RNF11_MOUSE
ID RNF11_MOUSE Reviewed; 154 AA.
AC Q9QYK7; B1AU36; B1AU37; Q9EQI1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RING finger protein 11;
DE AltName: Full=NEDD4 WW domain-binding protein 2;
DE AltName: Full=Sid 1669;
GN Name=Rnf11; Synonyms=N4wbp2, Sid1669;
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].
RX PubMed=10673045; DOI=10.1016/s0167-4781(99)00190-6;
RA Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y.,
RA Sugano S., Muramatsu M., Saito T.;
RT "Cloning and expression profile of mouse and human genes, Rnf11/RNF11,
RT encoding a novel RING-H2 finger protein.";
RL Biochim. Biophys. Acta 1489:421-427(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, INTERACTION WITH NEDD4, AND MUTAGENESIS
RP OF TYR-40.
RX PubMed=11042109; DOI=10.1042/bj3510557;
RA Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.;
RT "Identification of multiple proteins expressed in murine embryos as binding
RT partners for the WW domains of the ubiquitin-protein ligase Nedd4.";
RL Biochem. J. 351:557-565(2000).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1.
RX PubMed=19131965; DOI=10.1038/emboj.2008.285;
RA Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
RT "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB
RT signalling.";
RL EMBO J. 28:513-522(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential component of a ubiquitin-editing protein complex,
CC comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient
CC nature of inflammatory signaling pathways. Promotes the association of
CC TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-
CC 63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-
CC 48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation
CC and consequently termination of the TNF- or LPS-mediated activation of
CC NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for
CC ubiquitination, leading to its degradation by the 26S proteasome.
CC -!- SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts with
CC the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By similarity).
CC Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and
CC UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350,
CC EPS15 and STAMBP (By similarity). After TNF stimulation, interacts with
CC TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they
CC are lost after 1 hour of stimulation with TNF. Interacts with GGA1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9QYK7; P46935: Nedd4; NbExp=4; IntAct=EBI-4405826, EBI-773516;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear,
CC when phosphorylated by PKB/AKT1. {ECO:0000250}.
CC -!- DOMAIN: The PPxY motif mediates interaction with NEDD4.
CC {ECO:0000269|PubMed:11042109}.
CC -!- PTM: Ubiquitinated in the presence of ITCH, SMURF2 and UBE2D1, as well
CC as WWP1. {ECO:0000250}.
CC -!- PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the
CC proteasome. {ECO:0000250}.
CC -!- PTM: Acylation at both Gly-2 and Cys-4 is required for proper
CC localization to the endosomes. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44245.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB024427; BAA84682.1; -; mRNA.
DR EMBL; AF220206; AAG44245.1; ALT_INIT; mRNA.
DR EMBL; AL669905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL30703.1; -; Genomic_DNA.
DR EMBL; CH466527; EDL30704.1; -; Genomic_DNA.
DR EMBL; CH466527; EDL30705.1; -; Genomic_DNA.
DR EMBL; BC010299; AAH10299.1; -; mRNA.
DR EMBL; BC028255; AAH28255.1; -; mRNA.
DR CCDS; CCDS18464.1; -.
DR RefSeq; NP_038904.1; NM_013876.3.
DR AlphaFoldDB; Q9QYK7; -.
DR SMR; Q9QYK7; -.
DR BioGRID; 205930; 9.
DR IntAct; Q9QYK7; 8.
DR MINT; Q9QYK7; -.
DR STRING; 10090.ENSMUSP00000030284; -.
DR iPTMnet; Q9QYK7; -.
DR PhosphoSitePlus; Q9QYK7; -.
DR SwissPalm; Q9QYK7; -.
DR jPOST; Q9QYK7; -.
DR MaxQB; Q9QYK7; -.
DR PaxDb; Q9QYK7; -.
DR PeptideAtlas; Q9QYK7; -.
DR PRIDE; Q9QYK7; -.
DR ProteomicsDB; 300456; -.
DR Antibodypedia; 32937; 179 antibodies from 24 providers.
DR DNASU; 29864; -.
DR Ensembl; ENSMUST00000030284; ENSMUSP00000030284; ENSMUSG00000028557.
DR Ensembl; ENSMUST00000064167; ENSMUSP00000063798; ENSMUSG00000028557.
DR GeneID; 29864; -.
DR KEGG; mmu:29864; -.
DR UCSC; uc008ucm.1; mouse.
DR CTD; 26994; -.
DR MGI; MGI:1352759; Rnf11.
DR VEuPathDB; HostDB:ENSMUSG00000028557; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00730000110988; -.
DR HOGENOM; CLU_123539_1_0_1; -.
DR InParanoid; Q9QYK7; -.
DR OMA; HLDCIDN; -.
DR OrthoDB; 1261762at2759; -.
DR PhylomeDB; Q9QYK7; -.
DR TreeFam; TF318022; -.
DR BioGRID-ORCS; 29864; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf11; mouse.
DR PRO; PR:Q9QYK7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QYK7; protein.
DR Bgee; ENSMUSG00000028557; Expressed in blood and 265 other tissues.
DR ExpressionAtlas; Q9QYK7; baseline and differential.
DR Genevisible; Q9QYK7; MM.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IPI:MGI.
DR CDD; cd16468; RING-H2_RNF11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042981; RNF11_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Lipoprotein; Metal-binding; Myristate; Nucleus;
KW Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C5"
FT CHAIN 2..154
FT /note="RING finger protein 11"
FT /id="PRO_0000056051"
FT ZN_FING 99..140
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..40
FT /note="PPxY motif"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3C5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 40
FT /note="Y->A: Abolishes interaction with NEDD4."
FT /evidence="ECO:0000269|PubMed:11042109"
SQ SEQUENCE 154 AA; 17458 MW; EF192AB0C2D4BF87 CRC64;
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPIYH PTPSQTRLAT
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN
