RN220_MOUSE
ID RN220_MOUSE Reviewed; 566 AA.
AC Q6PDX6; A2APP0; Q3T9M4; Q3V3D7; Q8JZY5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase Rnf220;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 220;
DE AltName: Full=RING-type E3 ubiquitin transferase Rnf220 {ECO:0000305};
GN Name=Rnf220;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SIN3B.
RX PubMed=20170641; DOI=10.1016/j.bbrc.2010.02.066;
RA Kong Q., Zeng W., Wu J., Hu W., Li C., Mao B.;
RT "RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination.";
RL Biochem. Biophys. Res. Commun. 393:708-713(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC and proteasomal degradation of SIN3B (PubMed:20170641). Independently
CC of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-
CC mediated deubiquitination of CTNNB1 and promotes Wnt signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q5VTB9,
CC ECO:0000269|PubMed:20170641}.
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: Interacts with SIN3B (PubMed:20170641). Interacts with CTNNB1
CC (via Armadillo repeats 2-8) (By similarity). Interacts with USP7 (via
CC MATH domain) (By similarity). {ECO:0000250|UniProtKB:Q5VTB9,
CC ECO:0000269|PubMed:20170641}.
CC -!- INTERACTION:
CC Q6PDX6; Q62141: Sin3b; NbExp=5; IntAct=EBI-2795840, EBI-591450;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20170641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PDX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDX6-2; Sequence=VSP_023069, VSP_023072, VSP_023073;
CC Name=3;
CC IsoId=Q6PDX6-3; Sequence=VSP_023070, VSP_023071;
CC Name=4;
CC IsoId=Q6PDX6-4; Sequence=VSP_023068;
CC -!- PTM: Auto-ubiquitinated; leads to proteasomal degradation.
CC {ECO:0000250}.
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DR EMBL; AK041785; BAE20604.1; -; mRNA.
DR EMBL; AK172415; BAE42996.1; -; mRNA.
DR EMBL; AL645740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034875; AAH34875.1; -; mRNA.
DR EMBL; BC056359; AAH56359.1; -; mRNA.
DR EMBL; BC058415; AAH58415.1; -; mRNA.
DR CCDS; CCDS18534.1; -. [Q6PDX6-1]
DR CCDS; CCDS80149.1; -. [Q6PDX6-4]
DR CCDS; CCDS89815.1; -. [Q6PDX6-2]
DR RefSeq; NP_001297658.1; NM_001310729.1.
DR RefSeq; NP_001297659.1; NM_001310730.1. [Q6PDX6-2]
DR RefSeq; NP_001297660.1; NM_001310731.1. [Q6PDX6-4]
DR RefSeq; NP_080015.3; NM_025739.3. [Q6PDX6-1]
DR RefSeq; XP_011238891.1; XM_011240589.2. [Q6PDX6-4]
DR RefSeq; XP_017175844.1; XM_017320355.1.
DR RefSeq; XP_017175846.1; XM_017320357.1. [Q6PDX6-4]
DR AlphaFoldDB; Q6PDX6; -.
DR BioGRID; 211685; 4.
DR IntAct; Q6PDX6; 6.
DR STRING; 10090.ENSMUSP00000030439; -.
DR iPTMnet; Q6PDX6; -.
DR PhosphoSitePlus; Q6PDX6; -.
DR EPD; Q6PDX6; -.
DR MaxQB; Q6PDX6; -.
DR PaxDb; Q6PDX6; -.
DR PeptideAtlas; Q6PDX6; -.
DR PRIDE; Q6PDX6; -.
DR ProteomicsDB; 300547; -. [Q6PDX6-1]
DR ProteomicsDB; 300548; -. [Q6PDX6-2]
DR ProteomicsDB; 300549; -. [Q6PDX6-3]
DR ProteomicsDB; 300550; -. [Q6PDX6-4]
DR Antibodypedia; 32475; 62 antibodies from 14 providers.
DR DNASU; 66743; -.
DR Ensembl; ENSMUST00000030439; ENSMUSP00000030439; ENSMUSG00000028677. [Q6PDX6-1]
DR Ensembl; ENSMUST00000102690; ENSMUSP00000099751; ENSMUSG00000028677. [Q6PDX6-4]
DR Ensembl; ENSMUST00000221654; ENSMUSP00000152367; ENSMUSG00000028677. [Q6PDX6-2]
DR GeneID; 66743; -.
DR KEGG; mmu:66743; -.
DR UCSC; uc008uim.1; mouse. [Q6PDX6-4]
DR UCSC; uc008uin.1; mouse. [Q6PDX6-2]
DR UCSC; uc008uip.1; mouse. [Q6PDX6-1]
DR UCSC; uc008uiq.1; mouse. [Q6PDX6-3]
DR CTD; 55182; -.
DR MGI; MGI:1913993; Rnf220.
DR VEuPathDB; HostDB:ENSMUSG00000028677; -.
DR eggNOG; ENOG502QR1N; Eukaryota.
DR GeneTree; ENSGT00390000016573; -.
DR HOGENOM; CLU_035321_0_0_1; -.
DR InParanoid; Q6PDX6; -.
DR OrthoDB; 1583675at2759; -.
DR PhylomeDB; Q6PDX6; -.
DR TreeFam; TF324716; -.
DR BRENDA; 2.3.2.27; 3474.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66743; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf220; mouse.
DR PRO; PR:Q6PDX6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PDX6; protein.
DR Bgee; ENSMUSG00000028677; Expressed in embryonic post-anal tail and 257 other tissues.
DR ExpressionAtlas; Q6PDX6; baseline and differential.
DR Genevisible; Q6PDX6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0003358; P:noradrenergic neuron development; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IGI:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IGI:MGI.
DR CDD; cd16563; RING-HC_RNF220; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031824; RNF220_mid.
DR InterPro; IPR040178; RNF220_RING.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF15926; RNF220; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Isopeptide bond;
KW Metal-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..566
FT /note="E3 ubiquitin-protein ligase Rnf220"
FT /id="PRO_0000277659"
FT ZN_FING 514..553
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 277..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..522
FT /note="Required for targeting to the cytoplasm"
FT COILED 485..513
FT /evidence="ECO:0000255"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VTB9"
FT VAR_SEQ 1..321
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023068"
FT VAR_SEQ 1..284
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023069"
FT VAR_SEQ 211..239
FT /note="KKAVALFDSQAPLCPICQVLLRPSELQEH -> YFGWNPLLTPSKPASQKCS
FT TGWQHRTCSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023070"
FT VAR_SEQ 240..566
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023071"
FT VAR_SEQ 285..302
FT /note="ASPHSSATEDLHHSDRYQ -> MPRARSGRRSRGADGREE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023072"
FT VAR_SEQ 331
FT /note="Q -> QVCPLCSRPLAGSEQEMSRHVEHCLAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023073"
FT CONFLICT 553
FT /note="N -> S (in Ref. 3; AAH34875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 62693 MW; AC8D8B716E9E6BAA CRC64;
MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV PVSVDKDVHI
PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA PPNLDCTPIS MLNHSGVGAF
RPFASTEDRE SYQSAFTPAK RLKNCHDTES PHLRFSDADG KEYDFGTQLP SSSPGSLKVD
DTGKKIFAVS GLISDRETSS SPEDRNDRCK KKAVALFDSQ APLCPICQVL LRPSELQEHM
EQELEQLAQL PASKNSLLKD AMAPGTPKSL LLSASIKREG DSPTASPHSS ATEDLHHSDR
YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAVDIEHADS NRFEEYEWCG
QKRIRATTLL EGGFRGSGFV MCSGKENPDS DADLDVDGDD TLEYGKPQYT EADVIPCTGE
EPGEAKEREA LRGAVLNGGP PSTRITPEFS KWASDEMPST SNGEGSKQEA MQKTCKNSDI
EKITEESAVT TFEALKARVR ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL
RTLGAKKLCP QCNTITAPGD LRRIYL
