UBE3A_MOUSE
ID UBE3A_MOUSE Reviewed; 870 AA.
AC O08759; E9QKT1; P97482; Q8CE29;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ubiquitin-protein ligase E3A;
DE EC=2.3.2.26 {ECO:0000269|PubMed:20211139};
DE AltName: Full=HECT-type ubiquitin transferase E3A;
DE AltName: Full=Oncogenic protein-associated protein E6-AP;
GN Name=Ube3a;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9182527; DOI=10.1074/jbc.272.24.15085;
RA Hatakeyama S., Jensen J.P., Weissman A.M.;
RT "Subcellular localization and ubiquitin-conjugating enzyme (E2)
RT interactions of mammalian HECT family ubiquitin protein ligases.";
RL J. Biol. Chem. 272:15085-15092(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9110176; DOI=10.1101/gr.7.4.368;
RA Sutcliffe J.S., Jiang Y.-H., Galjaard R.-J., Matsuura T., Fang P.,
RA Kubota T., Christian S.L., Bressler J., Cattanach B., Ledbetter D.H.,
RA Beaudet A.L.;
RT "The E6-Ap ubiquitin-protein ligase (UBE3A) gene is localized within a
RT narrowed Angelman syndrome critical region.";
RL Genome Res. 7:368-377(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 DISRUPTION PHENOTYPE.
RX PubMed=9808466; DOI=10.1016/s0896-6273(00)80596-6;
RA Jiang Y.H., Armstrong D., Albrecht U., Atkins C.M., Noebels J.L.,
RA Eichele G., Sweatt J.D., Beaudet A.L.;
RT "Mutation of the Angelman ubiquitin ligase in mice causes increased
RT cytoplasmic p53 and deficits of contextual learning and long-term
RT potentiation.";
RL Neuron 21:799-811(1998).
RN [7]
RP IMPRINTING, AND DISRUPTION PHENOTYPE.
RX PubMed=11895368; DOI=10.1006/nbdi.2001.0463;
RA Miura K., Kishino T., Li E., Webber H., Dikkes P., Holmes G.L.,
RA Wagstaff J.;
RT "Neurobehavioral and electroencephalographic abnormalities in Ube3a
RT maternal-deficient mice.";
RL Neurobiol. Dis. 9:149-159(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP 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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ARC, INDUCTION, DISRUPTION
RP PHENOTYPE, ACTIVE SITE, AND MUTAGENESIS OF CYS-838.
RX PubMed=20211139; DOI=10.1016/j.cell.2010.01.026;
RA Greer P.L., Hanayama R., Bloodgood B.L., Mardinly A.R., Lipton D.M.,
RA Flavell S.W., Kim T.K., Griffith E.C., Waldon Z., Maehr R., Ploegh H.L.,
RA Chowdhury S., Worley P.F., Steen J., Greenberg M.E.;
RT "The Angelman syndrome protein Ube3A regulates synapse development by
RT ubiquitinating Arc.";
RL Cell 140:704-716(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ARNTL.
RX PubMed=24728990; DOI=10.1093/nar/gku225;
RA Gossan N.C., Zhang F., Guo B., Jin D., Yoshitane H., Yao A., Glossop N.,
RA Zhang Y.Q., Fukada Y., Meng Q.J.;
RT "The E3 ubiquitin ligase UBE3A is an integral component of the molecular
RT circadian clock through regulating the BMAL1 transcription factor.";
RL Nucleic Acids Res. 42:5765-5775(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC transfers it to its substrates. Several substrates have been identified
CC including the ARNTL/BMAL1, ARC, RAD23A and RAD23B, MCM7 (which is
CC involved in DNA replication), annexin A1, the PML tumor suppressor, and
CC the cell cycle regulator CDKN1B (PubMed:20211139, PubMed:24728990).
CC Additionally, may function as a cellular quality control ubiquitin
CC ligase by helping the degradation of the cytoplasmic misfolded
CC proteins. Finally, UBE3A also promotes its own degradation in vivo (By
CC similarity). Plays an important role in the regulation of the circadian
CC clock: involved in the ubiquitination of the core clock component
CC ARNTL/BMAL1, leading to its proteasomal degradation (PubMed:24728990).
CC Acts as a regulator of synaptic development by mediating ubiquitination
CC and degradation of ARC (PubMed:20211139). Synergizes with WBP2 in
CC enhancing PGR activity (By similarity). {ECO:0000250|UniProtKB:Q05086,
CC ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:24728990}.
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=2.3.2.26; Evidence={ECO:0000269|PubMed:20211139};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:20211139}.
CC -!- SUBUNIT: The active form is probably a homotrimer. Binds UBQLN1 and
CC UBQLN2. Interacts with the 26S proteasome. Interacts with BPY2.
CC Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be
CC mediated by NEURL4. Interacts with the proteasomal subunit PSMD4.
CC Interacts with ARNTL/BMAL1 (PubMed:24728990). Interacts with ARC
CC (PubMed:20211139). Interacts with ESR1 and WBP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q05086, ECO:0000269|PubMed:20211139,
CC ECO:0000269|PubMed:24728990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9182527}. Nucleus
CC {ECO:0000269|PubMed:9182527}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O08759-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08759-2; Sequence=VSP_057563;
CC Name=3;
CC IsoId=O08759-3; Sequence=VSP_057563, VSP_057564;
CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in brain, heart and
CC thymus. {ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:9110176}.
CC -!- INDUCTION: Up-regulated in response to neuronal activity.
CC {ECO:0000269|PubMed:20211139}.
CC -!- PTM: Phosphorylation at Tyr-654 by ABL1 impairs E3 ligase activity.
CC {ECO:0000250|UniProtKB:Q05086}.
CC -!- DISRUPTION PHENOTYPE: Mice with maternal deficiency display autism
CC spectrum disorders, characterized by motor dysfunction, inducible
CC seizures and a context-dependent learning deficit (PubMed:9808466,
CC PubMed:11895368). Long-term potentiation (LTP) is severely impaired
CC despite normal baseline synaptic transmission and neuroanatomy
CC (PubMed:9808466). The cytoplasmic abundance of p53/TP53 is increased in
CC postmitotic neurons (PubMed:9808466). Accumulation of ARC protein in
CC neurons, resulting in the excessive internalization of AMPA receptors
CC (AMPARs) at synapses and impaired synaptic function (PubMed:20211139).
CC {ECO:0000269|PubMed:11895368, ECO:0000269|PubMed:20211139,
CC ECO:0000269|PubMed:9808466}.
CC -!- MISCELLANEOUS: The Ube3a locus is imprinted with silencing of the
CC paternal allele in hippocampus and cerebellum in mice.
CC {ECO:0000269|PubMed:11895368}.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U96636; AAB63361.1; -; mRNA.
DR EMBL; U82122; AAB47756.1; ALT_FRAME; mRNA.
DR EMBL; AK029133; BAC26314.1; -; mRNA.
DR EMBL; AC167971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131658; AAI31659.1; -; mRNA.
DR EMBL; BC131659; AAI31660.1; -; mRNA.
DR CCDS; CCDS39973.1; -. [O08759-1]
DR CCDS; CCDS80733.1; -. [O08759-2]
DR RefSeq; NP_035798.2; NM_011668.2. [O08759-1]
DR RefSeq; NP_766598.1; NM_173010.3. [O08759-3]
DR RefSeq; XP_006540862.1; XM_006540799.3. [O08759-1]
DR RefSeq; XP_011249149.1; XM_011250847.2. [O08759-2]
DR RefSeq; XP_017177614.1; XM_017322125.1. [O08759-1]
DR AlphaFoldDB; O08759; -.
DR SMR; O08759; -.
DR IntAct; O08759; 2.
DR MINT; O08759; -.
DR STRING; 10090.ENSMUSP00000103161; -.
DR iPTMnet; O08759; -.
DR PhosphoSitePlus; O08759; -.
DR SwissPalm; O08759; -.
DR EPD; O08759; -.
DR jPOST; O08759; -.
DR MaxQB; O08759; -.
DR PaxDb; O08759; -.
DR PeptideAtlas; O08759; -.
DR PRIDE; O08759; -.
DR ProteomicsDB; 298183; -. [O08759-1]
DR ProteomicsDB; 298184; -. [O08759-2]
DR ProteomicsDB; 298185; -. [O08759-3]
DR Antibodypedia; 9118; 435 antibodies from 37 providers.
DR DNASU; 22215; -.
DR Ensembl; ENSMUST00000107537; ENSMUSP00000103161; ENSMUSG00000025326. [O08759-2]
DR Ensembl; ENSMUST00000200758; ENSMUSP00000143859; ENSMUSG00000025326. [O08759-1]
DR Ensembl; ENSMUST00000202945; ENSMUSP00000143962; ENSMUSG00000025326. [O08759-3]
DR GeneID; 22215; -.
DR KEGG; mmu:22215; -.
DR UCSC; uc009heg.1; mouse.
DR UCSC; uc009hei.1; mouse.
DR CTD; 7337; -.
DR MGI; MGI:105098; Ube3a.
DR VEuPathDB; HostDB:ENSMUSG00000025326; -.
DR eggNOG; KOG0941; Eukaryota.
DR GeneTree; ENSGT00940000155050; -.
DR HOGENOM; CLU_002173_5_0_1; -.
DR InParanoid; O08759; -.
DR OMA; GNAHCTN; -.
DR OrthoDB; 339404at2759; -.
DR PhylomeDB; O08759; -.
DR TreeFam; TF315189; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22215; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ube3a; mouse.
DR PRO; PR:O08759; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O08759; protein.
DR Bgee; ENSMUSG00000025326; Expressed in rostral migratory stream and 252 other tissues.
DR ExpressionAtlas; O08759; baseline and differential.
DR Genevisible; O08759; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IPI:MGI.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:MGI.
DR GO; GO:0061743; P:motor learning; ISO:MGI.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:1905528; P:positive regulation of Golgi lumen acidification; IMP:CACAO.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060736; P:prostate gland growth; IMP:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0035037; P:sperm entry; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 6.10.130.10; -; 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR017134; UBE3A.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Metal-binding;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..870
FT /note="Ubiquitin-protein ligase E3A"
FT /id="PRO_0000194981"
FT DOMAIN 542..870
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ZN_FING 42..81
FT /note="C4-type; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q05086"
FT REGION 171..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 838
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104,
FT ECO:0000269|PubMed:20211139"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 654
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q05086"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_057563"
FT VAR_SEQ 784..870
FT /note="Missing (in isoform 3)"
FT /id="VSP_057564"
FT MUTAGEN 838
FT /note="C->A: Abolishes catalytic activity. Abolishes
FT ability to ubiquitinate ARC."
FT /evidence="ECO:0000269|PubMed:20211139"
FT CONFLICT 7
FT /note="R -> S (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> D (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> L (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="S -> T (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="K -> N (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="F -> S (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="F -> G (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="R -> T (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="D -> N (in Ref. 2; AAB47756)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="Missing (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 710..711
FT /note="NL -> IS (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="Q -> L (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
FT CONFLICT 854..855
FT /note="KE -> NV (in Ref. 1; AAB63361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 99819 MW; CC6BBDDD5AE9C164 CRC64;
MATACKRSPG ESQSEDIEAS RMKRAAAKHL IERYYHQLTE GCGNEACTNE FCASCPTFLR
MDNNAAAIKA LELYKINAKL CDPHPSKKGA SSAYLENSKG ASNNSEIKMN KKEGKDFKDV
IYLTEEKVYE IYEFCRESED YSPLIRVIGR IFSSAEALVL SFRKVKQHTK EELKSLQEKD
EDKDEDEKEK AACSAAAMEE DSEASSSRMG DSSQGDNNVQ KLGPDDVTVD IDAIRRVYSS
LLANEKLETA FLNALVYLSP NVECDLTYHN VYTRDPNYLN LFIIVMENSN LHSPEYLEMA
LPLFCKAMCK LPLEAQGKLI RLWSKYSADQ IRRMMETFQQ LITYKVISNE FNSRNLVNDD
DAIVAASKCL KMVYYANVVG GDVDTNHNEE DDEEPIPESS ELTLQELLGD ERRNKKGPRV
DPLETELGVK TLDCRKPLIS FEEFINEPLN DVLEMDKDYT FFKVETENKF SFMTCPFILN
AVTKNLGLYY DNRIRMYSER RITVLYSLVQ GQQLNPYLRL KVRRDHIIDD ALVRLEMIAM
ENPADLKKQL YVEFEGEQGV DEGGVSKEFF QLVVEEIFNP DIGMFTYDEA TKLFWFNPSS
FETEGQFTLI GIVLGLAIYN NCILDVHFPM VVYRKLMGKK GTFRDLGDSH PVLYQSLKDL
LEYEGSVEDD MMITFQISQT DLFGNPMMYD LKENGDKIPI TNENRKEFVN LYSDYILNKS
VEKQFKAFRR GFHMVTNESP LKYLFRPEEI ELLICGSRNL DFQALEETTE YDGGYTRESV
VIREFWEIVH SFTDEQKRLF LQFTTGTDRA PVGGLGKLKM IIAKNGPDTE RLPTSHTCFN
VLLLPEYSSK EKLKERLLKA ITYAKGFGML
