O14545 · TRAD1_HUMAN

  • Protein
    TRAF-type zinc finger domain-containing protein 1
  • Gene
    TRAFD1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrion
Molecular Functionmetal ion binding
Biological Processnegative regulation of innate immune response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    TRAF-type zinc finger domain-containing protein 1
  • Alternative names
    • Protein FLN29

Gene names

    • Name
      TRAFD1
    • Synonyms
      FLN29

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O14545
  • Secondary accessions
    • A8K5L6
    • B4DI89

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 655 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00002784572-582UniProtTRAF-type zinc finger domain-containing protein 1
Modified residue (large scale data)98PRIDEPhosphoserine
Modified residue191UniProtPhosphoserine
Modified residue (large scale data)272PRIDEPhosphoserine
Modified residue278UniProtPhosphoserine
Modified residue (large scale data)278PRIDEPhosphoserine
Modified residue (large scale data)280PRIDEPhosphoserine
Modified residue320UniProtPhosphoserine
Modified residue (large scale data)323PRIDEPhosphothreonine
Modified residue (large scale data)325PRIDEPhosphoserine
Modified residue326UniProtPhosphoserine
Modified residue (large scale data)326PRIDEPhosphoserine
Modified residue327UniProtPhosphoserine
Modified residue (large scale data)327PRIDEPhosphoserine
Modified residue409UniProtPhosphoserine
Modified residue (large scale data)409PRIDEPhosphoserine
Modified residue (large scale data)414PRIDEPhosphothreonine
Modified residue415UniProtPhosphoserine
Modified residue (large scale data)415PRIDEPhosphoserine
Modified residue430UniProtPhosphoserine
Modified residue (large scale data)430PRIDEPhosphoserine
Modified residue (large scale data)433PRIDEPhosphotyrosine
Modified residue470UniProtPhosphoserine
Modified residue (large scale data)470PRIDEPhosphoserine
Modified residue (large scale data)479PRIDEPhosphoserine
Modified residue (large scale data)480PRIDEPhosphoserine
Modified residue (large scale data)487PRIDEPhosphoserine
Modified residue (large scale data)491PRIDEPhosphoserine
Modified residue (large scale data)501PRIDEPhosphoserine
Modified residue (large scale data)552PRIDEPhosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 (By similarity).
Interacts with TRAF6

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O14545CFTR P135699EBI-1396921, EBI-349854
BINARY O14545HTT P428585EBI-1396921, EBI-466029
BINARY O14545NGLY1 Q96IV07EBI-1396921, EBI-6165879

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for zinc finger, region, compositional bias.

TypeIDPosition(s)Description
Zinc finger27-103TRAF-type
Region217-236Disordered
Region401-582Disordered
Compositional bias415-431Basic and acidic residues
Compositional bias432-502Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O14545-1

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.

  • Length
    582
  • Mass (Da)
    64,841
  • Last updated
    1998-01-01 v1
  • Checksum
    4937682988851AC0
MAEFLDDQETRLCDNCKKEIPVFNFTIHEIHCQRNIGMCPTCKEPFPKSDMETHMAAEHCQVTCKCNKKLEKRLLKKHEETECPLRLAVCQHCDLELSILKLKEHEDYCGARTELCGNCGRNVLVKDLKTHPEVCGREGEEKRNEVAIPPNAYDESWGQDGIWIASQLLRQIEALDPPMRLPRRPLRAFESDVFHNRTTNQRNITAQVSIQNNLFEEQERQERNRGQQPPKEGGEESANLDFMLALSLQNEGQASSVAEQDFWRAVCEADQSHGGPRSLSDIKGAADEIMLPCEFCEELYPEELLIDHQTSCNPSRALPSLNTGSSSPRGVEEPDVIFQNFLQQAASNQLDSLMGLSNSHPVEESIIIPCEFCGVQLEEEVLFHHQDQCDQRPATATNHVTEGIPRLDSQPQETSPELPRRRVRHQGDLSSGYLDDTKQETANGPTSCLPPSRPINNMTATYNQLSRSTSGPRPGCQPSSPCVPKLSNSDSQDIQGRNRDSQNGAIAPGHVSVIRPPQNLYPENIVPSFSPGPSGRYGASGRSEGGRNSRVTPAAANYRSRTAKAKPSKQQGAGDAEEEEEE

O14545-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 134-164: VCGREGEEKRNEVAIPPNAYDESWGQDGIWI → LKNKRGRKGIEANSPPKRVVKRVQTWTSCWP
    • 165-582: Missing

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8VVF3F8VVF3_HUMANTRAFD1135
F8VWK2F8VWK2_HUMANTRAFD194
F8VNX8F8VNX8_HUMANTRAFD1283
S4R2Z9S4R2Z9_HUMANTRAFD172

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_056085134-164in isoform 2
Sequence conflict138in Ref. 2; BAF84020
Alternative sequenceVSP_056086165-582in isoform 2
Compositional bias415-431Basic and acidic residues
Compositional bias432-502Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB007447
EMBL· GenBank· DDBJ
BAA22541.1
EMBL· GenBank· DDBJ
mRNA
AK291331
EMBL· GenBank· DDBJ
BAF84020.1
EMBL· GenBank· DDBJ
mRNA
AK295474
EMBL· GenBank· DDBJ
BAG58401.1
EMBL· GenBank· DDBJ
mRNA
AC073575
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC003553
EMBL· GenBank· DDBJ
AAH03553.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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