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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

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF187 (EC:6.3.2.-)
Alternative name(s):
RING domain AP1 coactivator 1
Short name:
RACO-1
RING finger protein 187
Gene namesi
Name:Rnf187
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236E3 ubiquitin-protein ligase RNF187PRO_0000407929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei109 – 1091Asymmetric dimethylarginine; by PRMT1By similarity
Cross-linki195 – 195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei200 – 2001PhosphoserineCombined sources
Cross-linki224 – 224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

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).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

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiD3Z8N2.

PTM databases

iPTMnetiD3Z8N2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi262005. 1 interaction.
STRINGi10116.ENSRNOP00000065797.

Structurei

3D structure databases

ProteinModelPortaliD3Z8N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri12 – 5342RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

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 EDM04565.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EDM04566.1 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi262005. 1 interaction.
STRINGi10116.ENSRNOP00000065797.

PTM databases

iPTMnetiD3Z8N2.

Proteomic databases

PaxDbiD3Z8N2.

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

PROiD3Z8N2.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Euratools EST."
    Kube M., Klages S., Kuhl H., Thiel J., Beck A., Reinhardt R.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Identification of a co-activator that links growth factor signalling to c-Jun/AP-1 activation."
    Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.
    Nat. Cell Biol. 12:963-972(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JUN.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRN187_RAT
AccessioniPrimary (citable) accession number: D3Z8N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 8, 2016
This is version 33 of the entry and version 2 of the sequence. [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
  2. SIMILARITY comments
    Index of protein domains and families

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.