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Protein

E3 ubiquitin-protein ligase RNF187

Gene

Rnf187

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 53RING-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF187 (EC:2.3.2.27)
Alternative name(s):
RING domain AP1 coactivator 1
Short name:
RACO-1
RING finger protein 187
RING-type E3 ubiquitin transferase RNF187Curated
Gene namesi
Name:Rnf187
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1914224. Rnf187.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Shuttles between the cytoplasm and the nucleus.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002782421 – 236E3 ubiquitin-protein ligase RNF187Add BLAST236

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98Asymmetric dimethylarginine; by PRMT1By similarity1
Modified residuei109Asymmetric dimethylarginine; by PRMT1By similarity1
Modified residuei200PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the absence of growth factors and MAP3K1-induced 'Lys-63'-linked polyubiquitination. 'Lys-48'-autoubiquitination leads to degradation by the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination results in the stabilization of the protein. 'Lys-48'- and 'Lys-63'-linked polyubiquitinations occur most probably on the same 3 C-terminal lysine residues (Lys-195, Lys-224 and Lys-225) and are thus mutually exclusive. Other sites of ubiquitination are not excluded.By similarity
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.By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BFX1.
MaxQBiQ8BFX1.
PaxDbiQ8BFX1.
PeptideAtlasiQ8BFX1.
PRIDEiQ8BFX1.

PTM databases

iPTMnetiQ8BFX1.
PhosphoSitePlusiQ8BFX1.

Expressioni

Gene expression databases

CleanExiMM_RNF187.
ExpressionAtlasiQ8BFX1. baseline and differential.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with JUN, independently of JUN phosphorylation.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8BFX1.
SMRiQ8BFX1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri12 – 53RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410JC6A. Eukaryota.
ENOG4111A5E. LUCA.
GeneTreeiENSGT00390000009510.
HOGENOMiHOG000154159.
HOVERGENiHBG093909.
InParanoidiQ8BFX1.
KOiK15709.
TreeFamiTF351093.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
PfamiView protein in Pfam
PF00097. zf-C3HC4. 1 hit.
SMARTiView protein in SMART
SM00184. RING. 1 hit.
PROSITEiView protein in PROSITE
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BFX1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPAGPADA ICALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP
60 70 80 90 100
ECADDCWQRA VEPSRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD
110 120 130 140 150
GDPLCSACRM AAGPEPPEWE PRWRKALRGK ENKGSVEIMR KDLNDARDLH
160 170 180 190 200
GQAESAAAVW KGHVMDRRKK ALTDYKKLRA FFVEEEEHFL QEAEKDEGAS
210 220 230
EDDELADPAD RFRSLLQAVS ELEKKHRNLG LSMLLQ
Length:236
Mass (Da):26,313
Last modified:May 3, 2011 - v2
Checksum:i48B73A52619F2768
GO

Sequence cautioni

The sequence AAH96522 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH96522 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA92754 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAA92754 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC29916 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAC29916 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC40679 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAC40679 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030190 mRNA. Translation: BAA92754.1. Sequence problems.
AK037991 mRNA. Translation: BAC29916.1. Sequence problems.
AK075944 mRNA. Translation: BAC36073.1.
AK076158 mRNA. Translation: BAC36225.1.
AK088973 mRNA. Translation: BAC40679.1. Sequence problems.
AL662809 Genomic DNA. Translation: CAM24481.1.
BC072613 mRNA. Translation: AAH72613.1.
BC096522 mRNA. Translation: AAH96522.1. Sequence problems.
CCDSiCCDS78953.1.
RefSeqiNP_071868.2. NM_022423.2.
UniGeneiMm.249986.

Genome annotation databases

EnsembliENSMUST00000217262; ENSMUSP00000150777; ENSMUSG00000020496.
GeneIDi108660.
KEGGimmu:108660.
UCSCiuc007jcq.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiRN187_MOUSE
AccessioniPrimary (citable) accession number: Q8BFX1
Secondary accession number(s): Q4VA64
, Q8C2B0, Q8CAS0, Q9JMF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 3, 2011
Last modified: August 30, 2017
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

This sequence initiates at a CTG codon.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways