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)

P62837

- UB2D2_HUMAN

UniProt

P62837 - UB2D2_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 D2

Gene

UBE2D2

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-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.9 Publications

    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: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. cellular response to hypoxia Source: Reactome
    3. innate immune response Source: Reactome
    4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    5. protein K48-linked ubiquitination Source: UniProtKB
    6. protein polyubiquitination Source: BHF-UCL
    7. protein ubiquitination Source: BHF-UCL
    8. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    9. toll-like receptor 3 signaling pathway Source: Reactome
    10. toll-like receptor 4 signaling pathway Source: Reactome
    11. toll-like receptor signaling pathway Source: Reactome
    12. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    13. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    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.
    SignaLinkiP62837.
    UniPathwayiUPA00143.

    Protein family/group databases

    TCDBi3.A.20.1.1. the peroxisomal protein importer (ppi) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 D2 (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein D2
    Ubiquitin-conjugating enzyme E2(17)KB 2
    Ubiquitin-conjugating enzyme E2-17 kDa 2
    Ubiquitin-protein ligase D2
    p53-regulated ubiquitin-conjugating enzyme 1
    Gene namesi
    Name:UBE2D2
    Synonyms:PUBC1, UBC4, UBC5B, UBCH4, UBCH5B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:12475. UBE2D2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. protein complex Source: MGI
    4. ubiquitin ligase complex Source: BHF-UCL

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631K → A or E: Strongly reduced interaction with CNTO4. 1 Publication
    Mutagenesisi85 – 851C → A: Catalytically inactive. Loss of ability to promote FBXW2-mediated GCM1 ubiquitination. Inhibition of TNF-alpha-induced degradation of NFKBIA. 3 Publications

    Organism-specific databases

    PharmGKBiPA37125.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D2PRO_0000082462Add
    BLAST

    Proteomic databases

    PaxDbiP62837.
    PRIDEiP62837.

    PTM databases

    PhosphoSiteiP62837.

    Expressioni

    Gene expression databases

    ArrayExpressiP62837.
    BgeeiP62837.
    CleanExiHS_UBE2D2.
    GenevestigatoriP62837.

    Organism-specific databases

    HPAiHPA003920.

    Interactioni

    Subunit structurei

    Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM4O151512EBI-347677,EBI-398437
    OTUB1Q96FW15EBI-347677,EBI-1058491
    RNF11Q9Y3C55EBI-347677,EBI-396669
    RNF43Q68DV72EBI-347677,EBI-1647060
    RNF5Q999423EBI-347677,EBI-348482
    TRAF6Q9Y4K32EBI-347677,EBI-359276
    XIAPP981702EBI-347677,EBI-517127
    ZNRF1Q8ND254EBI-347677,EBI-2129250

    Protein-protein interaction databases

    BioGridi113170. 202 interactions.
    DIPiDIP-29267N.
    IntActiP62837. 96 interactions.
    MINTiMINT-1035011.
    STRINGi9606.ENSP00000381717.

    Structurei

    Secondary structure

    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1515
    Beta strandi19 – 2810
    Beta strandi32 – 387
    Beta strandi41 – 433
    Turni44 – 474
    Beta strandi49 – 557
    Turni58 – 614
    Beta strandi66 – 716
    Beta strandi76 – 783
    Beta strandi82 – 843
    Helixi87 – 893
    Turni90 – 923
    Helixi99 – 11113
    Beta strandi115 – 1173
    Helixi121 – 1299
    Helixi131 – 14515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UR6NMR-A1-147[»]
    1W4UNMR-A1-147[»]
    2C4OX-ray1.94A/B/C/D1-147[»]
    2CLWX-ray1.94A/B/C/D1-147[»]
    2ESKX-ray1.36A1-147[»]
    2ESOX-ray1.50A1-147[»]
    2ESPX-ray1.52A1-147[»]
    2ESQX-ray1.44A1-147[»]
    3A33X-ray2.20A1-147[»]
    3JVZX-ray3.30A/B2-147[»]
    3JW0X-ray3.10A/B2-147[»]
    3L1YX-ray1.60A1-147[»]
    3TGDX-ray1.80A1-147[»]
    3ZNIX-ray2.21C/G/K/O2-147[»]
    4A49X-ray2.21B1-147[»]
    4A4BX-ray2.79C1-147[»]
    4A4CX-ray2.70C1-147[»]
    4AUQX-ray2.18A/D1-147[»]
    4DDGX-ray3.30A/B/C/J/K/L1-147[»]
    4LDTX-ray1.90C1-147[»]
    ProteinModelPortaliP62837.
    SMRiP62837. Positions 1-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62837.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    KOiK06689.
    OMAiNDLGRDP.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiP62837.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62837-1) [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

    MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF    50
    FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS 100
    KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM 147
    Length:147
    Mass (Da):16,735
    Last modified:August 16, 2004 - v1
    Checksum:iC942BE7853CBC355
    GO
    Isoform 2 (identifier: P62837-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:118
    Mass (Da):13,635
    Checksum:iCC29567199FE8084
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281K → Q in AAC41750. (PubMed:7724550)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_045180Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39317 mRNA. Translation: AAA91460.1.
    L40146 Genomic DNA. Translation: AAC41750.1.
    AY651263 mRNA. Translation: AAX35690.1.
    AF317220 mRNA. Translation: AAK93958.1.
    AK001311 mRNA. Translation: BAG50891.1.
    AK001428 mRNA. Translation: BAG50911.1.
    AC010378 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62095.1.
    CH471062 Genomic DNA. Translation: EAW62096.1.
    CH471062 Genomic DNA. Translation: EAW62097.1.
    BC033349 mRNA. Translation: AAH33349.1.
    CCDSiCCDS43369.1. [P62837-1]
    CCDS47275.1. [P62837-2]
    PIRiI59365.
    RefSeqiNP_003330.1. NM_003339.2. [P62837-1]
    NP_862821.1. NM_181838.1. [P62837-2]
    UniGeneiHs.108332.

    Genome annotation databases

    EnsembliENST00000253815; ENSP00000253815; ENSG00000131508. [P62837-2]
    ENST00000398733; ENSP00000381717; ENSG00000131508. [P62837-1]
    ENST00000398734; ENSP00000381718; ENSG00000131508. [P62837-1]
    ENST00000505548; ENSP00000424941; ENSG00000131508. [P62837-2]
    ENST00000511725; ENSP00000429613; ENSG00000131508. [P62837-2]
    GeneIDi7322.
    KEGGihsa:7322.
    UCSCiuc003leq.3. human. [P62837-1]

    Polymorphism databases

    DMDMi51338685.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39317 mRNA. Translation: AAA91460.1 .
    L40146 Genomic DNA. Translation: AAC41750.1 .
    AY651263 mRNA. Translation: AAX35690.1 .
    AF317220 mRNA. Translation: AAK93958.1 .
    AK001311 mRNA. Translation: BAG50891.1 .
    AK001428 mRNA. Translation: BAG50911.1 .
    AC010378 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62095.1 .
    CH471062 Genomic DNA. Translation: EAW62096.1 .
    CH471062 Genomic DNA. Translation: EAW62097.1 .
    BC033349 mRNA. Translation: AAH33349.1 .
    CCDSi CCDS43369.1. [P62837-1 ]
    CCDS47275.1. [P62837-2 ]
    PIRi I59365.
    RefSeqi NP_003330.1. NM_003339.2. [P62837-1 ]
    NP_862821.1. NM_181838.1. [P62837-2 ]
    UniGenei Hs.108332.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UR6 NMR - A 1-147 [» ]
    1W4U NMR - A 1-147 [» ]
    2C4O X-ray 1.94 A/B/C/D 1-147 [» ]
    2CLW X-ray 1.94 A/B/C/D 1-147 [» ]
    2ESK X-ray 1.36 A 1-147 [» ]
    2ESO X-ray 1.50 A 1-147 [» ]
    2ESP X-ray 1.52 A 1-147 [» ]
    2ESQ X-ray 1.44 A 1-147 [» ]
    3A33 X-ray 2.20 A 1-147 [» ]
    3JVZ X-ray 3.30 A/B 2-147 [» ]
    3JW0 X-ray 3.10 A/B 2-147 [» ]
    3L1Y X-ray 1.60 A 1-147 [» ]
    3TGD X-ray 1.80 A 1-147 [» ]
    3ZNI X-ray 2.21 C/G/K/O 2-147 [» ]
    4A49 X-ray 2.21 B 1-147 [» ]
    4A4B X-ray 2.79 C 1-147 [» ]
    4A4C X-ray 2.70 C 1-147 [» ]
    4AUQ X-ray 2.18 A/D 1-147 [» ]
    4DDG X-ray 3.30 A/B/C/J/K/L 1-147 [» ]
    4LDT X-ray 1.90 C 1-147 [» ]
    ProteinModelPortali P62837.
    SMRi P62837. Positions 1-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113170. 202 interactions.
    DIPi DIP-29267N.
    IntActi P62837. 96 interactions.
    MINTi MINT-1035011.
    STRINGi 9606.ENSP00000381717.

    Protein family/group databases

    TCDBi 3.A.20.1.1. the peroxisomal protein importer (ppi) family.

    PTM databases

    PhosphoSitei P62837.

    Polymorphism databases

    DMDMi 51338685.

    Proteomic databases

    PaxDbi P62837.
    PRIDEi P62837.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253815 ; ENSP00000253815 ; ENSG00000131508 . [P62837-2 ]
    ENST00000398733 ; ENSP00000381717 ; ENSG00000131508 . [P62837-1 ]
    ENST00000398734 ; ENSP00000381718 ; ENSG00000131508 . [P62837-1 ]
    ENST00000505548 ; ENSP00000424941 ; ENSG00000131508 . [P62837-2 ]
    ENST00000511725 ; ENSP00000429613 ; ENSG00000131508 . [P62837-2 ]
    GeneIDi 7322.
    KEGGi hsa:7322.
    UCSCi uc003leq.3. human. [P62837-1 ]

    Organism-specific databases

    CTDi 7322.
    GeneCardsi GC05P138920.
    H-InvDB HIX0019025.
    HIX0028451.
    HGNCi HGNC:12475. UBE2D2.
    HPAi HPA003920.
    MIMi 602962. gene.
    neXtProti NX_P62837.
    PharmGKBi PA37125.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    KOi K06689.
    OMAi NDLGRDP.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi P62837.
    TreeFami TF101108.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    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 P62837.

    Miscellaneous databases

    EvolutionaryTracei P62837.
    GeneWikii UBE2D2.
    GenomeRNAii 7322.
    NextBioi 28630.
    PROi P62837.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62837.
    Bgeei P62837.
    CleanExi HS_UBE2D2.
    Genevestigatori P62837.

    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).
      Tissue: Peripheral blood lymphocyte.
    2. "Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)."
      Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., Theodoras A., Pagano M., Draetta G.
      Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
      Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
      Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "Cloning and identification of a p53-regulated ubiquitin-conjugating enzyme, PUBC1."
      Yin Y.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "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] (ISOFORM 1).
      Tissue: Teratocarcinoma.
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Testis.
    9. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 73-90, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    10. "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.
    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. "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain."
      Yu P., Chen Y., Tagle D.A., Cai T.
      Genomics 79:869-874(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PJA1 AND PJA2.
    13. Cited for: FUNCTION.
    14. "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair."
      Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R., Timmers H.T.
      J. Mol. Biol. 337:157-165(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNOT4, MUTAGENESIS OF LYS-63.
    15. "Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology."
      Windheim M., Peggie M., Cohen P.
      Biochem. J. 409:723-729(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation."
      Chiang M.H., Chen L.F., Chen H.
      Biol. Reprod. 79:914-920(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-85.
    17. "Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor."
      Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E.
      J. Biol. Chem. 283:14190-14197(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3."
      Zeng W., Xu M., Liu S., Sun L., Chen Z.J.
      Mol. Cell 36:315-325(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    19. "Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity."
      Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M., Chen Z.J.
      Cell 141:315-330(2010) [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: FUNCTION, INTERACTION WITH CBLC, MUTAGENESIS OF CYS-85.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Solution structure of the ubiquitin-conjugating enzyme UbcH5B."
      Houben K., Dominguez C., van Schaik F.M., Timmers H.T., Bonvin A.M., Boelens R.
      J. Mol. Biol. 344:513-526(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    24. "Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates."
      Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M., Kurimoto E., Tanaka K., Wakatsuki S., Kato K.
      Structure 18:138-147(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

    Entry informationi

    Entry nameiUB2D2_HUMAN
    AccessioniPrimary (citable) accession number: P62837
    Secondary accession number(s): D3DQC9
    , P51669, Q3MN78, Q96RP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 124 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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