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Protein

E3 ubiquitin-protein ligase RNF187

Gene

Rnf187

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1308636. 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_00004079291 – 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 residuei200PhosphoserineCombined sources1

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

PaxDbiD3Z8N2.
PRIDEiD3Z8N2.

PTM databases

iPTMnetiD3Z8N2.
PhosphoSitePlusiD3Z8N2.

Interactioni

Subunit structurei

Homodimer. Interacts with JUN, independently of JUN phosphorylation.By similarity

Protein-protein interaction databases

BioGridi262005. 1 interactor.
STRINGi10116.ENSRNOP00000065797.

Structurei

3D structure databases

ProteinModelPortaliD3Z8N2.
SMRiD3Z8N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-CH-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.
InParanoidiD3Z8N2.
KOiK15709.
TreeFamiTF351093.

Family and domain databases

CDDicd00162. RING. 1 hit.
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.

D3Z8N2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPAGPAEA 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
DDDELADPAD RFRSLLQAVS ELEKKHRNLG LSMLLQ
Length:236
Mass (Da):26,313
Last modified:May 3, 2011 - v2
Checksum:i5C6477677464D3D6
GO

Sequence cautioni

The sequence EDM04565 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EDM04566 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM031715 mRNA. No translation available.
FM033519 mRNA. No translation available.
CH473948 Genomic DNA. Translation: EDM04565.1. Sequence problems.
CH473948 Genomic DNA. Translation: EDM04566.1. Sequence problems.
RefSeqiNP_001157736.1. NM_001164264.1.
UniGeneiRn.100245.

Genome annotation databases

GeneIDi360533.
KEGGirno:360533.
UCSCiRGD:1308636. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM031715 mRNA. No translation available.
FM033519 mRNA. No translation available.
CH473948 Genomic DNA. Translation: EDM04565.1. Sequence problems.
CH473948 Genomic DNA. Translation: EDM04566.1. Sequence problems.
RefSeqiNP_001157736.1. NM_001164264.1.
UniGeneiRn.100245.

3D structure databases

ProteinModelPortaliD3Z8N2.
SMRiD3Z8N2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi262005. 1 interactor.
STRINGi10116.ENSRNOP00000065797.

PTM databases

iPTMnetiD3Z8N2.
PhosphoSitePlusiD3Z8N2.

Proteomic databases

PaxDbiD3Z8N2.
PRIDEiD3Z8N2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi360533.
KEGGirno:360533.
UCSCiRGD:1308636. rat.

Organism-specific databases

CTDi149603.
RGDi1308636. Rnf187.

Phylogenomic databases

eggNOGiENOG410JC6A. Eukaryota.
ENOG4111A5E. LUCA.
InParanoidiD3Z8N2.
KOiK15709.
TreeFamiTF351093.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiPR:D3Z8N2.

Family and domain databases

CDDicd00162. RING. 1 hit.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiRN187_RAT
AccessioniPrimary (citable) accession number: D3Z8N2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 10, 2017
This is version 40 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.