Reviewed, UniProtKB/Swiss-Prot P52483 (UB2E3_MOUSE)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 E3
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase E3
    Ubiquitin carrier protein E3
    Ubiquitin-conjugating enzyme E2-23 kDa
      Short name=UbcM2

Gene names

Name:	Ube2e3
Synonyms:	Ubce4, Ubcm2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest. Ref.7
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with NEDD4L. The ubiquitin-loaded form interacts specifically with importin-11 (IPO11), leading to its import into the nucleus. Ref.7 Ref.5 Ref.6
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner. Ref.5 Ref.6
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Growth regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein modification Inferred from electronic annotation. Source: InterPro regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Ubiquitin-conjugating enzyme E2 E3		PRO_0000082475
Sites
	Active site	145	1	Glycyl thioester intermediate
Amino acid modifications
	Modified residue	3	1	Phosphoserine By similarity
	Modified residue	12	1	Phosphoserine By similarity
	Modified residue	91	1	Phosphotyrosine Ref.8
Experimental info
	Mutagenesis	145	1	C → S or A: Loss of enzymatic activity, interaction with IPO11, nuclear import, and effect on cell growth. Ref.7 Ref.6 Ref.2
	Sequence conflict	31	1	E → K in CAA63352. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52483-1 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: 821CB1382478DC9F	FASTA	207	22,913
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions." Matuschewski K., Hauser H.P., Treier M., Jentsch S. J. Biol. Chem. 271:2789-2794(1996) [PubMed: 8576256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Isolation of growth suppressors from a cDNA expression library." Pestov D.G., Grzeszkiewicz T.M., Lau L.F. Oncogene 17:3187-3197(1998) [PubMed: 9872334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-145. Strain: Swiss.
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	"Importin-11, a nuclear import receptor for the ubiquitin-conjugating enzyme, UbcM2." Plafker S.M., Macara I.G. EMBO J. 19:5502-5513(2000) [PubMed: 11032817] [Abstract] Cited for: INTERACTION WITH IPO11, SUBCELLULAR LOCATION.
[6]	"Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import." Plafker S.M., Plafker K.S., Weissman A.M., Macara I.G. J. Cell Biol. 167:649-659(2004) [PubMed: 15545318] [Abstract] Cited for: INTERACTION WITH IPO11, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-145.
[7]	"Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-dependent regulation of the epithelial Na+ channel." Debonneville C., Staub O. Mol. Cell. Biol. 24:2397-2409(2004) [PubMed: 14993279] [Abstract] Cited for: INTERACTION WITH NEDD4L, MUTAGENESIS OF CYS-145, FUNCTION.
[8]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, MASS SPECTROMETRY. Tissue: Mast cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X92664 mRNA. Translation: CAA63352.1. AF003346 mRNA. Translation: AAB60948.1. AK076011 mRNA. Translation: BAC36118.1. AK168072 mRNA. Translation: BAE40046.1. BC011477 mRNA. Translation: AAH11477.1.
IPI	IPI00323176.
RefSeq	NP_033480.1. XP_001477430.1.
UniGene	Mm.1485 Mm.393087
3D structure databases
SMR	P52483. Positions 60-207.
ModBase	Search...
Protein-protein interaction databases
STRING	P52483.
PTM databases
PhosphoSite	P52483.
Proteomic databases
PRIDE	P52483.
Genome annotation databases
Ensembl	ENSMUST00000028398; ENSMUSP00000028398; ENSMUSG00000027011; Mus musculus. [Genome view] ENSMUST00000121433; ENSMUSP00000113463; ENSMUSG00000027011; Mus musculus. [Genome view]
GeneID	100047012. 22193.
KEGG	mmu:100047012. mmu:22193.
UCSC	uc008kgn.1. mouse.
Organism-specific databases
CTD	22193.
MGI	MGI:107412. Ube2e3.
Phylogenomic databases
eggNOG	roNOG11519.
HOGENOM	HBG756483.
HOVERGEN	P52483.
InParanoid	P52483.
OMA	NSQGAIC.
PhylomeDB	P52483.
Enzyme and pathway databases
BRENDA	6.3.2.19. 244.
Gene expression databases
ArrayExpress	P52483.
Bgee	P52483.
Genevestigator	P52483.
GermOnline	ENSMUSG00000027011. Mus musculus.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	460449.
SOURCE	Search...

Entry information

Entry name

UB2E3_MOUSE

Accession

Primary (citable) accession number: P52483
Secondary accession number(s): O09180, Q3TI00, Q91X63

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 24, 2004
Last modified:	February 9, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)