ID A0A087WRE9_MOUSE Unreviewed; 264 AA. AC A0A087WRE9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 24-JUL-2024, entry version 54. DE RecName: Full=E3 ubiquitin-protein ligase RING2 {ECO:0000256|ARBA:ARBA00019736}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; DE AltName: Full=RING finger protein 1B {ECO:0000256|ARBA:ARBA00030504}; DE AltName: Full=RING finger protein 2 {ECO:0000256|ARBA:ARBA00032293}; DE AltName: Full=RING-type E3 ubiquitin transferase RING2 {ECO:0000256|ARBA:ARBA00030910}; GN Name=Rnf2 {ECO:0000313|Ensembl:ENSMUSP00000140594.2, GN ECO:0000313|MGI:MGI:1101759}; 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 {ECO:0000313|Ensembl:ENSMUSP00000140594.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Proteomes:UP000000589}; 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 [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000140594.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140594.2}; RG Ensembl; RL Submitted (APR-2024) to UniProtKB. 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; Evidence={ECO:0000256|ARBA:ARBA00000900}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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 AlphaFoldDB; A0A087WRE9; -. DR SMR; A0A087WRE9; -. DR jPOST; A0A087WRE9; -. DR ProteomicsDB; 310125; -. DR Antibodypedia; 20609; 455 antibodies from 44 providers. DR Ensembl; ENSMUST00000186415.7; ENSMUSP00000140594.2; ENSMUSG00000026484.14. DR AGR; MGI:1101759; -. DR MGI; MGI:1101759; Rnf2. DR VEuPathDB; HostDB:ENSMUSG00000026484; -. DR GeneTree; ENSGT00940000154499; -. DR UniPathway; UPA00143; -. DR ChiTaRS; Rnf2; mouse. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000026484; Expressed in undifferentiated genital tubercle and 268 other cell types or tissues. DR ExpressionAtlas; A0A087WRE9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031519; C:PcG protein complex; IEA:UniProt. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR CDD; cd17167; RAWUL_RING2; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR032443; RAWUL. DR InterPro; IPR043540; RING1/RING2. DR InterPro; IPR037937; RING2_RAWUL_dom. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1. DR PANTHER; PTHR46076:SF4; E3 UBIQUITIN-PROTEIN LIGASE RING2; 1. DR Pfam; PF16207; RAWUL; 1. DR Pfam; PF13923; zf-C3HC4_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A087WRE9, KW ECO:0007829|ProteomicsDB:A0A087WRE9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 51..76 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 86..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 86..122 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 264 AA; 29226 MW; 2772168F333B16C8 CRC64; MSQAVQTNGT QPLSKTWELS LYELQRTPQE AITDGLEIVV SPRSLHSELM CPICLDMLKN TMTTKECLHR FCADCIITAL RSGLQRGKKQ QIENGSGAED NGDSSHCSNA STHSNQEAGP SNKRTKTSDD SGLELDNNNA AVAIDPVMDG ASEIELVFRP HPTLMEKDDS AQTRYIKTSG NATVDHLSKY LAVRLALEEL RSKGESNQMN LDTASEKQYT IYIATASGQF TVLNGSFSLE LVSEKYWKVN KPMELYYAPT KEHK //