RN187_MOUSE
ID RN187_MOUSE Reviewed; 236 AA.
AC Q8BFX1; Q4VA64; Q8C2B0; Q8CAS0; Q9JMF6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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).
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 (By similarity). Interacts with JUN, independently
CC of JUN phosphorylation (PubMed:20852630). Interacts (via C-terminus)
CC with TRIM7 (By similarity). {ECO:0000250|UniProtKB:Q5TA31,
CC ECO:0000269|PubMed:20852630}.
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-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=AAH96522.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH96522.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAA92754.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92754.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAC29916.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC29916.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAC40679.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40679.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AB030190; BAA92754.1; ALT_SEQ; mRNA.
DR EMBL; AK037991; BAC29916.1; ALT_SEQ; mRNA.
DR EMBL; AK075944; BAC36073.1; -; mRNA.
DR EMBL; AK076158; BAC36225.1; -; mRNA.
DR EMBL; AK088973; BAC40679.1; ALT_SEQ; mRNA.
DR EMBL; AL662809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072613; AAH72613.1; -; mRNA.
DR EMBL; BC096522; AAH96522.1; ALT_SEQ; mRNA.
DR CCDS; CCDS78953.1; -.
DR RefSeq; NP_071868.2; NM_022423.2.
DR AlphaFoldDB; Q8BFX1; -.
DR STRING; 10090.ENSMUSP00000091703; -.
DR iPTMnet; Q8BFX1; -.
DR PhosphoSitePlus; Q8BFX1; -.
DR EPD; Q8BFX1; -.
DR MaxQB; Q8BFX1; -.
DR PaxDb; Q8BFX1; -.
DR PeptideAtlas; Q8BFX1; -.
DR PRIDE; Q8BFX1; -.
DR ProteomicsDB; 300421; -.
DR DNASU; 108660; -.
DR GeneID; 108660; -.
DR KEGG; mmu:108660; -.
DR UCSC; uc007jcq.1; mouse.
DR CTD; 149603; -.
DR MGI; MGI:1914224; Rnf187.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q8BFX1; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF351093; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 108660; 1 hit in 52 CRISPR screens.
DR ChiTaRS; Rnf187; mouse.
DR PRO; PR:Q8BFX1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BFX1; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP: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_0000278242"
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:0000250|UniProtKB:D3Z8N2"
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; 48B73A52619F2768 CRC64;
MALPAGPADA ICALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP ECADDCWQRA
VEPSRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD GDPLCSACRM AAGPEPPEWE
PRWRKALRGK ENKGSVEIMR KDLNDARDLH GQAESAAAVW KGHVMDRRKK ALTDYKKLRA
FFVEEEEHFL QEAEKDEGAS EDDELADPAD RFRSLLQAVS ELEKKHRNLG LSMLLQ
