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Protein

TRAF-interacting protein with FHA domain-containing protein A

Gene

Tifa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein which mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, resulting in the downstream activation of NF-kappa-B and AP-1 pathways. Induces the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism.By similarity1 Publication

GO - Biological processi

  • I-kappaB kinase/NF-kappaB signaling Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
TRAF-interacting protein with FHA domain-containing protein A
Alternative name(s):
TRAF2-binding protein
Gene namesi
Name:Tifa
Synonyms:T2bp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2182965. Tifa.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184TRAF-interacting protein with FHA domain-containing protein APRO_0000320690Add
BLAST

Proteomic databases

MaxQBiQ793I8.
PaxDbiQ793I8.
PRIDEiQ793I8.

PTM databases

PhosphoSiteiQ793I8.

Expressioni

Tissue specificityi

Highly expressed in the spleen and at lower levels in heart, brain, lung, liver, kidney and testes.2 Publications

Gene expression databases

BgeeiQ793I8.
ExpressionAtlasiQ793I8. baseline and differential.
GenevisibleiQ793I8. MM.

Interactioni

Subunit structurei

Homotrimer. Interacts with IRAK1, TIFAB, TRAF2 and TRAF6. Binding to TIFAB inhibits TRAF6 activation possibly by inducing a conformational change in TIFA. Binding to ZCCHC11 suppresses the TRAF6-dependent activation of NF-kappa-B.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q624062EBI-524817,EBI-448533
Traf6P701962EBI-524817,EBI-448028

Protein-protein interaction databases

BioGridi229244. 2 interactions.
IntActiQ793I8. 2 interactions.
STRINGi10090.ENSMUSP00000054036.

Structurei

3D structure databases

ProteinModelPortaliQ793I8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 10357FHAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IYNH. Eukaryota.
ENOG4111T8W. LUCA.
GeneTreeiENSGT00510000048615.
HOGENOMiHOG000072694.
HOVERGENiHBG059530.
InParanoidiQ793I8.
OMAiRNSNICH.
OrthoDBiEOG7C2R2H.
PhylomeDBiQ793I8.
TreeFamiTF333218.

Family and domain databases

InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q793I8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFEDADTE ETVTCLQMTI YHPGQQSGIF KSIRFCSKEK FPSIEVVKFG
60 70 80 90 100
RNSNMCQYTF QDKQVSRIQF VLQPFKQFNS SVLSFEIKNM SKKTSLMVDN
110 120 130 140 150
QELGYLNKMD LPYKCMLRFG EYQFLLQKED GESVESFETQ FIMSSRPLLQ
160 170 180
ENNWPTQNPI PEDGMYSSYF THRSSPSEMD ENEL
Length:184
Mass (Da):21,560
Last modified:October 11, 2005 - v1
Checksum:i1466F2A7307F03E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901M → I in BAE38653 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB062111 mRNA. Translation: BAB86903.1.
AK041891 mRNA. Translation: BAE43315.1.
AK044221 mRNA. Translation: BAC31825.1.
AK149408 mRNA. Translation: BAE28856.1.
AK149864 mRNA. Translation: BAE29133.1.
AK151651 mRNA. Translation: BAE30580.1.
AK166239 mRNA. Translation: BAE38653.1.
BC065775 mRNA. Translation: AAH65775.1.
CCDSiCCDS38628.1.
RefSeqiNP_660115.1. NM_145133.3.
XP_006501299.1. XM_006501236.2.
XP_006501300.1. XM_006501237.2.
XP_006501301.1. XM_006501238.2.
XP_006501302.1. XM_006501239.2.
UniGeneiMm.31852.

Genome annotation databases

EnsembliENSMUST00000054483; ENSMUSP00000054036; ENSMUSG00000046688.
ENSMUST00000163775; ENSMUSP00000132309; ENSMUSG00000046688.
ENSMUST00000164447; ENSMUSP00000126692; ENSMUSG00000046688.
ENSMUST00000171621; ENSMUSP00000127700; ENSMUSG00000046688.
GeneIDi211550.
KEGGimmu:211550.
UCSCiuc008rhm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB062111 mRNA. Translation: BAB86903.1.
AK041891 mRNA. Translation: BAE43315.1.
AK044221 mRNA. Translation: BAC31825.1.
AK149408 mRNA. Translation: BAE28856.1.
AK149864 mRNA. Translation: BAE29133.1.
AK151651 mRNA. Translation: BAE30580.1.
AK166239 mRNA. Translation: BAE38653.1.
BC065775 mRNA. Translation: AAH65775.1.
CCDSiCCDS38628.1.
RefSeqiNP_660115.1. NM_145133.3.
XP_006501299.1. XM_006501236.2.
XP_006501300.1. XM_006501237.2.
XP_006501301.1. XM_006501238.2.
XP_006501302.1. XM_006501239.2.
UniGeneiMm.31852.

3D structure databases

ProteinModelPortaliQ793I8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229244. 2 interactions.
IntActiQ793I8. 2 interactions.
STRINGi10090.ENSMUSP00000054036.

PTM databases

PhosphoSiteiQ793I8.

Proteomic databases

MaxQBiQ793I8.
PaxDbiQ793I8.
PRIDEiQ793I8.

Protocols and materials databases

DNASUi211550.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054483; ENSMUSP00000054036; ENSMUSG00000046688.
ENSMUST00000163775; ENSMUSP00000132309; ENSMUSG00000046688.
ENSMUST00000164447; ENSMUSP00000126692; ENSMUSG00000046688.
ENSMUST00000171621; ENSMUSP00000127700; ENSMUSG00000046688.
GeneIDi211550.
KEGGimmu:211550.
UCSCiuc008rhm.1. mouse.

Organism-specific databases

CTDi92610.
MGIiMGI:2182965. Tifa.

Phylogenomic databases

eggNOGiENOG410IYNH. Eukaryota.
ENOG4111T8W. LUCA.
GeneTreeiENSGT00510000048615.
HOGENOMiHOG000072694.
HOVERGENiHBG059530.
InParanoidiQ793I8.
OMAiRNSNICH.
OrthoDBiEOG7C2R2H.
PhylomeDBiQ793I8.
TreeFamiTF333218.

Miscellaneous databases

NextBioi373282.
PROiQ793I8.
SOURCEiSearch...

Gene expression databases

BgeeiQ793I8.
ExpressionAtlasiQ793I8. baseline and differential.
GenevisibleiQ793I8. MM.

Family and domain databases

InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of TIFA as an adapter protein that links tumor necrosis factor receptor-associated factor 6 (TRAF6) to interleukin-1 (IL-1) receptor-associated kinase-1 (IRAK-1) in IL-1 receptor signaling."
    Takatsuna H., Kato H., Gohda J., Akiyama T., Moriya A., Okamoto Y., Yamagata Y., Otsuka M., Umezawa K., Semba K., Inoue J.
    J. Biol. Chem. 278:12144-12150(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Liver, Mammary gland, Retina and Thymus.
  3. "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: Mammary glandImported.
  4. "T2BP, a novel TRAF2 binding protein, can activate NF-kappaB and AP-1 without TNF stimulation."
    Kanamori M., Suzuki H., Saito R., Muramatsu M., Hayashizaki Y.
    Biochem. Biophys. Res. Commun. 290:1108-1113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAF2, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Spleen.

Entry informationi

Entry nameiTIFA_MOUSE
AccessioniPrimary (citable) accession number: Q793I8
Secondary accession number(s): Q3TLY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 11, 2005
Last modified: May 11, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.