RN187_RAT
ID RN187_RAT Reviewed; 236 AA.
AC D3Z8N2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=E3 ubiquitin-protein ligase RNF187;
DE EC=2.3.2.27;
DE AltName: Full=RING domain AP1 coactivator 1;
DE Short=RACO-1;
DE AltName: Full=RING finger protein 187;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF187 {ECO:0000305};
GN Name=Rnf187;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kube M., Klages S., Kuhl H., Thiel J., Beck A., Reinhardt R.;
RT "Euratools EST.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH JUN.
RX PubMed=20852630; DOI=10.1038/ncb2098;
RA Davies C.C., Chakraborty A., Cipriani F., Haigh K., Haigh J.J., Behrens A.;
RT "Identification of a co-activator that links growth factor signalling to c-
RT Jun/AP-1 activation.";
RL Nat. Cell Biol. 12:963-972(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a coactivator of
CC JUN-mediated gene activation in response to growth factor signaling via
CC the MAP3K1 pathway, independently from MAPK8.
CC {ECO:0000250|UniProtKB:Q5TA31}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with JUN, independently of JUN
CC phosphorylation. Interacts (via C-terminus) with TRIM7.
CC {ECO:0000250|UniProtKB:Q5TA31}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5TA31}. Nucleus
CC {ECO:0000250|UniProtKB:Q5TA31}. Note=Shuttles between the cytoplasm and
CC the nucleus. {ECO:0000250|UniProtKB:Q5TA31}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked autoubiquitination in the
CC absence of growth factors and MAP3K1-induced 'Lys-63'-linked
CC polyubiquitination. 'Lys-48'-autoubiquitination leads to degradation by
CC the proteasome, while MAP3K1-induced 'Lys-63'-linked polyubiquitination
CC results in the stabilization of the protein. 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitinations occur most probably on the same 3 C-terminal
CC lysine residues (Lys-195, Lys-224 and Lys-225) and are thus mutually
CC exclusive. Other sites of ubiquitination are not excluded. 'Lys-63'-
CC linked polyubiquitination by TRIM7 in response to growth factor
CC signaling via the MEK/ERK pathway enhances protein stability.
CC {ECO:0000250|UniProtKB:Q5TA31}.
CC -!- PTM: Arginine methylation by PRMT1 stabilizes RNF187 by facilitating
CC K63-linked ubiquitin chain formation, and enables dimerization, c-Jun
CC interaction and subsequent AP1 target gene expression.
CC {ECO:0000250|UniProtKB:Q5TA31}.
CC -!- CAUTION: This sequence initiates at a CTG codon.
CC {ECO:0000305|PubMed:20852630}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDM04565.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EDM04566.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FM031715; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FM033519; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH473948; EDM04565.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH473948; EDM04566.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001157736.1; NM_001164264.1.
DR AlphaFoldDB; D3Z8N2; -.
DR SMR; D3Z8N2; -.
DR BioGRID; 262005; 1.
DR STRING; 10116.ENSRNOP00000065797; -.
DR iPTMnet; D3Z8N2; -.
DR PhosphoSitePlus; D3Z8N2; -.
DR PaxDb; D3Z8N2; -.
DR PRIDE; D3Z8N2; -.
DR GeneID; 360533; -.
DR KEGG; rno:360533; -.
DR UCSC; RGD:1308636; rat.
DR CTD; 149603; -.
DR RGD; 1308636; Rnf187.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; D3Z8N2; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF351093; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:D3Z8N2; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..236
FT /note="E3 ubiquitin-protein ligase RNF187"
FT /id="PRO_0000407929"
FT ZN_FING 12..53
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 98
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q5TA31"
FT MOD_RES 109
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q5TA31"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q5TA31"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q5TA31"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q5TA31"
SQ SEQUENCE 236 AA; 26313 MW; 5C6477677464D3D6 CRC64;
MALPAGPAEA ICALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP ECADDCWQRA
VEPSRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD GDPLCSACRM AAGPEPPEWE
PRWRKALRGK ENKGSVEIMR KDLNDARDLH GQAESAAAVW KGHVMDRRKK ALTDYKKLRA
FFVEEEEHFL QEAEKDEGAS DDDELADPAD RFRSLLQAVS ELEKKHRNLG LSMLLQ
