Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

TIR domain-containing adapter molecule 1

Gene

TICAM1

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

Functioni

Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively.3 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Apoptosis, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_1503. Ligand-dependent caspase activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_355217. TRAF3 deficiency - HSE.
REACT_355281. TICAM1 deficiency - HSE.
REACT_6809. MyD88-independent TLR3/TLR4 cascade.
SignaLinkiQ8IUC6.

Names & Taxonomyi

Protein namesi
Recommended name:
TIR domain-containing adapter molecule 1
Short name:
TICAM-1
Alternative name(s):
Proline-rich, vinculin and TIR domain-containing protein B
Putative NF-kappa-B-activating protein 502H
Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta
Short name:
MyD88-3
Short name:
TIR domain-containing adapter protein inducing IFN-beta
Gene namesi
Name:TICAM1
Synonyms:PRVTIRB, TRIF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:18348. TICAM1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endosome membrane Source: Reactome
  • ripoptosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Herpes simplex encephalitis 4 (HSE4)1 Publication

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

Disease descriptionA rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.

See also OMIM:614850
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861S → L in HSE4. 1 Publication
Corresponds to variant rs146550489 [ dbSNP | Ensembl ].
VAR_069082

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881E → A: Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-252 and A-303. 1 Publication
Mutagenesisi252 – 2521E → A: Loss of TCAM1-induced NF-kappa-B activation. Reduces interaction with TRAF6 and activation of NF-kappa-B signaling pathway; when associated with A-88 and A-303. 2 Publications
Mutagenesisi281 – 2811D → E: Resistant to caspase cleavage, no effect on TRIM38-mediated degradation; when associated with E-289. 1 Publication
Mutagenesisi289 – 2891D → E: Resistant to caspase cleavage, no effect on TRIM38-mediated degradation; when associated with E-281. 1 Publication
Mutagenesisi303 – 3031E → A: Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-88 and A-252. 1 Publication
Mutagenesisi434 – 4341P → H: Abolishes interaction with TLR3. 1 Publication
Mutagenesisi493 – 4931E → A: Loss of TCAM1-induced NF-kappa-B and IRF3 activation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614850. phenotype.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA142670812.

Polymorphism and mutation databases

BioMutaiTICAM1.
DMDMi74727957.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 712712TIR domain-containing adapter molecule 1PRO_0000317663Add
BLAST

Post-translational modificationi

Phosphorylated by TBK1.1 Publication
Polyubiquitinated by TRIM38 with 'Lys-48'-linked chains, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8IUC6.
PaxDbiQ8IUC6.
PRIDEiQ8IUC6.

PTM databases

PhosphoSiteiQ8IUC6.

Expressioni

Tissue specificityi

Ubiquitously expressed but with higher levels in liver.2 Publications

Gene expression databases

BgeeiQ8IUC6.
CleanExiHS_TICAM1.
ExpressionAtlasiQ8IUC6. baseline and differential.
GenevestigatoriQ8IUC6.

Organism-specific databases

HPAiHPA042460.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts (via the TIR domain) with TLR3; mediates TLR3 signaling. Interacts with AZI2, TBK1, IRF3 and IRF7. Interacts with TICAM2 in TLR4 recruitment. Interaction with PIAS4 inhibits the TICAM1-induced NF-kappa-B, IRF and IFNB1 activation. Interacts with IKBKB and IKBKE. Interaction with SARM1 blocks TICAM1-dependent transcription factor activation. Interacts with TRAF3 (By similarity). Interacts with TRAF6. Interacts with TRAFD1 (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi127114. 27 interactions.
DIPiDIP-33490N.
IntActiQ8IUC6. 4 interactions.
MINTiMINT-1202912.
STRINGi9606.ENSP00000248244.

Structurei

Secondary structure

1
712
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169Combined sources
Helixi20 – 3011Combined sources
Helixi40 – 5011Combined sources
Helixi54 – 629Combined sources
Turni63 – 664Combined sources
Helixi68 – 769Combined sources
Beta strandi83 – 853Combined sources
Helixi93 – 10513Combined sources
Helixi111 – 12717Combined sources
Helixi133 – 14412Combined sources
Beta strandi369 – 3713Combined sources
Helixi406 – 41712Combined sources
Beta strandi431 – 4333Combined sources
Helixi444 – 4474Combined sources
Beta strandi448 – 4558Combined sources
Helixi462 – 47514Combined sources
Turni477 – 4804Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi492 – 4943Combined sources
Helixi503 – 5064Combined sources
Beta strandi508 – 5103Combined sources
Beta strandi513 – 5164Combined sources
Helixi520 – 5278Combined sources
Helixi530 – 5356Combined sources
Turni536 – 5405Combined sources
Helixi541 – 5433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1XNMR-A387-545[»]
2M63NMR-A1-156[»]
3RC4X-ray1.50B360-372[»]
4BSXX-ray2.23A/B/C/D1-153[»]
4C0MX-ray2.80A/B/C/D1-153[»]
ProteinModelPortaliQ8IUC6.
SMRiQ8IUC6. Positions 1-156, 386-545.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IUC6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini390 – 46071TIRAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 153153TRIF-NTD1 PublicationAdd
BLAST
Regioni512 – 712201Sufficient to induce apoptosisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 918TRAF6-binding
Motifi248 – 2558TRAF6-binding
Motifi299 – 30911TRAF6-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi213 – 371159Pro-richAdd
BLAST
Compositional biasi614 – 67865Pro-richAdd
BLAST

Domaini

The N-terminal region is essential for activation of the IFNB promoter activity.3 Publications
The N-terminal domain (TRIF-NTD) is globular and consists of two alpha-helical subdomains connected by a 14-residue linker. It shares structural similarity with IFIT family members N-terminal regions.1 Publication

Sequence similaritiesi

Contains 1 TIR domain.Curated

Phylogenomic databases

eggNOGiNOG67739.
GeneTreeiENSGT00510000049574.
HOGENOMiHOG000068973.
HOVERGENiHBG108551.
InParanoidiQ8IUC6.
KOiK05842.
OMAiEEKLCPA.
OrthoDBiEOG7GFB4H.
PhylomeDBiQ8IUC6.
TreeFamiTF336953.

Family and domain databases

InterProiIPR025735. RHIM_dom.
IPR017278. TICAM1.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF12721. RHIM. 1 hit.
[Graphical view]
PIRSFiPIRSF037744. TIR_Ticam. 1 hit.
SUPFAMiSSF52200. SSF52200. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8IUC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACTGPSLPS AFDILGAAGQ DKLLYLKHKL KTPRPGCQGQ DLLHAMVLLK
60 70 80 90 100
LGQETEARIS LEALKADAVA RLVARQWAGV DSTEDPEEPP DVSWAVARLY
110 120 130 140 150
HLLAEEKLCP ASLRDVAYQE AVRTLSSRDD HRLGELQDEA RNRCGWDIAG
160 170 180 190 200
DPGSIRTLQS NLGCLPPSSA LPSGTRSLPR PIDGVSDWSQ GCSLRSTGSP
210 220 230 240 250
ASLASNLEIS QSPTMPFLSL HRSPHGPSKL CDDPQASLVP EPVPGGCQEP
260 270 280 290 300
EEMSWPPSGE IASPPELPSS PPPGLPEVAP DATSTGLPDT PAAPETSTNY
310 320 330 340 350
PVECTEGSAG PQSLPLPILE PVKNPCSVKD QTPLQLSVED TTSPNTKPCP
360 370 380 390 400
PTPTTPETSP PPPPPPPSST PCSAHLTPSS LFPSSLESSS EQKFYNFVIL
410 420 430 440 450
HARADEHIAL RVREKLEALG VPDGATFCED FQVPGRGELS CLQDAIDHSA
460 470 480 490 500
FIILLLTSNF DCRLSLHQVN QAMMSNLTRQ GSPDCVIPFL PLESSPAQLS
510 520 530 540 550
SDTASLLSGL VRLDEHSQIF ARKVANTFKP HRLQARKAMW RKEQDTRALR
560 570 580 590 600
EQSQHLDGER MQAAALNAAY SAYLQSYLSY QAQMEQLQVA FGSHMSFGTG
610 620 630 640 650
APYGARMPFG GQVPLGAPPP FPTWPGCPQP PPLHAWQAGT PPPPSPQPAA
660 670 680 690 700
FPQSLPFPQS PAFPTASPAP PQSPGLQPLI IHHAQMVQLG LNNHMWNQRG
710
SQAPEDKTQE AE
Length:712
Mass (Da):76,422
Last modified:March 1, 2003 - v1
Checksum:i5D071E3BE9240D9A
GO

Sequence cautioni

The sequence AAO85488.1 differs from that shown. Reason: Frameshift at positions 141, 148 and 161. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471D → T in AAO85488 (Ref. 6) Curated
Sequence conflicti150 – 1501G → W in AAO85488 (Ref. 6) Curated
Sequence conflicti162 – 1621L → S in AAO85488 (Ref. 6) Curated
Sequence conflicti633 – 65927Missing in AAO85488 (Ref. 6) CuratedAdd
BLAST
Sequence conflicti660 – 6601S → P in AAO85488 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461M → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_038789
Natural varianti75 – 751R → C.
Corresponds to variant rs11466719 [ dbSNP | Ensembl ].
VAR_051416
Natural varianti186 – 1861S → L in HSE4. 1 Publication
Corresponds to variant rs146550489 [ dbSNP | Ensembl ].
VAR_069082
Natural varianti275 – 2751L → V.
Corresponds to variant rs11466721 [ dbSNP | Ensembl ].
VAR_051417
Natural varianti666 – 6661A → T.
Corresponds to variant rs11466724 [ dbSNP | Ensembl ].
VAR_051418

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093555 mRNA. Translation: BAC44839.1.
AB086380 mRNA. Translation: BAC55579.1.
AB446484 mRNA. Translation: BAG55261.1.
AB097023 mRNA. Translation: BAC77376.1.
BC009860 mRNA. Translation: AAH09860.2.
BC136556 mRNA. Translation: AAI36557.1.
BC136557 mRNA. Translation: AAI36558.1.
AF492646 mRNA. Translation: AAO85488.1. Frameshift.
AF070530 mRNA. Translation: AAC28630.1.
CCDSiCCDS12136.1.
RefSeqiNP_891549.1. NM_182919.3.
UniGeneiHs.29344.

Genome annotation databases

EnsembliENST00000248244; ENSP00000248244; ENSG00000127666.
GeneIDi148022.
KEGGihsa:148022.
UCSCiuc002mbi.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093555 mRNA. Translation: BAC44839.1.
AB086380 mRNA. Translation: BAC55579.1.
AB446484 mRNA. Translation: BAG55261.1.
AB097023 mRNA. Translation: BAC77376.1.
BC009860 mRNA. Translation: AAH09860.2.
BC136556 mRNA. Translation: AAI36557.1.
BC136557 mRNA. Translation: AAI36558.1.
AF492646 mRNA. Translation: AAO85488.1. Frameshift.
AF070530 mRNA. Translation: AAC28630.1.
CCDSiCCDS12136.1.
RefSeqiNP_891549.1. NM_182919.3.
UniGeneiHs.29344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1XNMR-A387-545[»]
2M63NMR-A1-156[»]
3RC4X-ray1.50B360-372[»]
4BSXX-ray2.23A/B/C/D1-153[»]
4C0MX-ray2.80A/B/C/D1-153[»]
ProteinModelPortaliQ8IUC6.
SMRiQ8IUC6. Positions 1-156, 386-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127114. 27 interactions.
DIPiDIP-33490N.
IntActiQ8IUC6. 4 interactions.
MINTiMINT-1202912.
STRINGi9606.ENSP00000248244.

PTM databases

PhosphoSiteiQ8IUC6.

Polymorphism and mutation databases

BioMutaiTICAM1.
DMDMi74727957.

Proteomic databases

MaxQBiQ8IUC6.
PaxDbiQ8IUC6.
PRIDEiQ8IUC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248244; ENSP00000248244; ENSG00000127666.
GeneIDi148022.
KEGGihsa:148022.
UCSCiuc002mbi.4. human.

Organism-specific databases

CTDi148022.
GeneCardsiGC19M004815.
HGNCiHGNC:18348. TICAM1.
HPAiHPA042460.
MIMi607601. gene.
614850. phenotype.
neXtProtiNX_Q8IUC6.
Orphaneti1930. Herpetic encephalitis.
PharmGKBiPA142670812.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG67739.
GeneTreeiENSGT00510000049574.
HOGENOMiHOG000068973.
HOVERGENiHBG108551.
InParanoidiQ8IUC6.
KOiK05842.
OMAiEEKLCPA.
OrthoDBiEOG7GFB4H.
PhylomeDBiQ8IUC6.
TreeFamiTF336953.

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_1503. Ligand-dependent caspase activation.
REACT_150361. TRIF-mediated programmed cell death.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25351. TRAF6 mediated induction of TAK1 complex.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_355217. TRAF3 deficiency - HSE.
REACT_355281. TICAM1 deficiency - HSE.
REACT_6809. MyD88-independent TLR3/TLR4 cascade.
SignaLinkiQ8IUC6.

Miscellaneous databases

ChiTaRSiTICAM1. human.
EvolutionaryTraceiQ8IUC6.
GenomeRNAii148022.
NextBioi85815.
PROiQ8IUC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IUC6.
CleanExiHS_TICAM1.
ExpressionAtlasiQ8IUC6. baseline and differential.
GenevestigatoriQ8IUC6.

Family and domain databases

InterProiIPR025735. RHIM_dom.
IPR017278. TICAM1.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF12721. RHIM. 1 hit.
[Graphical view]
PIRSFiPIRSF037744. TIR_Ticam. 1 hit.
SUPFAMiSSF52200. SSF52200. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling."
    Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S.
    J. Immunol. 169:6668-6672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH IRF3; TLR2 AND TLR3.
  2. "TICAM-1, an adapter molecule that participates in Toll-like receptor 3 mediated interferon-beta induction."
    Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T.
    Nat. Immunol. 4:161-167(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TLR3, SUBUNIT, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF PRO-434.
    Tissue: Lung.
  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].
  4. "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  5. "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].
    Tissue: Ovary and Testis.
  6. "PRVTIRB is a differentially expressed gene."
    Begum N.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 137-712.
  7. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-712.
    Tissue: Brain.
  8. "TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing adapter protein involved in TIR signaling."
    Bin L.-H., Xu L.-G., Shu H.-B.
    J. Biol. Chem. 278:24526-24532(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TICAM2.
  9. "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 TRAF6 AND TBK1, PHOSPHORYLATION BY TBK1, MOTIF, MUTAGENESIS OF GLU-88; GLU-252 AND GLU-303.
  10. "PIASy represses TRIF-induced ISRE and NF-kappaB activation but not apoptosis."
    Zhang J., Xu L.G., Han K.J., Wei X., Shu H.B.
    FEBS Lett. 570:97-101(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIAS4.
  11. "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
    Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
    J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKB; IKBKE; IRF3; IRF7; TBK1 AND TRAF6, DOMAIN.
  12. "Toll-like receptor 3-mediated activation of NF-kappaB and IRF3 diverges at Toll-IL-1 receptor domain-containing adapter inducing IFN-beta."
    Jiang Z., Mak T.W., Sen G., Li X.
    Proc. Natl. Acad. Sci. U.S.A. 101:3533-3538(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF6, MUTAGENESIS OF GLU-252 AND GLU-493.
  13. "NF-kappaB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation."
    Sasai M., Oshiumi H., Matsumoto M., Inoue N., Fujita F., Nakanishi M., Seya T.
    J. Immunol. 174:27-30(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AZI2.
  14. "The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling."
    Carty M., Goodbody R., Schroeder M., Stack J., Moynagh P.N., Bowie A.G.
    Nat. Immunol. 7:1074-1081(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SARM1.
  15. "The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling."
    O'Neill L.A., Bowie A.G.
    Nat. Rev. Immunol. 7:353-364(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "TRIM38 negatively regulates TLR3-mediated IFN-beta signaling by targeting TRIF for degradation."
    Xue Q., Zhou Z., Lei X., Liu X., He B., Wang J., Hung T.
    PLoS ONE 7:E46825-E46825(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY TRIM38, MUTAGENESIS OF ASP-281 AND ASP-289.
  18. "The TLR signalling adaptor TRIF/TICAM-1 has an N-terminal helical domain with structural similarity to IFIT proteins."
    Ullah M.O., Ve T., Mangan M., Alaidarous M., Sweet M.J., Mansell A., Kobe B.
    Acta Crystallogr. D 69:2420-2430(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 1-153, TRIF-NTD REGION.
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-46.
  20. Cited for: VARIANT HSE4 LEU-186.

Entry informationi

Entry nameiTCAM1_HUMAN
AccessioniPrimary (citable) accession number: Q8IUC6
Secondary accession number(s): B3Y691
, O75532, Q86XP8, Q96GA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2003
Last modified: May 27, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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.