UB2E3_MOUSE
ID UB2E3_MOUSE Reviewed; 207 AA.
AC P52483; O09180; Q3TI00; Q91X63;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 E3;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme E3;
DE AltName: Full=UbcM2;
DE AltName: Full=Ubiquitin carrier protein E3;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-23 kDa;
DE AltName: Full=Ubiquitin-protein ligase E3;
GN Name=Ube2e3; Synonyms=Ubce4, Ubcm2;
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].
RC STRAIN=BALB/cJ;
RX PubMed=8576256; DOI=10.1074/jbc.271.5.2789;
RA Matuschewski K., Hauser H.P., Treier M., Jentsch S.;
RT "Identification of a novel family of ubiquitin-conjugating enzymes with
RT distinct amino-terminal extensions.";
RL J. Biol. Chem. 271:2789-2794(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF CYS-145.
RC STRAIN=SWR/J;
RX PubMed=9872334; DOI=10.1038/sj.onc.1202260;
RA Pestov D.G., Grzeszkiewicz T.M., Lau L.F.;
RT "Isolation of growth suppressors from a cDNA expression library.";
RL Oncogene 17:3187-3197(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
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 MRNA].
RC TISSUE=Liver;
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 [5]
RP INTERACTION WITH IPO11, AND SUBCELLULAR LOCATION.
RX PubMed=11032817; DOI=10.1093/emboj/19.20.5502;
RA Plafker S.M., Macara I.G.;
RT "Importin-11, a nuclear import receptor for the ubiquitin-conjugating
RT enzyme, UbcM2.";
RL EMBO J. 19:5502-5513(2000).
RN [6]
RP INTERACTION WITH IPO11, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-145.
RX PubMed=15545318; DOI=10.1083/jcb.200406001;
RA Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.;
RT "Ubiquitin charging of human class III ubiquitin-conjugating enzymes
RT triggers their nuclear import.";
RL J. Cell Biol. 167:649-659(2004).
RN [7]
RP INTERACTION WITH NEDD4L, MUTAGENESIS OF CYS-145, AND FUNCTION.
RX PubMed=14993279; DOI=10.1128/mcb.24.6.2397-2409.2004;
RA Debonneville C., Staub O.;
RT "Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-
RT dependent regulation of the epithelial Na+ channel.";
RL Mol. Cell. Biol. 24:2397-2409(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and
CC 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination (By
CC similarity). Participates in the regulation of transepithelial sodium
CC transport in renal cells. May be involved in cell growth arrest.
CC {ECO:0000250|UniProtKB:Q969T4, ECO:0000269|PubMed:14993279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000250|UniProtKB:Q969T4, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with NEDD4L. The ubiquitin-loaded form interacts
CC specifically with importin-11 (IPO11), leading to its import into the
CC nucleus. {ECO:0000269|PubMed:11032817, ECO:0000269|PubMed:14993279,
CC ECO:0000269|PubMed:15545318}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC nucleus and cytoplasm in a IPO11-dependent manner.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X92664; CAA63352.1; -; mRNA.
DR EMBL; AF003346; AAB60948.1; -; mRNA.
DR EMBL; AK076011; BAC36118.1; -; mRNA.
DR EMBL; AK168072; BAE40046.1; -; mRNA.
DR EMBL; BC011477; AAH11477.1; -; mRNA.
DR CCDS; CCDS16167.1; -.
DR RefSeq; NP_033480.1; NM_009454.2.
DR RefSeq; XP_006499224.1; XM_006499161.3.
DR RefSeq; XP_006499225.1; XM_006499162.3.
DR RefSeq; XP_006499226.1; XM_006499163.3.
DR AlphaFoldDB; P52483; -.
DR SMR; P52483; -.
DR BioGRID; 204405; 15.
DR IntAct; P52483; 1.
DR STRING; 10090.ENSMUSP00000028398; -.
DR iPTMnet; P52483; -.
DR PhosphoSitePlus; P52483; -.
DR SwissPalm; P52483; -.
DR jPOST; P52483; -.
DR MaxQB; P52483; -.
DR PaxDb; P52483; -.
DR PeptideAtlas; P52483; -.
DR PRIDE; P52483; -.
DR ProteomicsDB; 298172; -.
DR Antibodypedia; 1150; 660 antibodies from 32 providers.
DR DNASU; 22193; -.
DR Ensembl; ENSMUST00000028398; ENSMUSP00000028398; ENSMUSG00000027011.
DR Ensembl; ENSMUST00000121433; ENSMUSP00000113463; ENSMUSG00000027011.
DR GeneID; 22193; -.
DR KEGG; mmu:22193; -.
DR UCSC; uc008kgm.1; mouse.
DR CTD; 10477; -.
DR MGI; MGI:107412; Ube2e3.
DR VEuPathDB; HostDB:ENSMUSG00000027011; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155392; -.
DR HOGENOM; CLU_030988_14_4_1; -.
DR InParanoid; P52483; -.
DR OMA; GDRAKHD; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P52483; -.
DR TreeFam; TF101117; -.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22193; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Ube2e3; mouse.
DR PRO; PR:P52483; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P52483; protein.
DR Bgee; ENSMUSG00000027011; Expressed in pharyngeal arch 2 and 242 other tissues.
DR ExpressionAtlas; P52483; baseline and differential.
DR Genevisible; P52483; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; 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:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Growth regulation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
FT CHAIN 2..207
FT /note="Ubiquitin-conjugating enzyme E2 E3"
FT /id="PRO_0000082475"
FT DOMAIN 61..207
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
FT MUTAGEN 145
FT /note="C->S,A: Loss of enzymatic activity, interaction with
FT IPO11, nuclear import, and effect on cell growth."
FT /evidence="ECO:0000269|PubMed:14993279,
FT ECO:0000269|PubMed:15545318, ECO:0000269|PubMed:9872334"
FT CONFLICT 31
FT /note="E -> K (in Ref. 1; CAA63352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 22913 MW; 821CB1382478DC9F CRC64;
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS
TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY
PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV
GSIATQYLTN RAEHDRIARQ WTKRYAT
