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P68037

- UB2L3_MOUSE

UniProt

P68037 - UB2L3_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 L3

Gene

Ube2l3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis By similarity.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular response to glucocorticoid stimulus Source: UniProtKB
    3. cellular response to steroid hormone stimulus Source: UniProtKB
    4. protein K11-linked ubiquitination Source: UniProtKB
    5. protein polyubiquitination Source: UniProtKB
    6. protein ubiquitination Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription 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 L3 (EC:6.3.2.19)
    Alternative name(s):
    UbcM4
    Ubiquitin carrier protein L3
    Ubiquitin-protein ligase L3
    Gene namesi
    Name:Ube2l3
    Synonyms:Ubce7
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:109240. Ube2l3.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154Ubiquitin-conjugating enzyme E2 L3PRO_0000082477Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysineBy similarity
    Modified residuei131 – 1311N6-acetyllysineBy similarity
    Modified residuei138 – 1381N6-acetyllysineBy similarity

    Post-translational modificationi

    Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiP68037.
    PaxDbiP68037.
    PRIDEiP68037.

    PTM databases

    PhosphoSiteiP68037.

    Expressioni

    Gene expression databases

    ArrayExpressiP68037.
    BgeeiP68037.
    CleanExiMM_UBE2L3.
    GenevestigatoriP68037.

    Interactioni

    Subunit structurei

    Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204407. 11 interactions.
    IntActiP68037. 4 interactions.
    MINTiMINT-2736773.

    Structurei

    3D structure databases

    ProteinModelPortaliP68037.
    SMRiP68037. Positions 4-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119,respectively.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiP68037.
    KOiK04552.
    OMAiIALVNDX.
    OrthoDBiEOG7GXPD8.
    PhylomeDBiP68037.
    TreeFamiTF313043.

    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.

    P68037-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA    50
    FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK 100
    TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK 150
    RPVD 154
    Length:154
    Mass (Da):17,862
    Last modified:October 11, 2004 - v1
    Checksum:iF5A30243BE3C9985
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021D → V in AAB36018. (PubMed:8901595)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81004 Genomic DNA. Translation: AAB36018.1.
    X97042 mRNA. Translation: CAA65755.1.
    AJ130961 mRNA. Translation: CAA10265.1.
    AK007265 mRNA. Translation: BAB24925.1.
    CCDSiCCDS27997.1.
    PIRiJC6163.
    RefSeqiNP_033482.1. NM_009456.2.
    XP_006543833.1. XM_006543770.1.
    UniGeneiMm.3074.

    Genome annotation databases

    EnsembliENSMUST00000090192; ENSMUSP00000087658; ENSMUSG00000038965.
    ENSMUST00000115699; ENSMUSP00000111363; ENSMUSG00000038965.
    GeneIDi100042355.
    22195.
    KEGGimmu:100042355.
    mmu:22195.
    UCSCiuc007ykl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81004 Genomic DNA. Translation: AAB36018.1 .
    X97042 mRNA. Translation: CAA65755.1 .
    AJ130961 mRNA. Translation: CAA10265.1 .
    AK007265 mRNA. Translation: BAB24925.1 .
    CCDSi CCDS27997.1.
    PIRi JC6163.
    RefSeqi NP_033482.1. NM_009456.2.
    XP_006543833.1. XM_006543770.1.
    UniGenei Mm.3074.

    3D structure databases

    ProteinModelPortali P68037.
    SMRi P68037. Positions 4-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204407. 11 interactions.
    IntActi P68037. 4 interactions.
    MINTi MINT-2736773.

    PTM databases

    PhosphoSitei P68037.

    Proteomic databases

    MaxQBi P68037.
    PaxDbi P68037.
    PRIDEi P68037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000090192 ; ENSMUSP00000087658 ; ENSMUSG00000038965 .
    ENSMUST00000115699 ; ENSMUSP00000111363 ; ENSMUSG00000038965 .
    GeneIDi 100042355.
    22195.
    KEGGi mmu:100042355.
    mmu:22195.
    UCSCi uc007ykl.1. mouse.

    Organism-specific databases

    CTDi 7332.
    MGIi MGI:109240. Ube2l3.

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi P68037.
    KOi K04552.
    OMAi IALVNDX.
    OrthoDBi EOG7GXPD8.
    PhylomeDBi P68037.
    TreeFami TF313043.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 28696.
    PROi P68037.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68037.
    Bgeei P68037.
    CleanExi MM_UBE2L3.
    Genevestigatori P68037.

    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. "Provirus integration into a gene encoding a ubiquitin-conjugating enzyme results in a placental defect and embryonic lethality."
      Harbers K., Mueller U., Grams A., Li E., Jaenisch R., Franz T.
      Proc. Natl. Acad. Sci. U.S.A. 93:12412-12417(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    2. "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3."
      Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P., Coletta P.L., Lench N.J., Markham A.F.
      Mamm. Genome 6:725-731(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
      Tissue: Testis.

    Entry informationi

    Entry nameiUB2L3_MOUSE
    AccessioniPrimary (citable) accession number: P68037
    Secondary accession number(s): P51966, P70653, Q9HAV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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