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Protein

TIR domain-containing adapter molecule 2

Gene

TICAM2

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

Functioni

Functions as sorting adapter in LPS-TLR4 signaling to regulate the MYD88-independent pathway during the innate immune response to LPS. Physically bridges TLR4 and TICAM1 and functionally transmits LPS-TRL4 signal to TICAM1; signaling is proposed to occur in early endosomes after endocytosis of TLR4. May also be involved in IL1-triggered NF-kappa-B activation, functioning upstream of IRAK1, IRAK2, TRAF6, and IKBKB; however, reports are controversial. Involved in IL-18 signaling and is proposed to function as a sorting adaptor for MYD88 in IL-18 signaling during adaptive immune response.
Isoform 2: Proposed to inhibit LPS-TLR4 signaling at the late endosome by interaction with isoform 1 thereby disrupting the association of isoform 1 with TICAM1. May be involved in TLR4 degradation in late endosomes.

GO - Molecular functioni

  • phospholipid binding Source: Ensembl
  • signal transducer activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_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_6809. MyD88-independent TLR3/TLR4 cascade.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinkiQ86XR7.

Names & Taxonomyi

Protein namesi
Recommended name:
TIR domain-containing adapter molecule 2
Short name:
TICAM-2
Alternative name(s):
Putative NF-kappa-B-activating protein 502
TRIF-related adapter molecule
Toll-like receptor adaptor protein 3
Toll/interleukin-1 receptor domain-containing protein
Short name:
MyD88-4
Gene namesi
Name:TICAM2
Synonyms:TIRAP3, TIRP, TRAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:21354. TICAM2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

  • early endosome Source: UniProtKB
  • early endosome membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB
  • endosome membrane Source: Reactome
  • Golgi apparatus Source: UniProtKB-SubCell
  • late endosome Source: UniProtKB
  • late endosome membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Results in relocalization from membrane to cytosol; Loss of ability to transduce TLR4-signal. 1 Publication
Mutagenesisi6 – 61S → A: Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B. 1 Publication
Mutagenesisi10 – 101S → A: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B. 1 Publication
Mutagenesisi14 – 141S → A: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B. 1 Publication
Mutagenesisi16 – 161S → A: Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal. 1 Publication
Mutagenesisi16 – 161S → E: Significant decrease of localization in the membrane. 1 Publication
Mutagenesisi116 – 1161P → H: Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation. 2 Publications
Mutagenesisi117 – 1171C → H: Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4. 2 Publications

Organism-specific databases

PharmGKBiPA134881157.
PA165660570.

Polymorphism and mutation databases

BioMutaiTICAM2.
DMDMi74727858.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 235234TIR domain-containing adapter molecule 2PRO_0000317689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei16 – 161Phosphoserine; by PKC/PRKCE1 Publication

Post-translational modificationi

Phosphorylated by PRKCE in response to LPS. Phosphorylation is essential for its function. It is depleted from the membrane upon phosphorylation.1 Publication
Isoform 1 is myristoylated. Required for membrane association which is critical for its ability to initiate efficient signaling.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ86XR7.
PaxDbiQ86XR7.
PRIDEiQ86XR7.

PTM databases

PhosphoSiteiQ86XR7.

Expressioni

Tissue specificityi

Expressed in spleen, prostate, testis, uterus, small intestine, colon, peripheral blood leukocytes, heart, placenta, lung, liver, skeletal muscle, and pancreas Isoform 2 is ubiquitously expressed (at lower levels than isoform 1).3 Publications

Gene expression databases

BgeeiQ86XR7.
CleanExiHS_TICAM2.
GenevisibleiQ86XR7. HS.

Organism-specific databases

HPAiHPA008960.

Interactioni

Subunit structurei

Homodimer. Interacts with TLR4, TICAM1, IRF3 and IRF7 in response to LPS. Interacts with IL1R1, IL1RAP, IRAK2, IRAK3 and TRAF6. Interacts with protein kinase-inactive mutants of IRAK1 and IRAK4. Isoform 1 interacts with isoform 2; the interaction occurs in late endosomes and disrupts the interaction between isoform 1 and TICAM1. Interacts with MYD88; the interaction decreases after IL-18 stimulation in a time-dependent manner. Interacts with IL18R1 and IL18RAP.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-525927,EBI-10172134

Protein-protein interaction databases

BioGridi131694. 10 interactions.
DIPiDIP-33488N.
IntActiQ86XR7. 11 interactions.
STRINGi9606.ENSP00000386341.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi80 – 845Combined sources
Beta strandi87 – 893Combined sources
Helixi90 – 10011Combined sources
Turni101 – 1044Combined sources
Beta strandi108 – 1114Combined sources
Turni112 – 1143Combined sources
Beta strandi118 – 1203Combined sources
Helixi125 – 1284Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi135 – 1373Combined sources
Helixi141 – 15313Combined sources
Helixi155 – 1606Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi176 – 1783Combined sources
Helixi182 – 1843Combined sources
Turni187 – 1915Combined sources
Beta strandi196 – 1994Combined sources
Helixi202 – 2098Combined sources
Helixi212 – 23221Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1WNMR-A75-235[»]
ProteinModelPortaliQ86XR7.
SMRiQ86XR7. Positions 75-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 232160TIRPROSITE-ProRule annotationAdd
BLAST

Domaini

The TIR domain mediates the interaction with TRAF6 and MYD88.1 Publication

Sequence similaritiesi

Contains 1 TIR domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG43987.
GeneTreeiENSGT00670000097656.
HOGENOMiHOG000068974.
HOVERGENiHBG102133.
InParanoidiQ86XR7.
KOiK05409.
OMAiTRVAYCH.
OrthoDBiEOG70ZZP7.
PhylomeDBiQ86XR7.
TreeFamiTF313000.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000157. TIR_dom.
IPR015720. TMP21-related.
[Graphical view]
PANTHERiPTHR22811. PTHR22811. 1 hit.
PfamiPF13676. TIR_2. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86XR7-1) [UniParc]FASTAAdd to basket

Also known as: TRAM

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.

« Hide

        10         20         30         40         50
MGIGKSKINS CPLSLSWGKR HSVDTSPGYH ESDSKKSEDL SLCNVAEHSN
60 70 80 90 100
TTEGPTGKQE GAQSVEEMFE EEAEEEVFLK FVILHAEDDT DEALRVQNLL
110 120 130 140 150
QDDFGIKPGI IFAEMPCGRQ HLQNLDDAVN GSAWTILLLT ENFLRDTWCN
160 170 180 190 200
FQFYTSLMNS VNRQHKYNSV IPMRPLNNPL PRERTPFALQ TINALEEESR
210 220 230
GFPTQVERIF QESVYKTQQT IWKETRNMVQ RQFIA
Length:235
Mass (Da):26,916
Last modified:June 1, 2003 - v1
Checksum:i2D1171F9B04D9C4C
GO
Isoform 2 (identifier: Q86XR7-2) [UniParc]FASTAAdd to basket

Also known as: TAG, TRAM adaptor with GOLD domain

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGIGKSKINSCPLSLSWGKR → MPRPGSAQRW...EDLNTRVAYW

Show »
Length:404
Mass (Da):46,173
Checksum:iC539E6D9B8185764
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MGIGK…SWGKR → MPRPGSAQRWAAVAGRWGCR LLALLLLVPGPGGASEITFE LPDNAKQCFYEDIAQGTKCT LEFQVITGGHYDVDCRLEDP DGKVLYKEMKKQYDSFTFTA SKNGTYKFCFSNEFSTFTHK TVYFDFQVGEDPPLFPSENR VSALTQMESACVSIHEALKS VIDYQTHFRLREAQGRSRAE DLNTRVAYW in isoform 2. 1 PublicationVSP_047437Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY275836 mRNA. Translation: AAP81748.1.
AB109098 mRNA. Translation: BAC98399.1.
AB091054 mRNA. Translation: BAC98397.1.
AY232653 mRNA. Translation: AAO74498.1.
AY304581 mRNA. Translation: AAQ97430.1.
AY304582 mRNA. Translation: AAQ97431.1.
AY304583 mRNA. Translation: AAQ97432.1.
AY304584 mRNA. Translation: AAQ97433.1.
AB446491 mRNA. Translation: BAG55268.1.
AB097022 mRNA. Translation: BAC77375.1.
AC010226 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48960.1.
CH471086 Genomic DNA. Translation: EAW48961.1.
BC109265 mRNA. Translation: AAI09266.1.
BC109266 mRNA. Translation: AAI09267.1.
CCDSiCCDS4119.1. [Q86XR7-1]
RefSeqiNP_001157940.1. NM_001164468.3. [Q86XR7-2]
NP_001157941.1. NM_001164469.3.
NP_067681.1. NM_021649.7. [Q86XR7-1]
UniGeneiHs.718838.

Genome annotation databases

EnsembliENST00000427199; ENSP00000415139; ENSG00000243414.
GeneIDi100302736.
353376.
KEGGihsa:100302736.
hsa:353376.
UCSCiuc003krc.3. human. [Q86XR7-1]
uc003kre.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY275836 mRNA. Translation: AAP81748.1.
AB109098 mRNA. Translation: BAC98399.1.
AB091054 mRNA. Translation: BAC98397.1.
AY232653 mRNA. Translation: AAO74498.1.
AY304581 mRNA. Translation: AAQ97430.1.
AY304582 mRNA. Translation: AAQ97431.1.
AY304583 mRNA. Translation: AAQ97432.1.
AY304584 mRNA. Translation: AAQ97433.1.
AB446491 mRNA. Translation: BAG55268.1.
AB097022 mRNA. Translation: BAC77375.1.
AC010226 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48960.1.
CH471086 Genomic DNA. Translation: EAW48961.1.
BC109265 mRNA. Translation: AAI09266.1.
BC109266 mRNA. Translation: AAI09267.1.
CCDSiCCDS4119.1. [Q86XR7-1]
RefSeqiNP_001157940.1. NM_001164468.3. [Q86XR7-2]
NP_001157941.1. NM_001164469.3.
NP_067681.1. NM_021649.7. [Q86XR7-1]
UniGeneiHs.718838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1WNMR-A75-235[»]
ProteinModelPortaliQ86XR7.
SMRiQ86XR7. Positions 75-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131694. 10 interactions.
DIPiDIP-33488N.
IntActiQ86XR7. 11 interactions.
STRINGi9606.ENSP00000386341.

PTM databases

PhosphoSiteiQ86XR7.

Polymorphism and mutation databases

BioMutaiTICAM2.
DMDMi74727858.

Proteomic databases

MaxQBiQ86XR7.
PaxDbiQ86XR7.
PRIDEiQ86XR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000427199; ENSP00000415139; ENSG00000243414.
GeneIDi100302736.
353376.
KEGGihsa:100302736.
hsa:353376.
UCSCiuc003krc.3. human. [Q86XR7-1]
uc003kre.3. human.

Organism-specific databases

CTDi100302736.
353376.
GeneCardsiGC05M114942.
HGNCiHGNC:21354. TICAM2.
HPAiHPA008960.
MIMi608321. gene.
neXtProtiNX_Q86XR7.
PharmGKBiPA134881157.
PA165660570.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43987.
GeneTreeiENSGT00670000097656.
HOGENOMiHOG000068974.
HOVERGENiHBG102133.
InParanoidiQ86XR7.
KOiK05409.
OMAiTRVAYCH.
OrthoDBiEOG70ZZP7.
PhylomeDBiQ86XR7.
TreeFamiTF313000.

Enzyme and pathway databases

ReactomeiREACT_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_6809. MyD88-independent TLR3/TLR4 cascade.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
SignaLinkiQ86XR7.

Miscellaneous databases

GeneWikiiTICAM2.
NextBioi20796124.
PROiQ86XR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ86XR7.
CleanExiHS_TICAM2.
GenevisibleiQ86XR7. HS.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000157. TIR_dom.
IPR015720. TMP21-related.
[Graphical view]
PANTHERiPTHR22811. PTHR22811. 1 hit.
PfamiPF13676. TIR_2. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, INTERACTION WITH TRAF6; IL1R1; IL1RAP; IRAK1; IRAK2; IRAK3; IRAK4; TIRAP AND TICAM1, TISSUE SPECIFICITY.
  2. "TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-beta."
    Oshiumi H., Sasai M., Shida K., Fujita T., Matsumoto M., Seya T.
    J. Biol. Chem. 278:49751-49762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, INTERACTION WITH TICAM1 AND TLR4, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-116 AND CYS-117.
  3. "LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF."
    Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T.
    J. Exp. Med. 198:1043-1055(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TICAM1; TIRAP; TLR4; IRF3 AND IRF7, MUTAGENESIS OF PRO-116 AND CYS-117.
  4. "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).
  5. "TAG, a splice variant of the adaptor TRAM, negatively regulates the adaptor MyD88-independent TLR4 pathway."
    Palsson-McDermott E.M., Doyle S.L., McGettrick A.F., Hardy M., Husebye H., Banahan K., Gong M., Golenbock D., Espevik T., O'Neill L.A.
    Nat. Immunol. 10:579-586(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "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.
  7. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 1).
  10. "The myristoylation of TRIF-related adaptor molecule is essential for Toll-like receptor 4 signal transduction."
    Rowe D.C., McGettrick A.F., Latz E., Monks B.G., Gay N.J., Yamamoto M., Akira S., O'Neill L.A., Fitzgerald K.A., Golenbock D.T.
    Proc. Natl. Acad. Sci. U.S.A. 103:6299-6304(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
  11. "Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-like receptor 4 signaling."
    McGettrick A.F., Brint E.K., Palsson-McDermott E.M., Rowe D.C., Golenbock D.T., Gay N.J., Fitzgerald K.A., O'Neill L.A.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-16, MUTAGENESIS OF SER-6; SER-10; SER-14 AND SER-16.
  12. "TRAM is involved in IL-18 signaling and functions as a sorting adaptor for MyD88."
    Ohnishi H., Tochio H., Kato Z., Kawamoto N., Kimura T., Kubota K., Yamamoto T., Funasaka T., Nakano H., Wong R.W., Shirakawa M., Kondo N.
    PLoS ONE 7:E38423-E38423(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYD88; IL18R1 AND IL18RAP.

Entry informationi

Entry nameiTCAM2_HUMAN
AccessioniPrimary (citable) accession number: Q86XR7
Secondary accession number(s): B3Y698, Q6JUT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 126 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.