RN220_HUMAN
ID RN220_HUMAN Reviewed; 566 AA.
AC Q5VTB9; B3KPJ3; B4DLZ9; E9PCS1; Q4KMX2; Q9NVP6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
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; Synonyms=C1orf164;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP INTERACTION WITH CTNNB1 AND USP7, AND FUNCTION.
RX PubMed=25266658; DOI=10.1128/mcb.00731-14;
RA Ma P., Yang X., Kong Q., Li C., Yang S., Li Y., Mao B.;
RT "The ubiquitin ligase RNF220 enhances canonical Wnt signaling through USP7-
RT mediated deubiquitination of beta-catenin.";
RL Mol. Cell. Biol. 34:4355-4366(2014).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-277, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC and proteasomal degradation of SIN3B (By similarity). Independently of
CC its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-
CC mediated deubiquitination of CTNNB1 promoting Wnt signaling
CC (PubMed:25266658). {ECO:0000250|UniProtKB:Q6PDX6,
CC ECO:0000269|PubMed:25266658}.
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 (By similarity). Interacts with CTNNB1
CC (via Armadillo repeats 2-8) (PubMed:25266658). Interacts with USP7 (via
CC MATH domain) (PubMed:25266658). {ECO:0000250|UniProtKB:Q6PDX6,
CC ECO:0000269|PubMed:25266658}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6PDX6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VTB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VTB9-3; Sequence=VSP_055437, VSP_055438;
CC -!- PTM: Auto-ubiquitinated; leads to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AK001459; BAA91704.1; ALT_INIT; mRNA.
DR EMBL; AK056424; BAG51705.1; -; mRNA.
DR EMBL; AK297228; BAG59711.1; -; mRNA.
DR EMBL; AL122004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034221; AAH34221.1; -; mRNA.
DR EMBL; BC098266; AAH98266.1; -; mRNA.
DR EMBL; BC098300; AAH98300.1; -; mRNA.
DR CCDS; CCDS510.1; -. [Q5VTB9-1]
DR RefSeq; NP_001306885.1; NM_001319956.1. [Q5VTB9-1]
DR RefSeq; NP_001306886.1; NM_001319957.1. [Q5VTB9-3]
DR RefSeq; NP_060620.2; NM_018150.3. [Q5VTB9-1]
DR RefSeq; XP_016857112.1; XM_017001623.1.
DR RefSeq; XP_016857113.1; XM_017001624.1. [Q5VTB9-1]
DR RefSeq; XP_016857114.1; XM_017001625.1. [Q5VTB9-1]
DR AlphaFoldDB; Q5VTB9; -.
DR BioGRID; 120481; 32.
DR IntAct; Q5VTB9; 12.
DR MINT; Q5VTB9; -.
DR STRING; 9606.ENSP00000347548; -.
DR GlyGen; Q5VTB9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VTB9; -.
DR PhosphoSitePlus; Q5VTB9; -.
DR BioMuta; RNF220; -.
DR DMDM; 74756788; -.
DR EPD; Q5VTB9; -.
DR jPOST; Q5VTB9; -.
DR MassIVE; Q5VTB9; -.
DR MaxQB; Q5VTB9; -.
DR PaxDb; Q5VTB9; -.
DR PeptideAtlas; Q5VTB9; -.
DR PRIDE; Q5VTB9; -.
DR ProteomicsDB; 4573; -.
DR ProteomicsDB; 65319; -. [Q5VTB9-1]
DR Antibodypedia; 32475; 62 antibodies from 14 providers.
DR DNASU; 55182; -.
DR Ensembl; ENST00000355387.6; ENSP00000347548.2; ENSG00000187147.18. [Q5VTB9-1]
DR Ensembl; ENST00000361799.7; ENSP00000354872.2; ENSG00000187147.18. [Q5VTB9-1]
DR Ensembl; ENST00000372247.6; ENSP00000361321.2; ENSG00000187147.18. [Q5VTB9-1]
DR GeneID; 55182; -.
DR KEGG; hsa:55182; -.
DR MANE-Select; ENST00000361799.7; ENSP00000354872.2; NM_018150.4; NP_060620.2.
DR UCSC; uc001clv.2; human. [Q5VTB9-1]
DR CTD; 55182; -.
DR DisGeNET; 55182; -.
DR GeneCards; RNF220; -.
DR HGNC; HGNC:25552; RNF220.
DR HPA; ENSG00000187147; Tissue enriched (brain).
DR MIM; 616136; gene.
DR neXtProt; NX_Q5VTB9; -.
DR OpenTargets; ENSG00000187147; -.
DR PharmGKB; PA162401886; -.
DR VEuPathDB; HostDB:ENSG00000187147; -.
DR eggNOG; ENOG502QR1N; Eukaryota.
DR GeneTree; ENSGT00390000016573; -.
DR HOGENOM; CLU_035321_0_0_1; -.
DR InParanoid; Q5VTB9; -.
DR OMA; XGAKKLC; -.
DR OrthoDB; 1583675at2759; -.
DR PhylomeDB; Q5VTB9; -.
DR TreeFam; TF324716; -.
DR PathwayCommons; Q5VTB9; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q5VTB9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55182; 17 hits in 1119 CRISPR screens.
DR ChiTaRS; RNF220; human.
DR GeneWiki; RNF220; -.
DR GenomeRNAi; 55182; -.
DR Pharos; Q5VTB9; Tbio.
DR PRO; PR:Q5VTB9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VTB9; protein.
DR Bgee; ENSG00000187147; Expressed in C1 segment of cervical spinal cord and 204 other tissues.
DR ExpressionAtlas; Q5VTB9; baseline and differential.
DR Genevisible; Q5VTB9; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:GO_Central.
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:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl.
DR GO; GO:0003358; P:noradrenergic neuron development; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IGI:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS: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_0000277657"
FT ZN_FING 514..553
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..522
FT /note="Required for targeting to the cytoplasm"
FT /evidence="ECO:0000250"
FT COILED 485..513
FT /evidence="ECO:0000255"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055437"
FT VAR_SEQ 331
FT /note="Q -> QVCPLCNRPLAGSEQEMSRHVEHCLSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055438"
FT CONFLICT 84
FT /note="A -> V (in Ref. 3; AAH98300)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> E (in Ref. 1; BAG51705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 62765 MW; AAE3C723032B062B CRC64;
MDLHRAAFKM ENSSYLPNPL ASPALMVLAS TAEASRDASI PCQQPRPFGV PVSVDKDVHI
PFTNGSYTFA SMYHRQGGVP GTFANRDFPP SLLHLHPQFA PPNLDCTPIS MLNHSGVGAF
RPFASTEDRE SYQSAFTPAK RLKNCHDTES PHLRFSDADG KEYDFGTQLP SSSPGSLKVD
DTGKKIFAVS GLISDREASS SPEDRNDRCK KKAAALFDSQ APICPICQVL LRPSELQEHM
EQELEQLAQL PSSKNSLLKD AMAPGTPKSL LLSASIKREG ESPTASPHSS ATDDLHHSDR
YQTFLRVRAN RQTRLNARIG KMKRRKQDEG QREGSCMAED DAVDIEHENN NRFEEYEWCG
QKRIRATTLL EGGFRGSGFI MCSGKENPDS DADLDVDGDD TLEYGKPQYT EADVIPCTGE
EPGEAKEREA LRGAVLNGGP PSTRITPEFS KWASDEMPST SNGESSKQEA MQKTCKNSDI
EKITEDSAVT TFEALKARVR ELERQLSRGD RYKCLICMDS YSMPLTSIQC WHVHCEECWL
RTLGAKKLCP QCNTITAPGD LRRIYL
