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Protein

E3 ubiquitin-protein ligase RNF187

Gene

RNF187

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 MAPK8.1 Publication

Caution

This sequence initiates at a CTG codon.1 Publication

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

  • metal ion binding Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000168159.10
HGNCiHGNC:27146 RNF187
MIMi613754 gene
neXtProtiNX_Q5TA31

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → A: Loss of protein expression. 1 Publication1
Mutagenesisi12C → A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-15. 1 Publication1
Mutagenesisi15C → A: Increased RNF187 stability and reduced polyubiquitination; when associated with A-12. 1 Publication1
Mutagenesisi98R → K: Abolishes ubiquitination by TRIM7; when associated with K-109. 1 Publication1
Mutagenesisi109R → K: Abolishes ubiquitination by TRIM7; when associated with K-98. 1 Publication1
Mutagenesisi195K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-223 and R-224. 1 Publication1
Mutagenesisi223K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-224. 1 Publication1
Mutagenesisi224K → R: No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-223. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000168159
PharmGKBiPA142671058

Polymorphism and mutation databases

DMDMi332278146

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002782411 – 235E3 ubiquitin-protein ligase RNF187Add BLAST235

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei98Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei109Asymmetric dimethylarginine; by PRMT11 Publication1
Cross-linki195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki224Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

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).2 Publications
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.2 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

EPDiQ5TA31
MaxQBiQ5TA31
PaxDbiQ5TA31
PeptideAtlasiQ5TA31
PRIDEiQ5TA31

PTM databases

iPTMnetiQ5TA31
PhosphoSitePlusiQ5TA31

Expressioni

Gene expression databases

BgeeiENSG00000168159
CleanExiHS_RNF187
ExpressionAtlasiQ5TA31 baseline and differential
GenevisibleiQ5TA31 HS

Organism-specific databases

HPAiHPA030098

Interactioni

Subunit structurei

Homodimer (PubMed:23624934). Interacts with JUN, independently of JUN phosphorylation (PubMed:20852630). Interacts (via C-terminus) with TRIM7 (PubMed:25851810).3 Publications

Protein-protein interaction databases

BioGridi127223, 16 interactors
MINTiQ5TA31
STRINGi9606.ENSP00000306396

Structurei

3D structure databases

ProteinModelPortaliQ5TA31
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

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
InParanoidiQ5TA31
KOiK15709
OrthoDBiEOG091G0I4F
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.

Q5TA31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPAGPAEA ACALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP
60 70 80 90 100
ECADDCWQRA VEPGRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD
110 120 130 140 150
AGPLCAACRM AAGPEPPEWE PRWRKALRGK ENKGSVEIMR KDLNDARDLH
160 170 180 190 200
GQAESAAAVW KGHVMDRRKK ALTDYKKLRA FFVEEEEHFL QEAEKEEGLP
210 220 230
EDELADPTER FRSLLQAVSE LEKKHRNLGL SMLLQ
Length:235
Mass (Da):26,190
Last modified:May 3, 2011 - v2
Checksum:i6C16442F7419CD25
GO

Sequence cautioni

The sequence AAH12758 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH12758 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI23328 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139288 Genomic DNA Translation: CAI23328.1 Sequence problems.
BC012758 mRNA Translation: AAH12758.1 Sequence problems.
BC064481 mRNA Translation: AAH64481.1
CCDSiCCDS76271.1
RefSeqiNP_001010858.2, NM_001010858.2
UniGeneiHs.356377
Hs.679030

Genome annotation databases

EnsembliENST00000639044; ENSP00000492846; ENSG00000168159
GeneIDi149603
KEGGihsa:149603
UCSCiuc057qfa.1 human

Similar proteinsi

Entry informationi

Entry nameiRN187_HUMAN
AccessioniPrimary (citable) accession number: Q5TA31
Secondary accession number(s): A6NL57, Q6P2J7, Q6PJR0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 3, 2011
Last modified: May 23, 2018
This is version 97 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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