Q38HM4 · TRI63_MOUSE

  • Protein
    E3 ubiquitin-protein ligase TRIM63
  • Gene
    Trim63
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.

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.

135050100150200250300350
TypeIDPosition(s)Description
Binding site122Zn2+ (UniProtKB | ChEBI)
Binding site125Zn2+ (UniProtKB | ChEBI)
Binding site145Zn2+ (UniProtKB | ChEBI)
Binding site151Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcontractile muscle fiber
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular ComponentM band
Cellular Componentnucleus
Cellular ComponentZ disc
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processcellular response to dexamethasone stimulus
Biological Processmuscle contraction
Biological Processnegative regulation of cardiac muscle hypertrophy
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein monoubiquitination
Biological Processprotein ubiquitination
Biological Processregulation of gene expression
Biological Processresponse to denervation involved in regulation of muscle adaptation
Biological Processresponse to electrical stimulus involved in regulation of muscle adaptation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase TRIM63
  • EC number
  • Alternative names
    • Muscle-specific RING finger protein 1 (MuRF-1; MuRF1; Muscle RING finger protein 1)
    • RING-type E3 ubiquitin transferase TRIM63
    • Tripartite motif-containing protein 63

Gene names

    • Name
      Trim63
    • Synonyms
      Murf1, Rf1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q38HM4
  • Secondary accessions
    • Q8BWC4

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Localizes to the M- and Z-lines in skeletal muscle (By similarity).
Colocalizes with TNNI3 in myocytes

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal conditions. Under amino acid starvation, mice continue to synthesize muscle protein and degrade less muscle protein than wild-type, leading to a decrease in the blood levels of free amino acids. Besides, mutant mice display higher creatine kinase activity under amino acid starvation.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000562911-350E3 ubiquitin-protein ligase TRIM63

Proteomic databases

PTM databases

Expression

Induction

By hydrogen peroxide. Up-regulated in response to amino acid starvation.

Interaction

Subunit

Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 (By similarity).
Interacts with TNNI3. Forms a ternary complex with RACK1 and PRKCE. Interacts with CKM

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, region, coiled coil, domain, compositional bias.

TypeIDPosition(s)Description
Zinc finger23-79RING-type
Region74-218Interaction with TTN
Zinc finger117-159B box-type
Coiled coil207-269
Domain267-325COS
Compositional bias325-343Acidic residues
Region325-350Disordered

Domain

The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus (By similarity).
Also required for the E3 ubiquitin ligase activity
The B box-type zinc finger mediates homodimerization.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q38HM4-1

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
    350
  • Mass (Da)
    39,491
  • Last updated
    2005-11-22 v1
  • Checksum
    1840B7BB2F77DEC1
MDYKSGLIPDGNAMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLVDSCRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEEKLGFIEALILQYREQLEKSTKLVETAIQSLDEPGGATFLSSAKQLIKSNVEASKGCQLGKTEQGFENMDYFTLDLEHIAEALRAIDFGTDEEEEEFTEEEADEEEGVTTEGHQ

Q38HM4-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 111-151: SRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAH → RSVCSRTAPPLPQAPPTSRSLQLLSPAQRASTLYRRQNLSS
    • 152-350: Missing

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A2A9L4A2A9L4_MOUSETrim63352
F8VPZ1F8VPZ1_MOUSETrim63355

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict6in Ref. 2; BAC35199
Sequence conflict42in Ref. 2; BAC35199
Alternative sequenceVSP_016647111-151in isoform 2
Alternative sequenceVSP_016648152-350in isoform 2
Compositional bias325-343Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ229108
EMBL· GenBank· DDBJ
ABB16283.1
EMBL· GenBank· DDBJ
mRNA
AK052911
EMBL· GenBank· DDBJ
BAC35199.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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