Q99PP6 · TR34A_MOUSE

  • Protein
    E3 ubiquitin-protein ligase TRIM34A
  • Gene
    Trim34a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Functions as antiviral protein and contributes to the defense against retroviral infections (By similarity).
Acts as a capsid-specific restriction factor with the help of TRIM5 and prevents infection from non-host-adapted retroviruses. During influenza A virus infection, promotes programmed cell death by targeting ZBP1 for 'Lys-63'-linked polyubiquitination. In turn, promotes ZBP1 recruitment of RIPK3 to mediate virus-induced programmed necrosis (By similarity).
Negatively regulates the function of mitochondria by enhancing mitochondrial depolarization leading to cytochrome c release and mitochondria-dependent apoptosis. Promotes also the formation of multinucleated giant cells by means of cell fusion and phagocytosis in epithelial cells (By similarity).
Plays an essential role in sustaining the integrity of the inner mucus layer in the colon by controlling the exocytosis of the major component of colonic mucus MUC2 from colonic goblet cells (PubMed:32094504).

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site96Zn2+ (UniProtKB | ChEBI)
Binding site99Zn2+ (UniProtKB | ChEBI)
Binding site118Zn2+ (UniProtKB | ChEBI)
Binding site124Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmitochondrion
Cellular Componentnucleoplasm
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processdefense response to virus
Biological Processinnate immune response
Biological Processpositive regulation of autophagy
Biological Processpositive regulation of canonical NF-kappaB signal transduction
Biological Processprotein polyubiquitination
Biological Processregulation of protein localization
Biological Processregulation of viral entry into host cell

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase TRIM34A
  • EC number
  • Alternative names
    • Tripartite motif-containing protein 34A

Gene names

    • Name
      Trim34a

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q99PP6
  • Secondary accessions
    • E9PYZ4
    • F8VPK2
    • Q99PP4
    • Q99PP5

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Trim34a- and TRIM34b-deficient mice show an impaired integrity of the inner mucus layer.

Variants

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

The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000562491-485E3 ubiquitin-protein ligase TRIM34A

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homotrimer. Interacts (via B-box and SPRY domain) with TRIM5.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, coiled coil, domain.

TypeIDPosition(s)Description
Zinc finger15-59RING-type
Zinc finger91-132B box-type
Coiled coil136-170
Domain282-485B30.2/SPRY

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q99PP6-1

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.

  • Name
    Alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    485
  • Mass (Da)
    55,950
  • Last updated
    2022-12-14 v3
  • Checksum
    A9B5F3590C9A2614
MASTGLTNIQEKTTCPVCQELLTKALSLGCGHRVCQACLITKKNAVINPREKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKAICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKCQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELTAVRAYWDNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILGSKCFSSGKHYWEVDVSEKKAWTLGVYTRKRTLRFDVRQRKGQPNGYHRYKPQNGYWVIGLQHGSKYSIFEDSSNCDPTVLNPFVATPLHRVGVFLDCEEGTVSFLNVTNHGSLIYKFSQCCFSQPAYPYFNPWDCPAPMTLCPLNS

Q99PP6-2

  • Name
    Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 300-339: DNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILG → GKKLQMLKSLCSDHLSQVCGSMWPYHLCLLCYLIHIMNSS
    • 340-485: Missing

Q99PP6-3

  • Name
    Gamma
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 300-326: DNFTFNPENLNLNLILSEDHRQVTSVS → GSYSVYKVGFKYRAIFLPQLPRCSTAG
    • 327-485: Missing

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict293in Ref. 1; AAG53514/AAG53513
Alternative sequenceVSP_011925300-326in isoform Gamma
Alternative sequenceVSP_011923300-339in isoform Beta
Alternative sequenceVSP_011926327-485in isoform Gamma
Alternative sequenceVSP_011924340-485in isoform Beta
Sequence conflict430in Ref. 1; AAG53512

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF220139
EMBL· GenBank· DDBJ
AAG53512.1
EMBL· GenBank· DDBJ
mRNA
AF220140
EMBL· GenBank· DDBJ
AAG53513.1
EMBL· GenBank· DDBJ
mRNA
AF220141
EMBL· GenBank· DDBJ
AAG53514.1
EMBL· GenBank· DDBJ
mRNA
AC123830
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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