RNF187
entrez
149603
canonical
uniprot
Q5TA31
canonical
ensembl
ENSG00000168159
resolver
ensembl
ENSG00000285426
resolver
ensp
ENSP00000306396
resolver
ensp
ENSP00000495836
resolver
enst
ENST00000305943
resolver
enst
ENST00000643372
resolver
genesymbol
RNF187
resolver
hgnc
HGNC:27146
resolver
uniprot
A6NL57
resolver
uniprot
Q6P2J7
resolver
uniprot
Q6PJR0
resolver
uniprot_entry
RN187_HUMAN
resolver
uniprot_sec
A6NL57
resolver
uniprot_sec
Q6P2J7
resolver
uniprot_sec
Q6PJR0
resolver
amino_acid_sequence
MALPAGPAEAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDGPFPCPECADDCWQRAVEPGRPPLSRRLLALEEAAAAPARDGPASEAALQLLCRADAGPLCAACRMAAGPEPPEWEPRWRKALRGKENKGSVEIMRKDLNDARDLHGQAESAAAVWKGHVMDRRKKALTDYKKLRAFFVEEEEHFLQEAEKEEGLPEDELADPTERFRSLLQAVSELEKKHRNLGLSMLLQ
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
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. {ECO:0000269|PubMed:20852630}.
uniprot
proteins
mass_dalton
26190
uniprot
proteins
mutagenesis
MUTAGEN 1; /note="M->A: Loss of protein expression."; /evidence="ECO:0000269|PubMed:20852630"; MUTAGEN 12; /note="C->A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-15."; /evidence="ECO:0000269|PubMed:20852630"; MUTAGEN 15; /note="C->A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-12."; /evidence="ECO:0000269|PubMed:20852630"; MUTAGEN 98; /note="R->K: Abolishes ubiquitination by TRIM7; when associated with K-109."; /evidence="ECO:0000269|PubMed:25851810"; MUTAGEN 109; /note="R->K: Abolishes ubiquitination by TRIM7; when associated with K-98."; /evidence="ECO:0000269|PubMed:25851810"; MUTAGEN 195; /note="K->R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-223 and R-224."; /evidence="ECO:0000269|PubMed:20852630"; MUTAGEN 223; /note="K->R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-224."; /evidence="ECO:0000269|PubMed:20852630"; MUTAGEN 224; /note="K->R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-223."; /evidence="ECO:0000269|PubMed:20852630
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:25851810}.; PTM: 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. {ECO:0000269|PubMed:20852630, ECO:0000269|PubMed:23624934}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
20852630
uniprot
proteins
pubmed
23624934
uniprot
proteins
pubmed
25851810
uniprot
proteins
sequence_length
235
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20852630}. Nucleus {ECO:0000269|PubMed:20852630}. Note=Predominantly located in the cytoplasm. Shuttles between the cytoplasm and the nucleus.
uniprot
proteins