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P61077

- UB2D3_HUMAN

UniProt

P61077 - UB2D3_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 D3

Gene

UBE2D3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction 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 sitei85 – 851Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. BMP signaling pathway Source: Reactome
    3. cellular protein modification process Source: ProtInc
    4. cellular response to hypoxia Source: Reactome
    5. DNA repair Source: UniProtKB-KW
    6. gene expression Source: Reactome
    7. innate immune response Source: Reactome
    8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    9. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    10. negative regulation of type I interferon production Source: Reactome
    11. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    12. protein K11-linked ubiquitination Source: UniProtKB
    13. protein K48-linked ubiquitination Source: UniProtKB
    14. protein monoubiquitination Source: UniProtKB
    15. protein polyubiquitination Source: UniProtKB
    16. protein ubiquitination Source: UniProtKB
    17. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    18. toll-like receptor 3 signaling pathway Source: Reactome
    19. toll-like receptor 4 signaling pathway Source: Reactome
    20. toll-like receptor signaling pathway Source: Reactome
    21. transcription, DNA-templated Source: Reactome
    22. transcription initiation from RNA polymerase II promoter Source: Reactome
    23. transforming growth factor beta receptor signaling pathway Source: Reactome
    24. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    25. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_12034. Signaling by BMP.
    REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP61077.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 D3 (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein D3
    Ubiquitin-conjugating enzyme E2(17)KB 3
    Ubiquitin-conjugating enzyme E2-17 kDa 3
    Ubiquitin-protein ligase D3
    Gene namesi
    Name:UBE2D3
    Synonyms:UBC5C, UBCH5C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:12476. UBE2D3.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome membrane Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771N → S: Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PARK2. 1 Publication
    Mutagenesisi85 – 851C → A: Loss of function. 1 Publication
    Mutagenesisi87 – 871D → E or P: Has intermediate lysine reactivity. 1 Publication
    Mutagenesisi87 – 871D → K: Abolishes affect lysine reactivity. 1 Publication
    Mutagenesisi87 – 871D → N: Does not affect lysine reactivity. 1 Publication
    Mutagenesisi117 – 1171D → H: Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1. 1 Publication

    Organism-specific databases

    PharmGKBiPA37126.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D3PRO_0000082466Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 1071 Publication

    Post-translational modificationi

    Phosphorylated by AURKB.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP61077.
    PRIDEiP61077.

    PTM databases

    PhosphoSiteiP61077.

    Expressioni

    Gene expression databases

    ArrayExpressiP61077.
    BgeeiP61077.
    CleanExiHS_UBE2D3.
    GenevestigatoriP61077.

    Organism-specific databases

    HPAiHPA003920.

    Interactioni

    Subunit structurei

    Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex; when Cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts with BRCA1; the DNA damage checkpoint promotes the association with BRCA1 after ionizing radiation. Interacts non-covalently with ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OTUB1Q96FW14EBI-348268,EBI-1058491
    RNF11Q9Y3C53EBI-348268,EBI-396669
    RNF126Q9BV683EBI-348268,EBI-357322
    RNF43Q68DV72EBI-348268,EBI-1647060
    RNF5Q999423EBI-348268,EBI-348482
    TRAF6Q9Y4K32EBI-348268,EBI-359276
    XIAPP981702EBI-348268,EBI-517127
    ZNRF1Q8ND253EBI-348268,EBI-2129250

    Protein-protein interaction databases

    BioGridi113171. 194 interactions.
    DIPiDIP-29062N.
    IntActiP61077. 92 interactions.
    MINTiMINT-1032046.
    STRINGi9606.ENSP00000349722.

    Structurei

    Secondary structure

    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1515
    Beta strandi21 – 266
    Beta strandi32 – 387
    Beta strandi41 – 433
    Turni44 – 474
    Beta strandi49 – 557
    Turni58 – 614
    Beta strandi66 – 694
    Helixi87 – 893
    Turni90 – 923
    Helixi99 – 11113
    Helixi121 – 1299
    Helixi131 – 14515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X23X-ray1.85A/B/C/D1-147[»]
    2FUHNMR-A2-147[»]
    3L1ZX-ray3.17A1-147[»]
    3RPGX-ray2.65A2-147[»]
    3UGBX-ray2.35A1-147[»]
    4BVUX-ray2.70B1-147[»]
    ProteinModelPortaliP61077.
    SMRiP61077. Positions 1-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61077.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG063308.
    KOiK06689.
    OMAiSAGPCED.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiP61077.
    TreeFamiTF101108.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61077-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF    50
    FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS 100
    KVLLSICSLL CDPNPDDPLV PEIARIYKTD RDKYNRISRE WTQKYAM 147
    Length:147
    Mass (Da):16,687
    Last modified:April 26, 2004 - v1
    Checksum:iADD74A8A708EFEE3
    GO
    Isoform 2 (identifier: P61077-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-147: YNRISREWTQKYAM → YNRLAREWTEKYAML

    Show »
    Length:148
    Mass (Da):16,785
    Checksum:iE73DC194DB6D4EFE
    GO
    Isoform 3 (identifier: P61077-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: MALKRINK → MLSNRKCLSK

    Show »
    Length:149
    Mass (Da):16,893
    Checksum:iF20F36FCD312444A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501Missing in DB045280. (PubMed:14702039)Curated
    Sequence conflicti123 – 1231I → L in AAH66917. (PubMed:15489334)Curated
    Sequence conflicti137 – 1371I → V in CAG33197. (PubMed:14702039)Curated
    Sequence conflicti147 – 1471M → I in CAG33197. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88MALKRINK → MLSNRKCLSK in isoform 3. 1 PublicationVSP_038096
    Alternative sequencei134 – 14714YNRIS…QKYAM → YNRLAREWTEKYAML in isoform 2. 1 PublicationVSP_038097Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39318 mRNA. Translation: AAA91461.1.
    AF213884 Genomic DNA. Translation: AAF35234.1.
    AK095822 mRNA. Translation: BAC04632.1.
    DB045280 mRNA. No translation available.
    CR456916 mRNA. Translation: CAG33197.1.
    AC018797 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06138.1.
    CH471057 Genomic DNA. Translation: EAX06143.1.
    BC003395 mRNA. Translation: AAH03395.1.
    BC037894 mRNA. Translation: AAH37894.1.
    BC066917 mRNA. Translation: AAH66917.1.
    CCDSiCCDS3659.1. [P61077-3]
    CCDS3660.1. [P61077-1]
    CCDS3661.1. [P61077-2]
    RefSeqiNP_003331.1. NM_003340.6. [P61077-1]
    NP_871615.1. NM_181886.3. [P61077-1]
    NP_871616.1. NM_181887.2. [P61077-1]
    NP_871617.1. NM_181888.3. [P61077-1]
    NP_871618.1. NM_181889.2. [P61077-1]
    NP_871619.1. NM_181890.2. [P61077-1]
    NP_871620.1. NM_181891.2. [P61077-1]
    NP_871621.1. NM_181892.3. [P61077-2]
    NP_871622.1. NM_181893.2. [P61077-3]
    XP_005263257.1. XM_005263200.2. [P61077-2]
    XP_006714360.1. XM_006714297.1. [P61077-2]
    XP_006714361.1. XM_006714298.1. [P61077-2]
    XP_006714362.1. XM_006714299.1. [P61077-2]
    UniGeneiHs.518773.
    Hs.595430.
    Hs.621366.

    Genome annotation databases

    EnsembliENST00000321805; ENSP00000318494; ENSG00000109332. [P61077-1]
    ENST00000338145; ENSP00000337208; ENSG00000109332. [P61077-1]
    ENST00000343106; ENSP00000345285; ENSG00000109332. [P61077-2]
    ENST00000349311; ENSP00000344069; ENSG00000109332. [P61077-1]
    ENST00000357194; ENSP00000349722; ENSG00000109332. [P61077-3]
    ENST00000394801; ENSP00000378280; ENSG00000109332. [P61077-1]
    ENST00000394803; ENSP00000378282; ENSG00000109332. [P61077-1]
    ENST00000394804; ENSP00000378283; ENSG00000109332. [P61077-1]
    ENST00000453744; ENSP00000396901; ENSG00000109332. [P61077-1]
    GeneIDi7323.
    KEGGihsa:7323.
    UCSCiuc003hwi.3. human. [P61077-2]
    uc003hwk.3. human. [P61077-1]
    uc003hwq.3. human. [P61077-3]

    Polymorphism databases

    DMDMi46577654.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39318 mRNA. Translation: AAA91461.1 .
    AF213884 Genomic DNA. Translation: AAF35234.1 .
    AK095822 mRNA. Translation: BAC04632.1 .
    DB045280 mRNA. No translation available.
    CR456916 mRNA. Translation: CAG33197.1 .
    AC018797 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX06138.1 .
    CH471057 Genomic DNA. Translation: EAX06143.1 .
    BC003395 mRNA. Translation: AAH03395.1 .
    BC037894 mRNA. Translation: AAH37894.1 .
    BC066917 mRNA. Translation: AAH66917.1 .
    CCDSi CCDS3659.1. [P61077-3 ]
    CCDS3660.1. [P61077-1 ]
    CCDS3661.1. [P61077-2 ]
    RefSeqi NP_003331.1. NM_003340.6. [P61077-1 ]
    NP_871615.1. NM_181886.3. [P61077-1 ]
    NP_871616.1. NM_181887.2. [P61077-1 ]
    NP_871617.1. NM_181888.3. [P61077-1 ]
    NP_871618.1. NM_181889.2. [P61077-1 ]
    NP_871619.1. NM_181890.2. [P61077-1 ]
    NP_871620.1. NM_181891.2. [P61077-1 ]
    NP_871621.1. NM_181892.3. [P61077-2 ]
    NP_871622.1. NM_181893.2. [P61077-3 ]
    XP_005263257.1. XM_005263200.2. [P61077-2 ]
    XP_006714360.1. XM_006714297.1. [P61077-2 ]
    XP_006714361.1. XM_006714298.1. [P61077-2 ]
    XP_006714362.1. XM_006714299.1. [P61077-2 ]
    UniGenei Hs.518773.
    Hs.595430.
    Hs.621366.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X23 X-ray 1.85 A/B/C/D 1-147 [» ]
    2FUH NMR - A 2-147 [» ]
    3L1Z X-ray 3.17 A 1-147 [» ]
    3RPG X-ray 2.65 A 2-147 [» ]
    3UGB X-ray 2.35 A 1-147 [» ]
    4BVU X-ray 2.70 B 1-147 [» ]
    ProteinModelPortali P61077.
    SMRi P61077. Positions 1-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113171. 194 interactions.
    DIPi DIP-29062N.
    IntActi P61077. 92 interactions.
    MINTi MINT-1032046.
    STRINGi 9606.ENSP00000349722.

    PTM databases

    PhosphoSitei P61077.

    Polymorphism databases

    DMDMi 46577654.

    Proteomic databases

    MaxQBi P61077.
    PRIDEi P61077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321805 ; ENSP00000318494 ; ENSG00000109332 . [P61077-1 ]
    ENST00000338145 ; ENSP00000337208 ; ENSG00000109332 . [P61077-1 ]
    ENST00000343106 ; ENSP00000345285 ; ENSG00000109332 . [P61077-2 ]
    ENST00000349311 ; ENSP00000344069 ; ENSG00000109332 . [P61077-1 ]
    ENST00000357194 ; ENSP00000349722 ; ENSG00000109332 . [P61077-3 ]
    ENST00000394801 ; ENSP00000378280 ; ENSG00000109332 . [P61077-1 ]
    ENST00000394803 ; ENSP00000378282 ; ENSG00000109332 . [P61077-1 ]
    ENST00000394804 ; ENSP00000378283 ; ENSG00000109332 . [P61077-1 ]
    ENST00000453744 ; ENSP00000396901 ; ENSG00000109332 . [P61077-1 ]
    GeneIDi 7323.
    KEGGi hsa:7323.
    UCSCi uc003hwi.3. human. [P61077-2 ]
    uc003hwk.3. human. [P61077-1 ]
    uc003hwq.3. human. [P61077-3 ]

    Organism-specific databases

    CTDi 7323.
    GeneCardsi GC04M103717.
    HGNCi HGNC:12476. UBE2D3.
    HPAi HPA003920.
    MIMi 602963. gene.
    neXtProti NX_P61077.
    PharmGKBi PA37126.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG063308.
    KOi K06689.
    OMAi SAGPCED.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi P61077.
    TreeFami TF101108.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_12034. Signaling by BMP.
    REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P61077.

    Miscellaneous databases

    ChiTaRSi UBE2D3. human.
    EvolutionaryTracei P61077.
    GeneWikii UBE2D3.
    GenomeRNAii 7323.
    NextBioi 28636.
    PROi P61077.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61077.
    Bgeei P61077.
    CleanExi HS_UBE2D3.
    Genevestigatori P61077.

    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 family of closely related human ubiquitin conjugating enzymes."
      Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.
      J. Biol. Chem. 270:30408-30414(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genome sequencing of the chromosome 4q region implicated in human hepatocellular carcinoma pathogenesis."
      Chang H.-M., Tsai S.-F.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Chondrocyte and Testis.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain and Placenta.
    8. "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-85.
    9. "CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein."
      Murata S., Minami Y., Minami M., Chiba T., Tanaka K.
      EMBO Rep. 2:1133-1138(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Mammalian Numb is a target protein of Mdm2, ubiquitin ligase."
      Yogosawa S., Miyauchi Y., Honda R., Tanaka H., Yasuda H.
      Biochem. Biophys. Res. Commun. 302:869-872(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53."
      Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.
      J. Biol. Chem. 279:36440-36444(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: FUNCTION.
    13. Cited for: FUNCTION.
    14. "A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites."
      Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R., Boulton S.J.
      EMBO J. 25:2178-2188(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA1, FUNCTION.
    15. Cited for: INTERACTION WITH DAPK3, FUNCTION.
    16. "PCNA is ubiquitinated by RNF8."
      Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.
      Cell Cycle 7:3399-3404(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation."
      Umebayashi K., Stenmark H., Yoshimori T.
      Mol. Biol. Cell 19:3454-3462(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    18. "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.
    19. "Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions."
      Kubori T., Hyakutake A., Nagai H.
      Mol. Microbiol. 67:1307-1319(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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.
    21. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
      Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
      J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBLC.
    22. "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.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids."
      Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.
      Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASN-77; ASP-87 AND ASP-117.
    25. "A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination."
      Brzovic P.S., Lissounov A., Christensen D.E., Hoyt D.W., Klevit R.E.
      Mol. Cell 21:873-880(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-147 IN COMPLEX WITH THE BRCA1/BARD1 RING-DOMAIN HETERODIMER, INTERACTION WITH BRCA1.
    26. "Crystal structure of UBCH5C."
      Nakanishi M., Teshima N., Mizushima T., Murata S., Tanaka K., Yamane T.
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-147, DISULFIDE BOND.
    27. "Crystal structure of the U-Box domain of human e4b ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme."
      Benirschke R., Thompson J.R., Mer G.
      Submitted (MAY-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (3.17 ANGSTROMS) OF 1-147 IN COMPLEX WITH U-BOX DOMAIN OF UBE4B.

    Entry informationi

    Entry nameiUB2D3_HUMAN
    AccessioniPrimary (citable) accession number: P61077
    Secondary accession number(s): A6NJ93
    , A6NJB1, A6NM99, P47986, Q6IB88, Q6NXS4, Q8N924
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3