ref.12 Ref.16
Corresponds to variant rs5744174 [ dbSNP | Ensembl ].
VAR_018400
Natural variant6441I → F. Ref.5
Corresponds to variant rs5744175 [ dbSNP | Ensembl ].
VAR_070457
Natural variant7691L → F.
Corresponds to variant rs56243703 [ dbSNP | Ensembl ].
VAR_061858
Natural variant8221F → L. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9
Corresponds to variant rs7512943 [ dbSNP | Ensembl ].
VAR_047454

Experimental info

Sequence conflict2311L → V in AAC34376. Ref.1
Sequence conflict3521Y → C in AAC34376. Ref.1
Sequence conflict3871Q → R in AAI09120. Ref.8

Secondary structure

... 858
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60602 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 9EE0AB6EEFEA9051

FASTA85897,834
        10         20         30         40         50         60 
MGDHLDLLLG VVLMAGPVFG IPSCSFDGRI AFYRFCNLTQ VPQVLNTTER LLLSFNYIRT 

        70         80         90        100        110        120 
VTASSFPFLE QLQLLELGSQ YTPLTIDKEA FRNLPNLRIL DLGSSKIYFL HPDAFQGLFH 

       130        140        150        160        170        180 
LFELRLYFCG LSDAVLKDGY FRNLKALTRL DLSKNQIRSL YLHPSFGKLN SLKSIDFSSN 

       190        200        210        220        230        240 
QIFLVCEHEL EPLQGKTLSF FSLAANSLYS RVSVDWGKCM NPFRNMVLEI LDVSGNGWTV 

       250        260        270        280        290        300 
DITGNFSNAI SKSQAFSLIL AHHIMGAGFG FHNIKDPDQN TFAGLARSSV RHLDLSHGFV 

       310        320        330        340        350        360 
FSLNSRVFET LKDLKVLNLA YNKINKIADE AFYGLDNLQV LNLSYNLLGE LYSSNFYGLP 

       370        380        390        400        410        420 
KVAYIDLQKN HIAIIQDQTF KFLEKLQTLD LRDNALTTIH FIPSIPDIFL SGNKLVTLPK 

       430        440        450        460        470        480 
INLTANLIHL SENRLENLDI LYFLLRVPHL QILILNQNRF SSCSGDQTPS ENPSLEQLFL 

       490        500        510        520        530        540 
GENMLQLAWE TELCWDVFEG LSHLQVLYLN HNYLNSLPPG VFSHLTALRG LSLNSNRLTV 

       550        560        570        580        590        600 
LSHNDLPANL EILDISRNQL LAPNPDVFVS LSVLDITHNK FICECELSTF INWLNHTNVT 

       610        620        630        640        650        660 
IAGPPADIYC VYPDSFSGVS LFSLSTEGCD EEEVLKSLKF SLFIVCTVTL TLFLMTILTV 

       670        680        690        700        710        720 
TKFRGFCFIC YKTAQRLVFK DHPQGTEPDM YKYDAYLCFS SKDFTWVQNA LLKHLDTQYS 

       730        740        750        760        770        780 
DQNRFNLCFE ERDFVPGENR IANIQDAIWN SRKIVCLVSR HFLRDGWCLE AFSYAQGRCL 

       790        800        810        820        830        840 
SDLNSALIMV VVGSLSQYQL MKHQSIRGFV QKQQYLRWPE DFQDVGWFLH KLSQQILKKE 

       850 
KEKKKDNNIP LQTVATIS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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, SUBUNIT.
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31033.1.
RefSeqNP_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.
UniGeneHs.604542.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P95model-B551-560[»]
3J0Aelectron microscopy26.00A/B23-858[»]
ProteinModelPortalO60602.
SMRO60602. Positions 23-837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112955. 3 interactions.
IntActO60602. 2 interactions.
MINTMINT-4950390.
STRING9606.ENSP00000340089.

Chemistry

ChEMBLCHEMBL2176839.
GuidetoPHARMACOLOGY1755.

PTM databases

PhosphoSiteO60602.

Proteomic databases

PaxDbO60602.
PRIDEO60602.

Protocols and materials databases

DNASU7100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342210; ENSP00000340089; ENSG00000187554.
ENST00000366881; ENSP00000355846; ENSG00000187554.
ENST00000540964; ENSP00000440643; ENSG00000187554.
GeneID7100.
KEGGhsa:7100.
UCSCuc001hnv.2. human.

Organism-specific databases

CTD7100.
GeneCardsGC01M223283.
HGNCHGNC:11851. TLR5.
HPACAB009013.
HPA015573.
MIM109100. phenotype.
601744. phenotype.
603031. gene.
608556. phenotype.
neXtProtNX_O60602.
PharmGKBPA36553.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271351.
HOGENOMHOG000008675.
HOVERGENHBG023182.
InParanoidO60602.
KOK10168.
OMAVSGNGWT.
OrthoDBEOG7HMS0B.
PhylomeDBO60602.
TreeFamTF351113.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO60602.
BgeeO60602.
CleanExHS_TLR5.
GenevestigatorO60602.

Family and domain databases

Gene3D3.40.50.10140. 1 hit.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027176. TLR5.
[Graphical view]
PANTHERPTHR24365:SF221. PTHR24365:SF221. 1 hit.
PfamPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 4 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS51450. LRR. 12 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTLR_5.
GenomeRNAi7100.
NextBio13614062.
PROO60602.
SOURCESearch...

Entry information

Entry nameTLR5_HUMAN
AccessionPrimary (citable) accession number: O60602
Secondary accession number(s): B1AZ05 expand/collapse secondary AC list , B3Y633, B9VJ63, D1CS80, D3DTB8, O15456, Q32MI2, Q32MI3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM