ID RNF4_MOUSE Reviewed; 194 AA. AC Q9QZS2; O35941; Q541Z6; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=E3 ubiquitin-protein ligase RNF4 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000250|UniProtKB:P78317}; DE AltName: Full=RING finger protein 4 {ECO:0000305}; GN Name=Rnf4 {ECO:0000303|PubMed:10822263, ECO:0000312|MGI:MGI:1201691}; 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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INTERACTION WITH GSC2. RC STRAIN=CD-1; TISSUE=Embryo; RX PubMed=10822263; RX DOI=10.1002/(sici)1097-0177(200005)218:1<102::aid-dvdy9>3.0.co;2-a; RA Galili N., Nayak S., Epstein J.A., Buck C.A.; RT "Rnf4, a RING protein expressed in the developing nervous and reproductive RT systems, interacts with Gscl, a gene within the DiGeorge critical region."; RL Dev. Dyn. 218:102-111(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Bone marrow, Embryo, Kidney, Lymph node, and Visual cortex; 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 MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 16-178, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=9479498; DOI=10.1006/geno.1997.5105; RA Chiariotti L., Benvenuto G., Fedele M., Santoro M., Simeone A., Fusco A., RA Bruni C.B.; RT "Identification and characterization of a novel RING-finger gene (RNF4) RT mapping at 4p16.3."; RL Genomics 47:258-265(1998). RN [5] RP SUBCELLULAR LOCATION, AND INTERACTION WITH TCF20. RX PubMed=10849425; DOI=10.1074/jbc.m003405200; RA Lyngsoe C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S., RA Noerby P.L., Bonven B.J., Joergensen P.; RT "Interaction between the transcription factor SPBP and the positive RT cofactor RNF4. An interplay between protein binding zinc fingers."; RL J. Biol. Chem. 275:26144-26149(2000). RN [6] RP INTERACTION WITH TRPS1. RX PubMed=12885770; DOI=10.1074/jbc.m306259200; RA Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.; RT "The RING finger protein RNF4, a co-regulator of transcription, interacts RT with the TRPS1 transcription factor."; RL J. Biol. Chem. 278:38780-38785(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [8] RP INTERACTION WITH PARP1. RX PubMed=19779455; DOI=10.1038/emboj.2009.279; RA Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., RA Bischof O., Seeler J.S., Dejean A.; RT "PARP-1 transcriptional activity is regulated by sumoylation upon heat RT shock."; RL EMBO J. 28:3534-3548(2009). RN [9] RP FUNCTION, PATHWAY, AUTOUBIQUITINATION, MUTAGENESIS OF VAL-134; SER-155; RP VAL-161 AND TYR-193, AND SUBUNIT. RX PubMed=20681948; DOI=10.1042/bj20100957; RA Liew C.W., Sun H., Hunter T., Day C.L.; RT "RING domain dimerization is essential for RNF4 function."; RL Biochem. J. 431:23-29(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-99, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, and Spleen; 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 which binds polysumoylated chains CC covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys- CC 48'- and 'Lys-63'-linked polyubiquitination of those substrates and CC their subsequent targeting to the proteasome for degradation CC (PubMed:20681948). Regulates the degradation of several proteins CC including PML and the transcriptional activator PEA3 (By similarity). CC Involved in chromosome alignment and spindle assembly, it regulates the CC kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI CC to proteasomal degradation (By similarity). Regulates the cellular CC responses to hypoxia and heat shock through degradation of respectively CC EPAS1 and PARP1 (By similarity). Alternatively, it may also bind CC DNA/nucleosomes and have a more direct role in the regulation of CC transcription for instance enhancing basal transcription and steroid CC receptor-mediated transcriptional activation (By similarity). Catalyzes CC ubiquitination of sumoylated PARP1 in response to PARP1 trapping to CC chromatin, leading to PARP1 removal from chromatin by VCP/p97 (By CC similarity). {ECO:0000250|UniProtKB:P78317, CC ECO:0000269|PubMed:20681948}. 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:0000250|UniProtKB:P78317}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:20681948}. CC -!- SUBUNIT: Homodimer (via RING-type zinc finger domain) CC (PubMed:20681948). Interacts with GSC2 (PubMed:10822263). Interacts CC with AR/the androgen receptor and TBP (By similarity). Interacts with CC TCF20 (PubMed:10849425). Interacts with PATZ1 (By similarity). CC Interacts with TRPS1; negatively regulates TRPS1 transcriptional CC repressor activity (PubMed:12885770). Interacts with PML (isoform PML- CC 1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and CC isoform PML-6). Interacts with PRDM1/Blimp-1 (By similarity). CC {ECO:0000250|UniProtKB:O88846, ECO:0000250|UniProtKB:P78317, CC ECO:0000269|PubMed:10822263, ECO:0000269|PubMed:10849425, CC ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:20681948}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10822263}. Nucleus CC {ECO:0000269|PubMed:10822263, ECO:0000269|PubMed:10849425}. Nucleus, CC PML body {ECO:0000250|UniProtKB:P78317}. CC -!- TISSUE SPECIFICITY: In the embryo, expressed primarily in the CC developing nervous system with strong expression in the dorsal root CC ganglia and gonads (PubMed:10822263, PubMed:9479498). Ubiquitously CC expressed in the adult (PubMed:10822263, PubMed:9479498). CC {ECO:0000269|PubMed:10822263, ECO:0000269|PubMed:9479498}. CC -!- DEVELOPMENTAL STAGE: Expression is detected from embryonic day 7 and CC continues throughout development and into adulthood. CC {ECO:0000269|PubMed:10822263}. CC -!- DOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to CC polysumoylated substrate. {ECO:0000250|UniProtKB:P78317}. CC -!- DOMAIN: The RING-type zinc finger domain is required for the CC ubiquitination of polysumoylated substrates. CC {ECO:0000250|UniProtKB:O88846}. CC -!- PTM: Sumoylated; conjugated by one or two SUMO1 moieties. CC {ECO:0000250|UniProtKB:O88846}. CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:20681948}. 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; AF169300; AAF00620.1; -; mRNA. DR EMBL; AK019171; BAB31585.1; -; mRNA. DR EMBL; AK090162; BAC41119.1; -; mRNA. DR EMBL; AK147057; BAE27641.1; -; mRNA. DR EMBL; AK151116; BAE30125.1; -; mRNA. DR EMBL; AK158987; BAE34757.1; -; mRNA. DR EMBL; AK159778; BAE35362.1; -; mRNA. DR EMBL; AK159949; BAE35505.1; -; mRNA. DR EMBL; BC003282; AAH03282.1; -; mRNA. DR EMBL; U95141; AAC53539.1; -; mRNA. DR CCDS; CCDS57336.1; -. DR RefSeq; NP_001291198.1; NM_001304269.1. DR RefSeq; NP_001291199.1; NM_001304270.1. DR RefSeq; NP_035408.1; NM_011278.5. DR PDB; 2MP2; NMR; -; C=45-69. DR PDBsum; 2MP2; -. DR AlphaFoldDB; Q9QZS2; -. DR BMRB; Q9QZS2; -. DR SMR; Q9QZS2; -. DR BioGRID; 202920; 5. DR IntAct; Q9QZS2; 1. DR MINT; Q9QZS2; -. DR STRING; 10090.ENSMUSP00000138555; -. DR iPTMnet; Q9QZS2; -. DR PhosphoSitePlus; Q9QZS2; -. DR EPD; Q9QZS2; -. DR jPOST; Q9QZS2; -. DR MaxQB; Q9QZS2; -. DR PaxDb; 10090-ENSMUSP00000138555; -. DR ProteomicsDB; 260989; -. DR Pumba; Q9QZS2; -. DR Antibodypedia; 22369; 163 antibodies from 24 providers. DR DNASU; 19822; -. DR Ensembl; ENSMUST00000030992.13; ENSMUSP00000030992.6; ENSMUSG00000029110.14. DR Ensembl; ENSMUST00000182047.2; ENSMUSP00000138411.2; ENSMUSG00000029110.14. DR Ensembl; ENSMUST00000182709.8; ENSMUSP00000138555.2; ENSMUSG00000029110.14. DR GeneID; 19822; -. DR KEGG; mmu:19822; -. DR UCSC; uc008xcc.2; mouse. DR AGR; MGI:1201691; -. DR MGI; MGI:1201691; Rnf4. DR VEuPathDB; HostDB:ENSMUSG00000029110; -. DR eggNOG; KOG0320; Eukaryota. DR GeneTree; ENSGT00390000010318; -. DR HOGENOM; CLU_106856_0_0_1; -. DR InParanoid; Q9QZS2; -. DR OMA; ICMDVYS; -. DR OrthoDB; 2919802at2759; -. DR PhylomeDB; Q9QZS2; -. DR TreeFam; TF328387; -. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 19822; 17 hits in 78 CRISPR screens. DR ChiTaRS; Rnf4; mouse. DR PRO; PR:Q9QZS2; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9QZS2; Protein. DR Bgee; ENSMUSG00000029110; Expressed in seminiferous tubule of testis and 267 other cell types or tissues. DR ExpressionAtlas; Q9QZS2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:1990752; C:microtubule end; ISO:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI. DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI. DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB. DR GO; GO:0032184; F:SUMO polymer binding; ISS:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI. DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI. DR GO; GO:0072711; P:cellular response to hydroxyurea; ISO:MGI. DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:MGI. DR GO; GO:0120186; P:negative regulation of protein localization to chromatin; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. 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:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI. DR GO; GO:0090234; P:regulation of kinetochore assembly; ISS:UniProtKB. DR GO; GO:0090169; P:regulation of spindle assembly; ISS:UniProtKB. DR GO; GO:0046685; P:response to arsenic-containing substance; ISO:MGI. DR CDD; cd16533; RING-HC_RNF4; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR043295; RING-HC_RNF4. DR InterPro; IPR047134; RNF4. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR23041:SF78; E3 UBIQUITIN-PROTEIN LIGASE RNF4; 1. DR PANTHER; PTHR23041; RING FINGER DOMAIN-CONTAINING; 1. DR Pfam; PF13639; zf-RING_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. DR Genevisible; Q9QZS2; MM. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..194 FT /note="E3 ubiquitin-protein ligase RNF4" FT /id="PRO_0000056044" FT ZN_FING 136..181 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1..20 FT /note="Required for ubiquitination activity" FT /evidence="ECO:0000269|PubMed:12885770" FT REGION 6..65 FT /note="Mediates interaction with TRPS1" FT /evidence="ECO:0000269|PubMed:12885770" FT REGION 110..130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 40..43 FT /note="SUMO interaction motif 1; mediates the binding to FT polysumoylated substrates" FT /evidence="ECO:0000250|UniProtKB:P78317" FT MOTIF 50..53 FT /note="SUMO interaction motif 2; mediates the binding to FT polysumoylated substrates" FT /evidence="ECO:0000250|UniProtKB:P78317" FT MOTIF 61..63 FT /note="SUMO interaction motif 3; mediates the binding to FT polysumoylated substrates" FT /evidence="ECO:0000250|UniProtKB:P78317" FT MOTIF 71..74 FT /note="SUMO interaction motif 4; mediates the binding to FT polysumoylated substrates" FT /evidence="ECO:0000250|UniProtKB:P78317" FT COMPBIAS 1..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 139 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 166 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O88846" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O88846" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MUTAGEN 134 FT /note="V->E: Abolishes homodimerization. Strongly reduced FT E3 ubiquitin ligase activity." FT /evidence="ECO:0000269|PubMed:20681948" FT MUTAGEN 155 FT /note="S->A: No effect." FT /evidence="ECO:0000269|PubMed:20681948" FT MUTAGEN 155 FT /note="S->E: Abolishes homodimerization. Strongly reduced FT E3 ubiquitin ligase activity." FT /evidence="ECO:0000269|PubMed:20681948" FT MUTAGEN 161 FT /note="V->A: Abolishes homodimerization. Strongly reduced FT E3 ubiquitin ligase activity." FT /evidence="ECO:0000269|PubMed:20681948" FT MUTAGEN 193 FT /note="Y->A: Abolishes homodimerization. Loss of E3 FT ubiquitin ligase activity." FT /evidence="ECO:0000269|PubMed:20681948" SQ SEQUENCE 194 AA; 21911 MW; 9A0A4277725C62E5 CRC64; MSTRNPQRKR RGGTVNSRQT QKRTRETTST PEVSLETEPI ELVETVGDEI VDLTCESLEP VVVDLTHNDS VVIVEERRRP RRNGRRLRQD HADSCVVSSD DEELSRDKDV YVTTHTPRST KDDGATGPRP SGTVSCPICM DGYSEIVQNG RLIVSTECGH VFCSQCLRDS LKNANTCPTC RKKINHKRYH PIYI //