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   25-NOV-2008, entry version 70.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 E3;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase E3;
DE   AltName: Full=Ubiquitin carrier protein E3;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-23 kDa;
DE            Short=UbcM2;
GN   Name=Ube2e3; Synonyms=Ubce4, Ubcm2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=96162026; 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
RT   with 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=Swiss;
RX   MEDLINE=99087339; 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/2;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Participates in the regulation of transepithelial sodium
CC       transport in renal cells. May be involved in cell growth arrest.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with NEDD4L. The ubiquitin-loaded form
CC       interacts specifically with importin-11 (IPO11), leading to its
CC       import into the nucleus.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and cytoplasm in a IPO11-dependent manner.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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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   RefSeq; NP_033480.1; -.
DR   RefSeq; XP_001477430.1; -.
DR   UniGene; Mm.1485; -.
DR   UniGene; Mm.393087; -.
DR   HSSP; P15731; 1QCQ.
DR   SMR; P52483; 60-207.
DR   PhosphoSite; P52483; -.
DR   Ensembl; ENSMUSG00000027011; Mus musculus.
DR   GeneID; 100047012; -.
DR   GeneID; 22193; -.
DR   KEGG; mmu:100047012; -.
DR   KEGG; mmu:22193; -.
DR   MGI; MGI:107412; Ube2e3.
DR   HOGENOM; P52483; -.
DR   HOVERGEN; P52483; -.
DR   NextBio; 460449; -.
DR   ArrayExpress; P52483; -.
DR   GermOnline; ENSMUSG00000027011; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:UniProtKB-KW.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   PANTHER; PTHR11621; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Growth regulation; Ligase; Nucleus; Phosphoprotein;
KW   Ubl conjugation pathway.
FT   CHAIN         1    207       Ubiquitin-conjugating enzyme E2 E3.
FT                                /FTId=PRO_0000082475.
FT   ACT_SITE    145    145       Glycyl thioester intermediate.
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      91     91       Phosphotyrosine.
FT   MUTAGEN     145    145       C->S,A: Loss of enzymatic activity,
FT                                interaction with IPO11, nuclear import,
FT                                and effect on cell growth.
FT   CONFLICT     31     31       E -> K (in Ref. 1; CAA63352).
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
//