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Protein

Ubiquitin-conjugating enzyme E2 E3

Gene

Ube2e3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei145 – 1451Glycyl thioester intermediate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Growth regulation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ube2e3
Synonyms:Ubce4, Ubcm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:107412. Ube2e3.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Shuttles between the nucleus and cytoplasm in a IPO11-dependent manner.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451C → S or A: Loss of enzymatic activity, interaction with IPO11, nuclear import, and effect on cell growth. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 207206Ubiquitin-conjugating enzyme E2 E3PRO_0000082475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei8 – 81PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52483.
PaxDbiP52483.
PRIDEiP52483.

PTM databases

PhosphoSiteiP52483.

Expressioni

Gene expression databases

BgeeiP52483.
ExpressionAtlasiP52483. baseline and differential.
GenevestigatoriP52483.

Interactioni

Subunit structurei

Interacts with NEDD4L. The ubiquitin-loaded form interacts specifically with importin-11 (IPO11), leading to its import into the nucleus.3 Publications

Protein-protein interaction databases

BioGridi204405. 9 interactions.
IntActiP52483. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP52483.
SMRiP52483. Positions 60-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP52483.
KOiK06689.
OMAiEPRKDTK.
PhylomeDBiP52483.
TreeFamiTF101117.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK
60 70 80 90 100
LSSKTTAKLS TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP
110 120 130 140 150
PGSVYEGGVF FLDITFSSDY PFKPPKVTFR TRIYHCNINS QGVICLDILK
160 170 180 190 200
DNWSPALTIS KVLLSICSLL TDCNPADPLV GSIATQYLTN RAEHDRIARQ

WTKRYAT
Length:207
Mass (Da):22,913
Last modified:May 24, 2004 - v2
Checksum:i821CB1382478DC9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311E → K in CAA63352 (PubMed:8576256).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16167.1.
RefSeqiNP_033480.1. NM_009454.2.
XP_006499224.1. XM_006499161.2.
XP_006499225.1. XM_006499162.2.
XP_006499226.1. XM_006499163.2.
UniGeneiMm.1485.
Mm.393087.

Genome annotation databases

EnsembliENSMUST00000028398; ENSMUSP00000028398; ENSMUSG00000027011.
ENSMUST00000121433; ENSMUSP00000113463; ENSMUSG00000027011.
GeneIDi22193.
KEGGimmu:22193.
UCSCiuc008kgm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16167.1.
RefSeqiNP_033480.1. NM_009454.2.
XP_006499224.1. XM_006499161.2.
XP_006499225.1. XM_006499162.2.
XP_006499226.1. XM_006499163.2.
UniGeneiMm.1485.
Mm.393087.

3D structure databases

ProteinModelPortaliP52483.
SMRiP52483. Positions 60-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204405. 9 interactions.
IntActiP52483. 1 interaction.

PTM databases

PhosphoSiteiP52483.

Proteomic databases

MaxQBiP52483.
PaxDbiP52483.
PRIDEiP52483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028398; ENSMUSP00000028398; ENSMUSG00000027011.
ENSMUST00000121433; ENSMUSP00000113463; ENSMUSG00000027011.
GeneIDi22193.
KEGGimmu:22193.
UCSCiuc008kgm.1. mouse.

Organism-specific databases

CTDi10477.
MGIiMGI:107412. Ube2e3.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP52483.
KOiK06689.
OMAiEPRKDTK.
PhylomeDBiP52483.
TreeFamiTF101117.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe2e3. mouse.
NextBioi302169.
PROiP52483.
SOURCEiSearch...

Gene expression databases

BgeeiP52483.
ExpressionAtlasiP52483. baseline and differential.
GenevestigatoriP52483.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUB2E3_MOUSE
AccessioniPrimary (citable) accession number: P52483
Secondary accession number(s): O09180, Q3TI00, Q91X63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 24, 2004
Last modified: April 1, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.