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

    Gene ID: 7188, updated on 21-Dec-2019

    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
    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

    Genomic context

    See TRAF5 in Genome Data Viewer
    Location:
    1q32.3
    Exon count:
    14
    Annotation release Status Assembly Chr Location
    109.20191205 current GRCh38.p13 (GCF_000001405.39) 1 NC_000001.11 (211326594..211374946)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 1 NC_000001.10 (211499849..211548403)

    Chromosome 1 - NC_000001.11Genomic Context describing neighboring genes Neighboring gene PRELID1 pseudogene 5 Neighboring gene uncharacterized LOC105372902 Neighboring gene REST corepressor 3 Neighboring gene uncharacterized LOC107985258 Neighboring gene uncharacterized LOC107985259 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

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    identical protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    thioesterase binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    thioesterase binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    tumor necrosis factor receptor binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    ubiquitin protein ligase binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    ubiquitin protein ligase binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    apoptotic process IEA
    Inferred from Electronic Annotation
    more info
     
    positive regulation of DNA-binding transcription factor activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    positive regulation of I-kappaB kinase/NF-kappaB signaling IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    positive regulation of I-kappaB kinase/NF-kappaB signaling IEP
    Inferred from Expression Pattern
    more info
    PubMed 
    positive regulation of NF-kappaB transcription factor activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    positive regulation of NF-kappaB transcription factor activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    regulation of apoptotic process IEA
    Inferred from Electronic Annotation
    more info
     
    signal transduction IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    Component Evidence Code Pubs
    CD40 receptor complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    CD40 receptor complex ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    centrosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    cytoplasmic side of plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    cytoplasmic side of plasma membrane ISS
    Inferred from Sequence or Structural Similarity
    more info
     
    cytosol IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein-containing complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 

    General protein information

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

    NCBI Reference Sequences (RefSeq)

    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
      O00463
      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
      UniProtKB/Swiss-Prot
      O00463
      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_004619.3NP_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
      O00463
      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_145759.2NP_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
      O00463
      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: Homo sapiens Updated Annotation Release 109.20191205

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

    Reference GRCh38.p13 Primary Assembly

    Genomic

    1. NC_000001.11 Reference GRCh38.p13 Primary Assembly

      Range
      211326594..211374946
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011509960.3XP_011508262.1  TNF receptor-associated factor 5 isoform X2

      See identical proteins and their annotated locations for XP_011508262.1

      UniProtKB/Swiss-Prot
      O00463
      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_011509957.3XP_011508259.1  TNF receptor-associated factor 5 isoform X1

      Conserved Domains (3) summary
      smart00184
      Location:109145
      RING; Ring finger
      pfam02176
      Location:257315
      zf-TRAF; TRAF-type zinc finger
      cl02446
      Location:478624
      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. XM_024449459.1XP_024305227.1  TNF receptor-associated factor 5 isoform X4

      Conserved Domains (2) summary
      pfam02176
      Location:258316
      zf-TRAF; TRAF-type zinc finger
      cd16642
      Location:107149
      mRING-HC-C3HC3D_TRAF5; Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins
    4. XM_017002221.2XP_016857710.1  TNF receptor-associated factor 5 isoform X3

      UniProtKB/Swiss-Prot
      O00463
      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 ...
    5. XM_011509959.3XP_011508261.1  TNF receptor-associated factor 5 isoform X2

      See identical proteins and their annotated locations for XP_011508261.1

      UniProtKB/Swiss-Prot
      O00463
      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 ...
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