Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P52483

- UB2E3_MOUSE

UniProt

P52483 - UB2E3_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 E3

Gene

Ube2e3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (24 May 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. protein K11-linked ubiquitination Source: UniProtKB
    2. protein K48-linked ubiquitination Source: UniProtKB
    3. protein K63-linked ubiquitination Source: UniProtKB
    4. regulation of growth Source: UniProtKB-KW

    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: 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

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    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

    ArrayExpressiP52483.
    BgeeiP52483.
    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.
    GeneTreeiENSGT00690000102027.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiP52483.
    KOiK06689.
    OMAiAKPNPKM.
    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

    MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK    50
    LSSKTTAKLS TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP 100
    PGSVYEGGVF FLDITFSSDY PFKPPKVTFR TRIYHCNINS QGVICLDILK 150
    DNWSPALTIS KVLLSICSLL TDCNPADPLV GSIATQYLTN RAEHDRIARQ 200
    WTKRYAT 207
    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:
    EMBL
    GenBank
    DDBJ
    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_006499161.1.
    XP_006499225.1. XM_006499162.1.
    XP_006499226.1. XM_006499163.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS16167.1.
    RefSeqi NP_033480.1. NM_009454.2.
    XP_006499224.1. XM_006499161.1.
    XP_006499225.1. XM_006499162.1.
    XP_006499226.1. XM_006499163.1.
    UniGenei Mm.1485.
    Mm.393087.

    3D structure databases

    ProteinModelPortali P52483.
    SMRi P52483. Positions 60-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204405. 9 interactions.
    IntActi P52483. 1 interaction.

    PTM databases

    PhosphoSitei P52483.

    Proteomic databases

    MaxQBi P52483.
    PaxDbi P52483.
    PRIDEi P52483.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028398 ; ENSMUSP00000028398 ; ENSMUSG00000027011 .
    ENSMUST00000121433 ; ENSMUSP00000113463 ; ENSMUSG00000027011 .
    GeneIDi 22193.
    KEGGi mmu:22193.
    UCSCi uc008kgm.1. mouse.

    Organism-specific databases

    CTDi 10477.
    MGIi MGI:107412. Ube2e3.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00690000102027.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi P52483.
    KOi K06689.
    OMAi AKPNPKM.
    PhylomeDBi P52483.
    TreeFami TF101117.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 302169.
    PROi P52483.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52483.
    Bgeei P52483.
    Genevestigatori P52483.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 123 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