Q96F44 · TRI11_HUMAN

  • Protein
    E3 ubiquitin-protein ligase TRIM11
  • Gene
    TRIM11
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX (By similarity).
Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (By similarity).
May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (By similarity).
May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity).
Mediates MED15 ubiquitination leading to proteasomal degradation (PubMed:16904669).
May contribute to the innate restriction of retroviruses (PubMed:18248090).
Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression (PubMed:18248090).
Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain (PubMed:18248090).
May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle (PubMed:18248090).
Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (PubMed:27498865).
Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (PubMed:27498865).

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 site92Zn2+ (UniProtKB | ChEBI)
Binding site95Zn2+ (UniProtKB | ChEBI)
Binding site114Zn2+ (UniProtKB | ChEBI)
Binding site120Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleoplasm
Molecular Functionprotein domain specific binding
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processinnate immune response
Biological Processnegative regulation of AIM2 inflammasome complex assembly
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of neurogenesis
Biological Processnegative regulation of viral entry into host cell
Biological Processnegative regulation of viral transcription
Biological Processpositive regulation of viral entry into host cell
Biological Processprotein autoubiquitination
Biological Processprotein ubiquitination
Biological Processregulation of gene expression
Biological Processsuppression of viral release by host

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase TRIM11
  • EC number
  • Alternative names
    • Protein BIA1
    • RING finger protein 92
    • Tripartite motif-containing protein 11

Gene names

    • Name
      TRIM11
    • Synonyms
      RNF92

Organism names

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

Accessions

  • Primary accession
    Q96F44
  • Secondary accessions
    • A6NKE2
    • B2RB82
    • B3KUS3
    • B4DX88
    • Q5VSU1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis53Abolished E3 ubiquitin-protein ligase activity.
Mutagenesis56Abolished E3 ubiquitin-protein ligase activity.
Mutagenesis169Does not affect autoubiquitination.
Mutagenesis366Does not affect autoubiquitination.
Mutagenesis458Reduced autoubiquitination, leading to abolish interaction with SQSTM1/p62.

Variants

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

The viewer provides 438 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 chain, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00000562151-468UniProtE3 ubiquitin-protein ligase TRIM11
Modified residue85UniProtPhosphoserine
Modified residue (large scale data)85PRIDEPhosphoserine
Cross-link458UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Autoubiquitinated upon DNA stimulation; autoubiquitination at Lys-458 promotes interaction with SQSTM1/p62 and recruitment of AIM2 to autophagosomes.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Binds cytoplasmic tail of integrin alpha-1 (PubMed:11331580).
Interacts with the HN peptide (By similarity).
Interacts with PHOX2B (By similarity).
Interacts (when autoubiquitinated) with SQSTM1/p62; promoting AIM2 recruitment to autophagosomes (PubMed:27498865).
Interacts with AIM2; promoting its autophagy-dependent degradation (PubMed:27498865).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q96F44MED15 Q96RN55EBI-851809, EBI-394506

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for zinc finger, coiled coil, domain.

TypeIDPosition(s)Description
Zinc finger16-57RING-type
Zinc finger87-128B box-type
Coiled coil129-208
Domain268-461B30.2/SPRY

Domain

The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6 (By similarity).
They are also involved in MED15-binding (PubMed:16904669).
The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins.

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.

Q96F44-1

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
    468
  • Mass (Da)
    52,774
  • Last updated
    2002-12-06 v2
  • Checksum
    8DE4BDF79F221739
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ

Q96F44-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 288-385: DVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGS → RCGGPRWGDDSRRGPAKDLGSQPRVLCPATASSKLTVSWWWVVGKTSSAHTSDISCVGIFTPNNSSTSGNELGIQGFHSALNRIASADTTGVSTDPTD
    • 386-468: Missing

Q96F44-3

  • Name
    3
  • Note
    May be due to competing acceptor splice site.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
R4GNB9R4GNB9_HUMANTRIM11228
R4GNC3R4GNC3_HUMANTRIM1154
R4GMV1R4GMV1_HUMANTRIM11343

Sequence caution

The sequence AAH11629.1 differs from that shown. Reason: Erroneous initiation
The sequence BAG53535.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAG63300.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_039628169in isoform 3
Sequence conflict234in Ref. 2; BAG53535
Sequence conflict260in Ref. 2; BAG37129
Alternative sequenceVSP_012057288-385in isoform 2
Sequence conflict289in Ref. 2; BAG53535
Sequence conflict319in Ref. 2; BAG53535
Alternative sequenceVSP_012058386-468in isoform 2
Sequence conflict395-398in Ref. 5; AAG53498
Sequence conflict467in Ref. 5; AAG53498

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF327056
EMBL· GenBank· DDBJ
AAM63957.1
EMBL· GenBank· DDBJ
mRNA
AK074866
EMBL· GenBank· DDBJ
BAC11254.1
EMBL· GenBank· DDBJ
mRNA
AK314539
EMBL· GenBank· DDBJ
BAG37129.1
EMBL· GenBank· DDBJ
mRNA
AK097825
EMBL· GenBank· DDBJ
BAG53535.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK301859
EMBL· GenBank· DDBJ
BAG63300.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AL670729
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC011629
EMBL· GenBank· DDBJ
AAH11629.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC069227
EMBL· GenBank· DDBJ
AAH69227.1
EMBL· GenBank· DDBJ
mRNA
AF220125
EMBL· GenBank· DDBJ
AAG53498.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp