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P52483 (UB2E3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 E3

EC=6.3.2.19
Alternative name(s):
UbcM2
Ubiquitin carrier protein E3
Ubiquitin-conjugating enzyme E2-23 kDa
Ubiquitin-protein ligase E3
Gene names
Name:Ube2e3
Synonyms:Ubce4, Ubcm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination By similarity. 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.5 Ref.6 Ref.7

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 207206Ubiquitin-conjugating enzyme E2 E3
PRO_0000082475

Sites

Active site1451Glycyl thioester intermediate

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue81Phosphoserine By similarity

Experimental info

Mutagenesis1451C → S or A: Loss of enzymatic activity, interaction with IPO11, nuclear import, and effect on cell growth. Ref.2 Ref.6 Ref.7
Sequence conflict311E → K in CAA63352. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52483 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: 821CB1382478DC9F

FASTA20722,913
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEDD4L, MUTAGENESIS OF CYS-145, FUNCTION.
+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.
CCDSCCDS16167.1.
RefSeqNP_033480.1. NM_009454.2.
XP_006499224.1. XM_006499161.1.
XP_006499225.1. XM_006499162.1.
XP_006499226.1. XM_006499163.1.
UniGeneMm.1485.
Mm.393087.

3D structure databases

ProteinModelPortalP52483.
SMRP52483. Positions 60-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204405. 8 interactions.
IntActP52483. 1 interaction.

PTM databases

PhosphoSiteP52483.

Proteomic databases

MaxQBP52483.
PaxDbP52483.
PRIDEP52483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028398; ENSMUSP00000028398; ENSMUSG00000027011.
ENSMUST00000121433; ENSMUSP00000113463; ENSMUSG00000027011.
GeneID22193.
KEGGmmu:22193.
UCSCuc008kgm.1. mouse.

Organism-specific databases

CTD10477.
MGIMGI:107412. Ube2e3.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00690000102027.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidP52483.
KOK06689.
OMAAKPNPKM.
PhylomeDBP52483.
TreeFamTF101117.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP52483.
BgeeP52483.
GenevestigatorP52483.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302169.
PROP52483.
SOURCESearch...

Entry information

Entry nameUB2E3_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot