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UniProtKB/Swiss-Prot entry P52483


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UB2E3_MOUSE
Primary accession number P52483
Secondary accession numbers O09180 Q3TI00 Q91X63
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on May 24, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 68)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 E3
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase E3
Ubiquitin carrier protein E3
Ubiquitin-conjugating enzyme E2-23 kDa
UbcM2
Gene name
Name: Ube2e3
Synonyms: Ubce4, Ubcm2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
DOI=10.1074/jbc.271.5.2789; PubMed=8576256 [NCBI, ExPASy, EBI, Israel, Japan]
Matuschewski K., Hauser H.P., Treier M., Jentsch S.;
"Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions.";
J. Biol. Chem. 271:2789-2794(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF CYS-145.
STRAIN=Swiss;
DOI=10.1038/sj.onc.1202260; PubMed=9872334 [NCBI, ExPASy, EBI, Israel, Japan]
Pestov D.G., Grzeszkiewicz T.M., Lau L.F.;
"Isolation of growth suppressors from a cDNA expression library.";
Oncogene 17:3187-3197(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH IPO11, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/19.20.5502; PubMed=11032817 [NCBI, ExPASy, EBI, Israel, Japan]
Plafker S.M., Macara I.G.;
"Importin-11, a nuclear import receptor for the ubiquitin-conjugating enzyme, UbcM2.";
EMBO J. 19:5502-5513(2000).
[6]
INTERACTION WITH IPO11, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-145.
DOI=10.1083/jcb.200406001; PubMed=15545318 [NCBI, ExPASy, EBI, Israel, Japan]
Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G.;
"Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import.";
J. Cell Biol. 167:649-659(2004).
[7]
INTERACTION WITH NEDD4L, MUTAGENESIS OF CYS-145, AND FUNCTION.
DOI=10.1128/MCB.24.6.2397-2409.2004; PubMed=14993279 [NCBI, ExPASy, EBI, Israel, Japan]
Debonneville C., Staub O.;
"Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-dependent regulation of the epithelial Na+ channel.";
Mol. Cell. Biol. 24:2397-2409(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND MASS SPECTROMETRY.
TISSUE=Mast cell;
PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.";
J. Immunol. 179:5864-5876(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X92664; CAA63352.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003346; AAB60948.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK076011; BAC36118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168072; BAE40046.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011477; AAH11477.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_033480.1; -.
XP_001477430.1; -.
UniGene Mm.1485
3D structure databases
HSSP P15731; 1QCQ. [HSSP ENTRY / PDB]
SMR P52483; 60-207.
ModBase P52483.
PTM databases
PhosphoSite P52483; -.
Organism-specific databases
MGI MGI:107412; Ube2e3.
Gene expression databases
ArrayExpress P52483; -.
GermOnline ENSMUSG00000027011; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from MGI).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P52483.
Genome annotation databases
Ensembl ENSMUSG00000027011; Mus musculus. [Contig view]
GeneID 100047012; -.
22193; -.
KEGG mmu:100047012; -.
mmu:22193; -.
Phylogenomic databases
HOGENOM P52483; -.
HOVERGEN P52483; -.
Other
SOURCE Ube2e3; Mus musculus.
ProtoNet P52483.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Growth regulation; Ligase; Nucleus; Phosphoprotein; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   207  207     Ubiquitin-conjugating enzyme E2 E3. PRO_0000082475
ACT_SITE   145   145        Glycyl thioester intermediate. 
MOD_RES   12    12        Phosphoserine (By similarity). 
MOD_RES   91    91        Phosphotyrosine. 
MUTAGEN   145   145        C->S,A: Loss of enzymatic activity, interaction with IPO11, nuclear import, and effect on cell growth. 
CONFLICT   31    31        E -> K (in Ref. 1; CAA63352). 
Sequence information
Length: 207 AA [This is the length of the unprocessed precursor] Molecular weight: 22913 Da [This is the MW of the unprocessed precursor] CRC64: 821CB1382478DC9F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS 

        70         80         90        100        110        120 
TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY 

       130        140        150        160        170        180 
PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV 

       190        200 
GSIATQYLTN RAEHDRIARQ WTKRYAT 

P52483 in FASTA format

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