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Q8CFI2

- UB2R1_MOUSE

UniProt

Q8CFI2 - UB2R1_MOUSE

Protein

Ubiquitin-conjugating enzyme E2 R1

Gene

Cdc34

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei93 – 931Glycyl thioester intermediatePROSITE-ProRule annotation

    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. cell cycle Source: UniProtKB-KW
    2. negative regulation of cAMP-mediated signaling Source: Ensembl
    3. positive regulation of inclusion body assembly Source: Ensembl
    4. positive regulation of neuron apoptotic process Source: Ensembl
    5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    6. protein K48-linked ubiquitination Source: UniProtKB
    7. protein monoubiquitination Source: UniProtKB
    8. response to growth factor Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 R1 (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin-conjugating enzyme E2-32 kDa complementing
    Ubiquitin-conjugating enzyme E2-CDC34
    Ubiquitin-protein ligase R1
    Gene namesi
    Name:Cdc34
    Synonyms:Ubch3, Ube2r1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:102657. Cdc34.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Ubiquitin-conjugating enzyme E2 R1PRO_0000082452Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031Phosphoserine; by CK2By similarity
    Modified residuei221 – 2211Phosphoserine; by CK2By similarity
    Modified residuei230 – 2301Phosphoserine; by CK2By similarity
    Modified residuei232 – 2321Phosphothreonine; by CK2By similarity
    Modified residuei235 – 2351Phosphoserine; by CK2By similarity

    Post-translational modificationi

    Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8CFI2.
    PaxDbiQ8CFI2.
    PRIDEiQ8CFI2.

    PTM databases

    PhosphoSiteiQ8CFI2.

    Expressioni

    Gene expression databases

    BgeeiQ8CFI2.
    CleanExiMM_CDC34.
    GenevestigatoriQ8CFI2.

    Interactioni

    Subunit structurei

    Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened By similarity. When phosphorylated, interacts with beta-TrCP (BTRC) By similarity. Interacts with casein kinase subunit CSNK2B By similarity.By similarity

    Protein-protein interaction databases

    BioGridi229706. 2 interactions.
    IntActiQ8CFI2. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CFI2.
    SMRiQ8CFI2. Positions 4-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 23546SCF-bindingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi200 – 23536Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110436.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiQ8CFI2.
    KOiK02207.
    OMAiRVNLVDE.
    OrthoDBiEOG7VB2HT.
    PhylomeDBiQ8CFI2.
    TreeFamiTF101107.

    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.

    Q8CFI2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN    50
    TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP 100
    VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK 150
    WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD 200
    EGSDLFYDDY YEDGEVEEAD SCFGDEEDDS GTEES 235
    Length:235
    Mass (Da):26,622
    Last modified:March 1, 2003 - v1
    Checksum:i3259FA0CD407E1E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC039160 mRNA. Translation: AAH39160.1.
    BC094502 mRNA. Translation: AAH94502.1.
    CCDSiCCDS23983.1.
    RefSeqiNP_808281.1. NM_177613.2.
    XP_006513543.1. XM_006513480.1.
    XP_006513544.1. XM_006513481.1.
    UniGeneiMm.21981.

    Genome annotation databases

    EnsembliENSMUST00000020550; ENSMUSP00000020550; ENSMUSG00000020307.
    ENSMUST00000166603; ENSMUSP00000128806; ENSMUSG00000020307.
    GeneIDi216150.
    KEGGimmu:216150.
    UCSCiuc007fzi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC039160 mRNA. Translation: AAH39160.1 .
    BC094502 mRNA. Translation: AAH94502.1 .
    CCDSi CCDS23983.1.
    RefSeqi NP_808281.1. NM_177613.2.
    XP_006513543.1. XM_006513480.1.
    XP_006513544.1. XM_006513481.1.
    UniGenei Mm.21981.

    3D structure databases

    ProteinModelPortali Q8CFI2.
    SMRi Q8CFI2. Positions 4-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229706. 2 interactions.
    IntActi Q8CFI2. 3 interactions.

    PTM databases

    PhosphoSitei Q8CFI2.

    Proteomic databases

    MaxQBi Q8CFI2.
    PaxDbi Q8CFI2.
    PRIDEi Q8CFI2.

    Protocols and materials databases

    DNASUi 216150.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020550 ; ENSMUSP00000020550 ; ENSMUSG00000020307 .
    ENSMUST00000166603 ; ENSMUSP00000128806 ; ENSMUSG00000020307 .
    GeneIDi 216150.
    KEGGi mmu:216150.
    UCSCi uc007fzi.1. mouse.

    Organism-specific databases

    CTDi 997.
    MGIi MGI:102657. Cdc34.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00730000110436.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi Q8CFI2.
    KOi K02207.
    OMAi RVNLVDE.
    OrthoDBi EOG7VB2HT.
    PhylomeDBi Q8CFI2.
    TreeFami TF101107.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi CDC34. mouse.
    NextBioi 375008.
    PROi Q8CFI2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CFI2.
    CleanExi MM_CDC34.
    Genevestigatori Q8CFI2.

    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. "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].
      Strain: 129 and C57BL/6J.
      Tissue: Mammary tumor.
    2. "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
      Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
      Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCF COMPLEX, FUNCTION.

    Entry informationi

    Entry nameiUB2R1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CFI2
    Secondary accession number(s): Q505K8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 101 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