TRADD TNFRSF1A associated via death domain [Homo sapiens (human)] - Gene

Summary

Official Symbol: TRADDprovided by HGNC
Official Full Name: TNFRSF1A associated via death domainprovided by HGNC
Primary source: HGNC:HGNC:12030
See related: Ensembl:ENSG00000102871 MIM:603500; AllianceGenome:HGNC:12030
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: Hs.89862
Summary: The protein encoded by this gene is a death domain containing adaptor molecule that interacts with TNFRSF1A/TNFR1 and mediates programmed cell death signaling and NF-kappaB activation. This protein binds adaptor protein TRAF2, reduces the recruitment of inhibitor-of-apoptosis proteins (IAPs) by TRAF2, and thus suppresses TRAF2 mediated apoptosis. This protein can also interact with receptor TNFRSF6/FAS and adaptor protein FADD/MORT1, and is involved in the Fas-induced cell death pathway. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in stomach (RPKM 7.8), spleen (RPKM 7.4) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 16q22.1

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	16	NC_000016.10 (67154185..67159909, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	16	NC_060940.1 (72948477..72954201, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	16	NC_000016.9 (67188088..67193812, complement)

Chromosome 16 - NC_000016.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Roles of the adaptor protein tumor necrosis factor receptor type 1-associated death domain protein (TRADD) in human diseases.
Title: Roles of the adaptor protein tumor necrosis factor receptor type 1-associated death domain protein (TRADD) in human diseases.
RIPK1 and TRADD Regulate TNF-Induced Signaling and Ripoptosome Formation.
Title: RIPK1 and TRADD Regulate TNF-Induced Signaling and Ripoptosome Formation.
Structural basis of NF-kappaB signaling by the p75 neurotrophin receptor interaction with adaptor protein TRADD through their respective death domains.
Title: Structural basis of NF-κB signaling by the p75 neurotrophin receptor interaction with adaptor protein TRADD through their respective death domains.
Modulating TRADD to restore cellular homeostasis and inhibit apoptosis.
Title: Modulating TRADD to restore cellular homeostasis and inhibit apoptosis.
Coronin 1B regulates the TNFalpha-induced apoptosis of HUVECs by mediating the interaction between TRADD and FADD.
Title: Coronin 1B regulates the TNFα-induced apoptosis of HUVECs by mediating the interaction between TRADD and FADD.
SNHG9, delivered by adipocyte-derived exosomes, alleviates inflammation and apoptosis of endothelial cells through suppressing TRADD expression.
Title: SNHG9, delivered by adipocyte-derived exosomes, alleviates inflammation and apoptosis of endothelial cells through suppressing TRADD expression.
The TRADD C-terminal death domain comprises two super-secondary structures, an all-helix Greek key motif and a beta-hairpin motif flanked by two alpha helices, which make it unique among all known C-terminal death domain structures.
Title: Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily.
Translocation of TRADD to DSBs into the nucleus contributes to cell survival in response to DNA damage through an activation of NHEJ DNA repair.
Title: Nuclear TRADD prevents DNA damage-mediated death by facilitating non-homologous end-joining repair.
potential biological significance of TRADD mediated inflammatory response in the development of uterine leiomyoma, is reported.
Title: Identification of TRADD as a potential biomarker in human uterine leiomyoma through iTRAQ based proteomic profiling.
we found that ORF3 protein downregulates TLR3-mediated NF-kappaB signaling via TRADD and RIP1. Our findings provide a new perspective on the cellular response in HEV infection and expand our understanding of the molecular mechanisms of Hepatitis E virus (HEV) pathogenesis in innate immunity.
Title: The ORF3 Protein of Genotype 1 Hepatitis E Virus Suppresses TLR3-induced NF-κB Signaling via TRADD and RIP1.

Submit: New GeneRIF Correction See all GeneRIFs (44)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Variation

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See Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	The mRNA expression levels for alpha-tubulin, TRADD, IFN-gamma R2, GAS1, MADD, NF-kappaB, I-kappa B, 14-3-3 protein, APaf1, PARP, IGF-1 receptor, RB1, Rb2/p130, ARC, and caspase 6 are upregulated in human neuronal cells after treatment with HIV-1 gp120	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH69054 (e-PCR)
- UniSTS:27785

TRADD_1477 (e-PCR)
- UniSTS:281066

RH78922 (e-PCR)
- UniSTS:21246

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables death domain binding	IPI Inferred from Physical Interaction more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IEA Inferred from Electronic Annotation more info
enables protein-macromolecule adaptor activity	IDA Inferred from Direct Assay more info	PubMed
enables signaling adaptor activity	ISS Inferred from Sequence or Structural Similarity more info
enables transmembrane receptor protein tyrosine kinase adaptor activity	IBA Inferred from Biological aspect of Ancestor more info
enables transmembrane receptor protein tyrosine kinase adaptor activity	IPI Inferred from Physical Interaction more info	PubMed
enables tumor necrosis factor receptor binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in TRAIL-activated apoptotic signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic process	TAS Traceable Author Statement more info	PubMed
involved_in canonical NF-kappaB signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cell surface receptor protein tyrosine kinase signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in cellular response to tumor necrosis factor	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in extrinsic apoptotic signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in extrinsic apoptotic signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in extrinsic apoptotic signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in extrinsic apoptotic signaling pathway via death domain receptors	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of NF-kappaB transcription factor activity	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of apoptotic process	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of canonical NF-kappaB signal transduction	IEP Inferred from Expression Pattern more info	PubMed
involved_in positive regulation of canonical NF-kappaB signal transduction	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of hair follicle development	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of inflammatory response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in signal transduction	TAS Traceable Author Statement more info	PubMed
involved_in tumor necrosis factor-mediated signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in tumor necrosis factor-mediated signaling pathway	IEP Inferred from Expression Pattern more info	PubMed
involved_in tumor necrosis factor-mediated signaling pathway	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasmic side of plasma membrane	IC Inferred by Curator more info	PubMed
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in cytosol	TAS Traceable Author Statement more info
part_of death-inducing signaling complex	TAS Traceable Author Statement more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
part_of receptor complex	IDA Inferred from Direct Assay more info	PubMed
part_of tumor necrosis factor receptor superfamily complex	IBA Inferred from Biological aspect of Ancestor more info
part_of tumor necrosis factor receptor superfamily complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: tumor necrosis factor receptor type 1-associated DEATH domain protein

Names: TNFR1-associated death domain protein; tumor necrosis factor receptor type 1 associated death domain protein; tumor necrosis factor receptor-1-associated protein

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001323552.2 → NP_001310481.1 tumor necrosis factor receptor type 1-associated DEATH domain protein

Status: REVIEWED

Source sequence(s)

AC074143, BT006934, CA426418, DA353575

Consensus CDS

CCDS10829.1

UniProtKB/Swiss-Prot

B2RDS3, B3KQZ9, Q15628, Q52NZ1

Conserved Domains (2) summary

pfam09034
Location:51 → 160

TRADD_N; TRADD, N-terminal domain

cl14633
Location:215 → 304

DD; Death Domain Superfamily of protein-protein interaction domains
NM_003789.4 → NP_003780.1 tumor necrosis factor receptor type 1-associated DEATH domain protein

See identical proteins and their annotated locations for NP_003780.1

Status: REVIEWED

Source sequence(s)

BC004491, CA426418, DA353575

Consensus CDS

CCDS10829.1

UniProtKB/Swiss-Prot

B2RDS3, B3KQZ9, Q15628, Q52NZ1

Related

ENSP00000341268.4, ENST00000345057.9

Conserved Domains (2) summary

pfam09034
Location:51 → 160

TRADD_N; TRADD, N-terminal domain

cl14633
Location:215 → 304

DD; Death Domain Superfamily of protein-protein interaction domains

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000016.10 Reference GRCh38.p14 Primary Assembly

Range

67154185..67159909 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate T2T-CHM13v2.0

Genomic

NC_060940.1 Alternate T2T-CHM13v2.0

Range

72948477..72954201 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_153425.1: Suppressed sequence

Description

NM_153425.1: This RefSeq was permanently suppressed because currently there is not sufficient data to support this transcript variant.