Q5TA31 · RN187_HUMAN

  • Protein
    E3 ubiquitin-protein ligase RNF187
  • Gene
    RNF187
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8.

Caution

This sequence initiates at a CTG codon.

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionubiquitin-protein transferase activity
Biological Processpositive regulation of cell population proliferation
Biological Processpositive regulation of DNA-templated transcription
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein autoubiquitination
Biological Processprotein K48-linked ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RNF187
  • EC number
  • Alternative names
    • RING domain AP1 coactivator 1 (RACO-1)
    • RING finger protein 187
    • RING-type E3 ubiquitin transferase RNF187

Gene names

    • Name
      RNF187

Organism names

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

Accessions

  • Primary accession
    Q5TA31
  • Secondary accessions
    • A6NL57
    • Q6P2J7
    • Q6PJR0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis1Loss of protein expression.
Mutagenesis12Increased RNF187 stability and reduced polyubiquitination; when associated with A-15.
Mutagenesis15Increased RNF187 stability and reduced polyubiquitination; when associated with A-12.
Mutagenesis98Abolishes ubiquitination by TRIM7; when associated with K-109.
Mutagenesis109Abolishes ubiquitination by TRIM7; when associated with K-98.
Mutagenesis195No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-223 and R-224.
Mutagenesis223No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-224.
Mutagenesis224No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-223.

Variants

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

The viewer provides 241 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, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002782411-235E3 ubiquitin-protein ligase RNF187
Modified residue98Asymmetric dimethylarginine; by PRMT1
Modified residue109Asymmetric dimethylarginine; by PRMT1
Cross-link195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked polyubiquitination (PubMed:20852630).
'Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein (PubMed:20852630).
'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-223 and Lys-224) and are thus mutually exclusive (PubMed:20852630).
Other sites of ubiquitination are not excluded (PubMed:20852630).
'Lys-63'-linked polyubiquitination by TRIM7 in response to growth factor signaling via the MEK/ERK pathway enhances protein stability (PubMed:25851810).
Arginine methylation by PRMT1 stabilizes RNF187 by facilitating K63-linked ubiquitin chain formation, and enables dimerization, c-Jun interaction and subsequent AP1 target gene expression.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer (PubMed:23624934).
Interacts with JUN, independently of JUN phosphorylation (PubMed:20852630).
Interacts (via C-terminus) with TRIM7 (PubMed:25851810).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5TA31ZNF417 Q8TAU33EBI-6868977, EBI-740727
BINARY Q5TA31ZNF835 Q9Y2P03EBI-6868977, EBI-5667516

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for zinc finger.

TypeIDPosition(s)Description
Zinc finger12-53RING-type

Domain

The RING-type zinc finger domain is required for E3 ligase activity.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    235
  • Mass (Da)
    26,190
  • Last updated
    2011-05-03 v2
  • Checksum
    6C16442F7419CD25
MALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1X7SBW3A0A1X7SBW3_HUMANRNF187235

Sequence caution

The sequence AAH12758.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence AAH12758.1 differs from that shown. Reason: Miscellaneous discrepancy Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL139288
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC012758
EMBL· GenBank· DDBJ
AAH12758.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC064481
EMBL· GenBank· DDBJ
AAH64481.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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