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P58753 (TIRAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toll/interleukin-1 receptor domain-containing adapter protein

Short name=TIR domain-containing adapter protein
Alternative name(s):
Adaptor protein Wyatt
MyD88 adapter-like protein
Short name=MyD88-2
Gene names
Name:TIRAP
Synonyms:MAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter involved in TLR2 and TLR4 signaling pathways in the innate immune response. Acts via IRAK2 and TRAF-6, leading to the activation of NF-kappa-B, MAPK1, MAPK3 and JNK, and resulting in cytokine secretion and the inflammatory response. Positively regulates the production of TNF-alpha and interleukin-6. Ref.13 Ref.14

Subunit structure

Homodimer. Also forms heterodimers with MYD88. May interact with PIK3AP1 By similarity. Interacts with TLR4 and IRAK2 via their respective TIR domains. Interacts with BMX and TBK1. Interacts with EIF2AK2. Does not interact with IRAK1, nor TLR9. Ref.2 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17

Subcellular location

Cytoplasm. Cell membrane. Membrane. Note: Colocalizes with DAB2IP at the plasma membrane. Ref.15

Tissue specificity

Highly expressed in liver, kidney, spleen, skeletal muscle and heart. Also detected in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.

Post-translational modification

Phosphorylated by IRAK1 and IRAK4. Also phosphorylated by BTK. Ref.12 Ref.16

Polyubiquitinated. Polyubiquitination follows phosphorylation by BTK and leads to TIRAP degradation.

Polymorphism

Genetic variations in TIRAP may influence susceptibility or resistance to invasive pneumococcal disease [MIM:610799], malaria [MIM:611162], and tuberculosis [MIM:607948].

Genetic variations in TIRAP influence susceptibility or resistance to bacterial invasion of the blood and define the bacteremia susceptibility locus 1 (BACTS1) [MIM:614382].

Sequence similarities

Contains 1 TIR domain.

Caution

Variant Leu-180 has been reported to reduce TLR2 signal transduction (Ref.18). In contrast, Ref.14 reports that this variant is fully active and has no effect on signal transduction pathways and cytokine production.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMDisulfide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process3'-UTR-mediated mRNA stabilization

Inferred from direct assay PubMed 15294994. Source: BHF-UCL

I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement Ref.14. Source: BHF-UCL

TIRAP-dependent toll-like receptor 4 signaling pathway

Inferred from direct assay Ref.1. Source: BHF-UCL

cell surface receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to bacterial lipopeptide

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to lipoteichoic acid

Inferred from sequence or structural similarity. Source: BHF-UCL

defense response to Gram-positive bacterium

Inferred from sequence or structural similarity. Source: BHF-UCL

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

myeloid cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of growth of symbiont in host

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

positive regulation of JNK cascade

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

positive regulation of chemokine (C-X-C motif) ligand 1 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of chemokine (C-X-C motif) ligand 2 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-15 production

Inferred from direct assay PubMed 18583567. Source: BHF-UCL

positive regulation of interleukin-6 biosynthetic process

Inferred from mutant phenotype PubMed 16301656. Source: BHF-UCL

positive regulation of interleukin-8 production

Inferred from mutant phenotype PubMed 16301656. Source: BHF-UCL

positive regulation of neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein homodimerization activity

Inferred from direct assay PubMed 12062447. Source: BHF-UCL

positive regulation of toll-like receptor 2 signaling pathway

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

positive regulation of toll-like receptor 3 signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of toll-like receptor 4 signaling pathway

Inferred from mutant phenotype Ref.14. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 16301656Ref.14. Source: BHF-UCL

regulation of innate immune response

Inferred by curator Ref.1. Source: BHF-UCL

regulation of interferon-beta production

Inferred from sequence or structural similarity. Source: BHF-UCL

response to lipopolysaccharide

Inferred from direct assay Ref.1. Source: BHF-UCL

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.15. Source: UniProtKB

ruffle membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionToll-like receptor 2 binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

Toll-like receptor 4 binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

phosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding, bridging

Non-traceable author statement Ref.14. Source: BHF-UCL

protein heterodimerization activity

Inferred from direct assay Ref.14. Source: BHF-UCL

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase C binding

Inferred from physical interaction PubMed 17161867. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P58753-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P58753-2)

The sequence of this isoform differs from the canonical sequence as follows:
     216-221: YLQTLS → CKLLQEGEGERDSATVSDLL
Isoform 3 (identifier: P58753-3)

The sequence of this isoform differs from the canonical sequence as follows:
     221-221: S → WHLLYHGTPEIGVKLETENPCRASDSHKCDKRYRE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Toll/interleukin-1 receptor domain-containing adapter protein
PRO_0000072547

Regions

Domain84 – 221138TIR

Amino acid modifications

Disulfide bond89 ↔ 134 Ref.17
Disulfide bond142 ↔ 174 Ref.17

Natural variations

Alternative sequence216 – 2216YLQTLS → CKLLQEGEGERDSATVSDLL in isoform 2.
VSP_010765
Alternative sequence2211S → WHLLYHGTPEIGVKLETENP CRASDSHKCDKRYRE in isoform 3.
VSP_017239
Natural variant91A → P Does not affect NF-kappa-B activation and TNF-alpha production. Ref.7 Ref.14
Corresponds to variant rs8177369 [ dbSNP | Ensembl ].
VAR_019143
Natural variant131R → W Does not affect NF-kappa-B activation and TNF-alpha production. Ref.7 Ref.14
Corresponds to variant rs8177399 [ dbSNP | Ensembl ].
VAR_019144
Natural variant551S → N Does not affect NF-kappa-B activation and TNF-alpha production. Ref.1 Ref.6
Corresponds to variant rs3802813 [ dbSNP | Ensembl ].
VAR_036691
Natural variant961D → N Hypomorphic variant resulting in impaired NF-kappa-B activation and TNF-alpha production; cannot bind MYD88. Ref.7 Ref.14
Corresponds to variant rs8177400 [ dbSNP | Ensembl ].
VAR_019145
Natural variant1801S → L At heterozygosity it protects against invasive pneumococcal disease, malaria, bacteremia and tuberculosis; does not affect NF-kappa-B activation and TNF-alpha production; attenuates TLR2 signal transduction. Ref.7 Ref.14 Ref.18 Ref.19
Corresponds to variant rs8177374 [ dbSNP | Ensembl ].
VAR_019146
Natural variant1971V → I Does not affect NF-kappa-B activation and TNF-alpha production. Ref.14
Corresponds to variant rs7932976 [ dbSNP | Ensembl ].
VAR_061713

Experimental info

Mutagenesis1251P → H: Abolishes NF-kappa-B activation. Ref.1 Ref.2

Secondary structure

....................... 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 44A8454D04704540

FASTA22123,883
        10         20         30         40         50         60 
MASSTSLPAP GSRPKKPLGK MADWFRQTLL KKPKKRPNSP ESTSSDASQP TSQDSPLPPS 

        70         80         90        100        110        120 
LSSVTSPSLP PTHASDSGSS RWSKDYDVCV CHSEEDLVAA QDLVSYLEGS TASLRCFLQL 

       130        140        150        160        170        180 
RDATPGGAIV SELCQALSSS HCRVLLITPG FLQDPWCKYQ MLQALTEAPG AEGCTIPLLS 

       190        200        210        220 
GLSRAAYPPE LRFMYYVDGR GPDGGFRQVK EAVMRYLQTL S 

« Hide

Isoform 2 [UniParc].

Checksum: 383386AA03B70F32
Show »

FASTA23525,323
Isoform 3 [UniParc].

Checksum: 97287F7E2A010915
Show »

FASTA25527,948

References

« Hide 'large scale' references
[1]"Mal (MyD88-adapter-like) is required for Toll-like receptor-4 signal transduction."
Fitzgerald K.A., Palsson-McDermott E.M., Bowie A.G., Jefferies C.A., Mansell A.S., Brady G., Brint E., Dunne A., Gray P., Harte M.T., McMurray D., Smith D.E., Sims J.E., Bird T.A., O'Neill L.A.J.
Nature 413:78-83(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF PRO-125, VARIANT ASN-55.
Tissue: Dendritic cell.
[2]"TIRAP: an adapter molecule in the Toll signaling pathway."
Horng T., Barton G.M., Medzhitov R.
Nat. Immunol. 2:835-841(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF PRO-125, INTERACTION WITH EIF2AK2.
[3]"Characterization and structural analysis of TIR domain-containing adaptor protein Wyatt."
Kirk P.B., Pereira J.P., Bazan J.F.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Two isoforms of MAL, generated by alternative splicing, are found in humans but not mice."
Hardy M.P., O'Neill L.A.J.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[5]"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] (ISOFORM 1).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASN-55.
Tissue: Brain and Trachea.
[7]SeattleSNPs variation discovery resource
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-9; TRP-13; ASN-96 AND LEU-180.
[8]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Blood.
[11]"Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-kappa B and IFN-regulatory factor-3, in the Toll-like receptor signaling."
Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K., Akira S.
J. Immunol. 171:4304-4310(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBK1.
[12]"Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation."
Mansell A., Smith R., Doyle S.L., Gray P., Fenner J.E., Crack P.J., Nicholson S.E., Hilton D.J., O'Neill L.A., Hertzog P.J.
Nat. Immunol. 7:148-155(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY BTK, UBIQUITINATION.
[13]"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMX.
[14]"A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling."
Nagpal K., Plantinga T.S., Wong J., Monks B.G., Gay N.J., Netea M.G., Fitzgerald K.A., Golenbock D.T.
J. Biol. Chem. 284:25742-25748(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYD88, VARIANT ASN-96, CHARACTERIZATION OF VARIANTS PRO-9; TRP-13; ASN-96; LEU-180 AND ILE-197.
[15]"AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
Wan T., Liu T., Zhang H., Tang S., Min W.
J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYD88, SUBCELLULAR LOCATION.
[16]"IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal)."
Dunne A., Carpenter S., Brikos C., Gray P., Strelow A., Wesche H., Morrice N., O'Neill L.A.
J. Biol. Chem. 285:18276-18282(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY IRAK1 AND IRAK4.
[17]"Crystal structure of Toll-like receptor adaptor MAL/TIRAP reveals the molecular basis for signal transduction and disease protection."
Valkov E., Stamp A., Dimaio F., Baker D., Verstak B., Roversi P., Kellie S., Sweet M.J., Mansell A., Gay N.J., Martin J.L., Kobe B.
Proc. Natl. Acad. Sci. U.S.A. 108:14879-14884(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 79-221, SUBUNIT, DISULFIDE BONDS.
[18]"A Mal functional variant is associated with protection against invasive pneumococcal disease, bacteremia, malaria and tuberculosis."
Khor C.C., Chapman S.J., Vannberg F.O., Dunne A., Murphy C., Ling E.Y., Frodsham A.J., Walley A.J., Kyrieleis O., Khan A., Aucan C., Segal S., Moore C.E., Knox K., Campbell S.J., Lienhardt C., Scott A., Aaby P. expand/collapse author list , Sow O.Y., Grignani R.T., Sillah J., Sirugo G., Peshu N., Williams T.N., Maitland K., Davies R.J.O., Kwiatkowski D.P., Day N.P., Yala D., Crook D.W., Marsh K., Berkley J.A., O'Neill L.A.J., Hill A.V.S.
Nat. Genet. 39:523-528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-180, POSSIBLE INVOLVEMENT IN PROTECTION AGAINST INVASIVE PNEUMOCOCCAL DISEASE; BACTEREMIA; MALARIA AND TUBERCULOSIS.
[19]"Low frequency of the TIRAP S180L polymorphism in Africa, and its potential role in malaria, sepsis, and leprosy."
Hamann L., Kumpf O., Schuring R.P., Alpsoy E., Bedu-Addo G., Bienzle U., Oskam L., Mockenhaupt F.P., Schumann R.R.
BMC Med. Genet. 10:65-65(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-180.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF406652 mRNA. Translation: AAL01160.1.
AF378129 mRNA. Translation: AAL05627.1.
AF410783 mRNA. Translation: AAL05036.1.
AY576785 mRNA. Translation: AAT90417.1.
AY576786 mRNA. Translation: AAT90418.1.
AY576787 mRNA. Translation: AAT90419.1.
AB446477 mRNA. Translation: BAG55254.1.
AK124298 mRNA. Translation: BAG54027.1.
AK313147 mRNA. Translation: BAG35965.1.
AY282416 Genomic DNA. Translation: AAP31973.1.
AP001318 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67687.1.
CH471065 Genomic DNA. Translation: EAW67689.1.
BC032474 mRNA. Translation: AAH32474.1.
RefSeqNP_001034750.1. NM_001039661.1.
NP_683708.1. NM_148910.2.
UniGeneHs.537126.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y92X-ray3.01A79-221[»]
3UB2X-ray2.40A78-221[»]
3UB3X-ray2.75A78-221[»]
3UB4X-ray3.10A78-221[»]
4FZ5X-ray3.60A/B72-221[»]
4LQDX-ray2.45A81-221[»]
ProteinModelPortalP58753.
SMRP58753. Positions 79-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125325. 35 interactions.
IntActP58753. 28 interactions.
MINTMINT-4950450.
STRING9606.ENSP00000376445.

PTM databases

PhosphoSiteP58753.

Polymorphism databases

DMDM50403750.

Proteomic databases

PaxDbP58753.
PRIDEP58753.

Protocols and materials databases

DNASU114609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392678; ENSP00000376445; ENSG00000150455. [P58753-2]
ENST00000392679; ENSP00000376446; ENSG00000150455. [P58753-1]
ENST00000392680; ENSP00000376447; ENSG00000150455. [P58753-1]
ENST00000479770; ENSP00000436967; ENSG00000150455. [P58753-1]
GeneID114609.
KEGGhsa:114609.
UCSCuc001qdl.1. human. [P58753-2]
uc001qdm.1. human. [P58753-1]

Organism-specific databases

CTD114609.
GeneCardsGC11P126153.
HGNCHGNC:17192. TIRAP.
HPAHPA054431.
MIM606252. gene.
607948. phenotype.
610799. phenotype.
611162. phenotype.
614382. phenotype.
neXtProtNX_P58753.
PharmGKBPA134972842.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80263.
HOGENOMHOG000068972.
HOVERGENHBG054203.
KOK05403.
OMAAELRFMY.
PhylomeDBP58753.
TreeFamTF330734.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP58753.

Gene expression databases

ArrayExpressP58753.
BgeeP58753.
CleanExHS_MAL.
HS_TIRAP.
GenevestigatorP58753.

Family and domain databases

Gene3D3.40.50.10140. 1 hit.
InterProIPR000157. TIR_dom.
IPR017279. Tol-interleuk_rcpt_adapt_Tirap.
[Graphical view]
PANTHERPTHR22662. PTHR22662. 1 hit.
PfamPF13676. TIR_2. 1 hit.
[Graphical view]
PIRSFPIRSF037750. TIR_Tirap. 1 hit.
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi114609.
NextBio79099.
PROP58753.
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Entry information

Entry nameTIRAP_HUMAN
AccessionPrimary (citable) accession number: P58753
Secondary accession number(s): B3KW65 expand/collapse secondary AC list , Q56UH9, Q56UI0, Q8N5E5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 119 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM