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Protein

Ubiquitin-conjugating enzyme E2 R1

Gene

CDC34

Organism
Homo sapiens (Human)
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-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. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes.13 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit.1 Publication

Kineticsi

  1. KM=0.11 µM for beta-catenin-monoubiquin1 Publication

    Pathway: protein ubiquitination

    This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
    View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei93 – 931Glycyl thioester intermediate

    GO - Molecular functioni

    GO - Biological processi

    • cellular protein modification process Source: UniProtKB
    • DNA replication initiation Source: UniProtKB
    • G1/S transition of mitotic cell cycle Source: UniProtKB
    • negative regulation of cAMP-mediated signaling Source: UniProtKB
    • positive regulation of inclusion body assembly Source: Ensembl
    • positive regulation of neuron apoptotic process Source: Ensembl
    • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    • protein K48-linked ubiquitination Source: UniProtKB
    • protein polyubiquitination Source: UniProtKB
    • protein ubiquitination Source: UniProtKB
    • response to growth factor Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.3.2.B6. 2681.
    ReactomeiREACT_188323. CLEC7A (Dectin-1) signaling.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP49427.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1734. CDC34.

    Subcellular locationi

    • Cytoplasm
    • Nucleus

    • 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.

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • nucleoplasm Source: HPA
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851N → Q: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication
    Mutagenesisi87 – 871Y → A: Decreases polyubiquitination of NFKBIA. 1 Publication
    Mutagenesisi93 – 931C → S or A: Loss of function. 2 Publications
    Mutagenesisi95 – 951S → D: Inhibits both mono and polyubiquitination of NFKBIA. 1 Publication
    Mutagenesisi97 – 971L → S: Loss of function. 1 Publication
    Mutagenesisi102 – 1021D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-103. 1 Publication
    Mutagenesisi103 – 1031D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-102. 1 Publication
    Mutagenesisi108 – 1081E → A: Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112. 1 Publication
    Mutagenesisi112 – 1121E → A: Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108. 1 Publication
    Mutagenesisi138 – 1381S → A: Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA. 1 Publication
    Mutagenesisi143 – 1431D → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153. 1 Publication
    Mutagenesisi147 – 1471M → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153. 1 Publication
    Mutagenesisi149 – 1491R → A: Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153. 1 Publication
    Mutagenesisi150 – 1501K → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153. 1 Publication
    Mutagenesisi153 – 1531E → A: Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150. 1 Publication
    Mutagenesisi203 – 2031S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236. 1 Publication
    Mutagenesisi222 – 2221S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236. 1 Publication
    Mutagenesisi231 – 2311S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236. 2 Publications
    Mutagenesisi233 – 2331T → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236. 1 Publication
    Mutagenesisi236 – 2361S → A: Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233. 1 Publication

    Organism-specific databases

    PharmGKBiPA26265.

    Polymorphism and mutation databases

    BioMutaiCDC34.
    DMDMi2507505.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Ubiquitin-conjugating enzyme E2 R1PRO_0000082451Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031Phosphoserine; by CK22 Publications
    Modified residuei222 – 2221Phosphoserine; by CK22 Publications
    Modified residuei231 – 2311Phosphoserine; by CK23 Publications
    Modified residuei233 – 2331Phosphothreonine; by CK21 Publication
    Modified residuei236 – 2361Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Autoubiquitinated. Autoubiquitination is promoted by the human herpes virus 1 protein ICP0 and leads to degradation by the Ubiquitin-proteasomal pathway.2 Publications
    Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP49427.
    PaxDbiP49427.
    PeptideAtlasiP49427.
    PRIDEiP49427.

    PTM databases

    PhosphoSiteiP49427.

    Expressioni

    Tissue specificityi

    Expressed in testes during spermatogenesis to regulate repression of cAMP-induced transcription.1 Publication

    Inductioni

    Negatively regulated by the let-7 microRNA.1 Publication

    Gene expression databases

    BgeeiP49427.
    CleanExiHS_CDC34.
    ExpressionAtlasiP49427. baseline and differential.
    GenevisibleiP49427. HS.

    Organism-specific databases

    HPAiCAB005109.
    CAB047311.
    HPA002382.

    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. When phosphorylated, interacts with beta-TrCP (BTRC). Interacts with human herpes virus 1 protein ICP0 and associates with the proteasome for degradation. Interacts with casein kinase subunit CSNK2B.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUL1Q136163EBI-975634,EBI-359390
    SDCBPO005603EBI-975634,EBI-727004
    SIAH1Q8IUQ43EBI-975634,EBI-747107

    Protein-protein interaction databases

    BioGridi107432. 57 interactions.
    DIPiDIP-37783N.
    IntActiP49427. 15 interactions.
    MINTiMINT-238910.
    STRINGi9606.ENSP00000215574.

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 2215Combined sources
    Beta strandi28 – 325Combined sources
    Beta strandi40 – 467Combined sources
    Turni52 – 554Combined sources
    Beta strandi57 – 637Combined sources
    Turni66 – 694Combined sources
    Beta strandi74 – 796Combined sources
    Beta strandi90 – 923Combined sources
    Helixi94 – 974Combined sources
    Helixi120 – 13213Combined sources
    Helixi142 – 15312Combined sources
    Turni154 – 1563Combined sources
    Helixi160 – 17819Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OB4X-ray2.40A7-184[»]
    3RZ3X-ray2.30A/B/C/D7-184[»]
    4MDKX-ray2.61A/B/C/D7-184[»]
    ProteinModelPortaliP49427.
    SMRiP49427. Positions 7-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49427.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 23647SCF-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi200 – 23637Asp/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.2 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110436.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiP49427.
    KOiK02207.
    OMAiRVNLVDE.
    OrthoDBiEOG7VB2HT.
    PhylomeDBiP49427.
    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.

    P49427-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN
    60 70 80 90 100
    TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP
    110 120 130 140 150
    VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK
    160 170 180 190 200
    WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD
    210 220 230
    EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES
    Length:236
    Mass (Da):26,737
    Last modified:November 1, 1997 - v2
    Checksum:i258960666B589DB3
    GO

    Sequence cautioni

    The sequence AAC37534.1 differs from that shown. Reason: Erroneous initiation. Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti227 – 2271D → H.1 Publication
    Corresponds to variant rs16990650 [ dbSNP | Ensembl ].
    VAR_021277

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L22005 mRNA. Translation: AAC37534.1. Different initiation.
    BT006659 mRNA. Translation: AAP35305.1.
    AY650399 Genomic DNA. Translation: AAT46688.1.
    AK291554 mRNA. Translation: BAF84243.1.
    CH471242 Genomic DNA. Translation: EAW61190.1.
    BC009850 mRNA. Translation: AAH09850.1.
    BC018143 mRNA. Translation: AAH18143.1.
    BC023979 mRNA. Translation: AAH23979.1.
    CCDSiCCDS12030.1.
    PIRiA49630.
    RefSeqiNP_004350.1. NM_004359.1.
    UniGeneiHs.514997.

    Genome annotation databases

    EnsembliENST00000215574; ENSP00000215574; ENSG00000099804.
    GeneIDi997.
    KEGGihsa:997.
    UCSCiuc002lov.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L22005 mRNA. Translation: AAC37534.1. Different initiation.
    BT006659 mRNA. Translation: AAP35305.1.
    AY650399 Genomic DNA. Translation: AAT46688.1.
    AK291554 mRNA. Translation: BAF84243.1.
    CH471242 Genomic DNA. Translation: EAW61190.1.
    BC009850 mRNA. Translation: AAH09850.1.
    BC018143 mRNA. Translation: AAH18143.1.
    BC023979 mRNA. Translation: AAH23979.1.
    CCDSiCCDS12030.1.
    PIRiA49630.
    RefSeqiNP_004350.1. NM_004359.1.
    UniGeneiHs.514997.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OB4X-ray2.40A7-184[»]
    3RZ3X-ray2.30A/B/C/D7-184[»]
    4MDKX-ray2.61A/B/C/D7-184[»]
    ProteinModelPortaliP49427.
    SMRiP49427. Positions 7-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107432. 57 interactions.
    DIPiDIP-37783N.
    IntActiP49427. 15 interactions.
    MINTiMINT-238910.
    STRINGi9606.ENSP00000215574.

    PTM databases

    PhosphoSiteiP49427.

    Polymorphism and mutation databases

    BioMutaiCDC34.
    DMDMi2507505.

    Proteomic databases

    MaxQBiP49427.
    PaxDbiP49427.
    PeptideAtlasiP49427.
    PRIDEiP49427.

    Protocols and materials databases

    DNASUi997.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000215574; ENSP00000215574; ENSG00000099804.
    GeneIDi997.
    KEGGihsa:997.
    UCSCiuc002lov.3. human.

    Organism-specific databases

    CTDi997.
    GeneCardsiGC19P000532.
    HGNCiHGNC:1734. CDC34.
    HPAiCAB005109.
    CAB047311.
    HPA002382.
    MIMi116948. gene.
    neXtProtiNX_P49427.
    PharmGKBiPA26265.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00730000110436.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiP49427.
    KOiK02207.
    OMAiRVNLVDE.
    OrthoDBiEOG7VB2HT.
    PhylomeDBiP49427.
    TreeFamiTF101107.

    Enzyme and pathway databases

    UniPathwayiUPA00143.
    BRENDAi2.3.2.B6. 2681.
    ReactomeiREACT_188323. CLEC7A (Dectin-1) signaling.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP49427.

    Miscellaneous databases

    EvolutionaryTraceiP49427.
    GeneWikiiCDC34.
    GenomeRNAii997.
    NextBioi4188.
    PROiP49427.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP49427.
    CleanExiHS_CDC34.
    ExpressionAtlasiP49427. baseline and differential.
    GenevisibleiP49427. HS.

    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. "Cloning of the human homolog of the CDC34 cell cycle gene by complementation in yeast."
      Plon S.E., Leppig K.A., Do H.N., Groudine M.
      Proc. Natl. Acad. Sci. U.S.A. 90:10484-10488(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIEHS SNPs program
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-227.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Lung.
    7. "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha."
      Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A.
      J. Biol. Chem. 274:14823-14830(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-93.
    8. "Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis."
      Pati D., Meistrich M.L., Plon S.E.
      Mol. Cell. Biol. 19:5001-5013(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF5 AND CREM, FUNCTION, TISSUE SPECIFICITY.
    9. "Association of human ubiquitin-conjugating enzyme CDC34 with the mitotic spindle in anaphase."
      Reymond F., Wirbelauer C., Krek W.
      J. Cell Sci. 113:1687-1694(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN.
    10. "Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement of the Cdc34-SCF(p45Skp2) pathway."
      Charrasse S., Carena I., Brondani V., Klempnauer K.H., Ferrari S.
      Oncogene 19:2986-2995(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4."
      Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M.
      Oncogene 19:3529-3536(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCF COMPLEX.
    12. "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2."
      Block K., Boyer T.G., Yew P.R.
      J. Biol. Chem. 276:41049-41058(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSNK2B, PHOSPHORYLATION AT SER-203; SER-222; SER-231; THR-233 AND SER-236, MUTAGENESIS OF SER-203; SER-222; SER-231; THR-233 AND SER-236, SUBCELLULAR LOCATION.
    13. "The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity."
      Van Sant C., Hagglund R., Lopez P., Roizman B.
      Proc. Natl. Acad. Sci. U.S.A. 98:8815-8820(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN HERPESVIRUS 1 PROTEIN ICP0, ASSOCIATION WITH THE PROTEASOME.
    14. "The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34."
      Wu K., Chen A., Tan P., Pan Z.Q.
      J. Biol. Chem. 277:516-527(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCF COMPLEX, FUNCTION, ENZYME REGULATION.
    15. "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."
      Semplici F., Meggio F., Pinna L.A., Oliviero S.
      Oncogene 21:3978-3987(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION AT SER-231, MUTAGENESIS OF CYS-93; LEU-97 AND SER-231.
    16. "Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes."
      Hagglund R., Van Sant C., Lopez P., Roizman B.
      Proc. Natl. Acad. Sci. U.S.A. 99:631-636(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AUTOUBIQUITINATION.
    17. "Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0."
      Hagglund R., Roizman B.
      Proc. Natl. Acad. Sci. U.S.A. 99:7889-7894(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 PROTEIN ICP0, AUTOUBIQUITINATION.
    18. "The human ubiquitin-conjugating enzyme Cdc34 controls cellular proliferation through regulation of p27Kip1 protein levels."
      Butz N., Ruetz S., Natt F., Hall J., Weiler J., Mestan J., Ducarre M., Grossenbacher R., Hauser P., Kempf D., Hofmann F.
      Exp. Cell Res. 303:482-493(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box (SCF)-mediated ubiquitination and cell cycle progression."
      Sadowski M., Mawson A., Baker R., Sarcevic B.
      Biochem. J. 405:569-581(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-203; SER-222 AND SER-231, FUNCTION.
    20. "Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains."
      Gazdoiu S., Yamoah K., Wu K., Pan Z.Q.
      Mol. Cell. Biol. 27:7041-7052(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASN-85; TYR-87; SER-95; ASP-102; ASP-103; GLU-108; GLU-112; SER-138; ASP-143; MET-147; ARG-149; LYS-150 AND GLU-153.
    21. "Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation."
      Saha A., Deshaies R.J.
      Mol. Cell 32:21-31(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCF COMPLEX.
    22. "Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates."
      Kleiger G., Saha A., Lewis S., Kuhlman B., Deshaies R.J.
      Cell 139:957-968(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCF COMPLEX, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES.
    23. "Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src."
      Cen B., Li H., Weinstein I.B.
      J. Biol. Chem. 284:5265-5276(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A UBIQUITIN LIGASE COMPLEX WITH HINT1 AND RBX1, FUNCTION.
    24. "let-7 Overexpression leads to an increased fraction of cells in G2/M, direct down-regulation of Cdc34, and stabilization of Wee1 kinase in primary fibroblasts."
      Legesse-Miller A., Elemento O., Pfau S.J., Forman J.J., Tavazoie S., Coller H.A.
      J. Biol. Chem. 284:6605-6609(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION.
    25. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
      David Y., Ziv T., Admon A., Navon A.
      J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    26. "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
      Wu K., Kovacev J., Pan Z.Q.
      Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Human ubiquitin-conjugating enzyme cdc34."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-184.

    Entry informationi

    Entry nameiUB2R1_HUMAN
    AccessioniPrimary (citable) accession number: P49427
    Secondary accession number(s): A8K689
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 1, 1997
    Last modified: June 24, 2015
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. 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.