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TRAF5 TNF receptor associated factor 5 [ Homo sapiens (human) ]

Gene ID: 7188, updated on 27-Nov-2024

Summary

Official Symbol
TRAF5provided by HGNC
Official Full Name
TNF receptor associated factor 5provided by HGNC
Primary source
HGNC:HGNC:12035
See related
Ensembl:ENSG00000082512 MIM:602356; AllianceGenome:HGNC:12035
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
RNF84; MGC:39780
Summary
The scaffold protein encoded by this gene is a member of the tumor necrosis factor receptor-associated factor (TRAF) protein family and contains a meprin and TRAF homology (MATH) domain, a RING-type zinc finger, and two TRAF-type zinc fingers. TRAF proteins are associated with, and mediate signal transduction from members of the TNF receptor superfamily. This protein is one of the components of a multiple protein complex which binds to tumor necrosis factor (TNF) receptor cytoplasmic domains and mediates TNF-induced activation. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016]
Expression
Broad expression in lymph node (RPKM 13.9), appendix (RPKM 8.7) and 24 other tissues See more
Orthologs
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Genomic context

See TRAF5 in Genome Data Viewer
Location:
1q32.3
Exon count:
13
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 1 NC_000001.11 (211326635..211374946)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 1 NC_060925.1 (210572246..210620555)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 1 NC_000001.10 (211499977..211548288)

Chromosome 1 - NC_000001.11Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105372902 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 2482 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr1:211431921-211432422 Neighboring gene H3K27ac hESC enhancer GRCh37_chr1:211432925-211433424 Neighboring gene REST corepressor 3 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr1:211498879-211499380 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 2483 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 1784 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 2484 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 1785 Neighboring gene uncharacterized LOC124904504 Neighboring gene NANOG-H3K4me1 hESC enhancer GRCh37_chr1:211550792-211551568 Neighboring gene uncharacterized LOC107985259 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 2485 Neighboring gene long intergenic non-protein coding RNA 467

Genomic regions, transcripts, and products

Expression

  • Project title: 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Up-regulation of apoptosis genes such as caspase 1, NALP1, and TNF receptor-associated factor 5 are induced by HIV-gp120/ethanol in human neurons PubMed
Nef nef The interaction of HIV-1 Nef with TRAF2, TRAF5, and TRAF6 proteins activates NF-kappaB, leading to the degradation of IkappaB-alpha and the increased phosphorylation of IKK-alpha and IKK-beta in monocyte-derived macrophages PubMed
nef HIV-1 Nef interacts with TRAF2, TRAF5, and TRAF6 proteins via its C-terminal region (residues 55-206) in monocyte-derived macrophages PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables identical protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables signaling adaptor activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables thioesterase binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables tumor necrosis factor receptor binding IEA
Inferred from Electronic Annotation
more info
 
enables ubiquitin protein ligase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables ubiquitin protein ligase binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
part_of CD40 receptor complex ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in centrosome IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
 
is_active_in cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
located_in cytoplasmic side of plasma membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in cytosol IDA
Inferred from Direct Assay
more info
PubMed 
part_of plasma membrane signaling receptor complex IBA
Inferred from Biological aspect of Ancestor
more info
 

General protein information

Preferred Names
TNF receptor-associated factor 5
Names
RING finger protein 84

NCBI Reference Sequences (RefSeq)

NEW Try the new Transcript table

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)

  1. NM_001033910.3NP_001029082.1  TNF receptor-associated factor 5 isoform b

    See identical proteins and their annotated locations for NP_001029082.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) uses an alternate in-frame splice junction compared to variant 4. The resulting isoform (b) has the same N- and C-termini but is shorter compared to isoform a. Variants 1, 2, and 3 all encode the same isoform (b).
    Source sequence(s)
    AB000509, BU676629, DB290838, U69108
    Consensus CDS
    CCDS1497.1
    UniProtKB/Swiss-Prot
    B4DIS9, B4E0A2, O00463, Q6FHY1
    Related
    ENSP00000261464.5, ENST00000261464.10
    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:183241
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:404550
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...
  2. NM_001319207.2NP_001306136.1  TNF receptor-associated factor 5 isoform a

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) represents the longest transcript and encodes the longer isoform (a).
    Source sequence(s)
    AB000509, AK303286, AL590101, GD146999
    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:194252
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:415561
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...
  3. NM_004619.4NP_004610.1  TNF receptor-associated factor 5 isoform b

    See identical proteins and their annotated locations for NP_004610.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) differs in the 5' UTR and uses an alternate in-frame splice junction compared to variant 4. The resulting isoform (b) has the same N- and C-termini but is shorter compared to isoform a. Variants 1, 2, and 3 all encode the same isoform (b).
    Source sequence(s)
    AB000509, BU676629, DB218840, U69108
    Consensus CDS
    CCDS1497.1
    UniProtKB/Swiss-Prot
    B4DIS9, B4E0A2, O00463, Q6FHY1
    Related
    ENSP00000336825.2, ENST00000336184.6
    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:183241
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:404550
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...
  4. NM_145759.3NP_665702.1  TNF receptor-associated factor 5 isoform b

    See identical proteins and their annotated locations for NP_665702.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR and uses an alternate in-frame splice junction compared to variant 4. The resulting isoform (b) has the same N- and C-termini but is shorter compared to isoform a. Variants 1, 2, and 3 all encode the same isoform (b).
    Source sequence(s)
    AB000509, BC029600, BU676629, U69108
    Consensus CDS
    CCDS1497.1
    UniProtKB/Swiss-Prot
    B4DIS9, B4E0A2, O00463, Q6FHY1
    Related
    ENSP00000355971.3, ENST00000367004.3
    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:183241
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:404550
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...

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

  1. NC_000001.11 Reference GRCh38.p14 Primary Assembly

    Range
    211326635..211374946
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011509960.4XP_011508262.1  TNF receptor-associated factor 5 isoform X2

    See identical proteins and their annotated locations for XP_011508262.1

    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:194252
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:415561
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...
  2. XM_011509957.4XP_011508259.2  TNF receptor-associated factor 5 isoform X1

  3. XM_047429574.1XP_047285530.1  TNF receptor-associated factor 5 isoform X3

  4. XM_047429572.1XP_047285528.1  TNF receptor-associated factor 5 isoform X3

  5. XM_011509959.4XP_011508261.1  TNF receptor-associated factor 5 isoform X2

    See identical proteins and their annotated locations for XP_011508261.1

    Conserved Domains (3) summary
    smart00184
    Location:4581
    RING; Ring finger
    pfam02176
    Location:194252
    zf-TRAF; TRAF-type zinc finger
    cl02446
    Location:415561
    MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060925.1 Alternate T2T-CHM13v2.0

    Range
    210572246..210620555
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)