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P51668

- UB2D1_HUMAN

UniProt

P51668 - UB2D1_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 D1

Gene

UBE2D1

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 auto-ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.5 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. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. BMP signaling pathway Source: Reactome
    3. cellular response to hypoxia Source: Reactome
    4. gene expression Source: Reactome
    5. innate immune response Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. mitotic spindle assembly checkpoint 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 ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. positive regulation of protein ubiquitination Source: UniProtKB
    12. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    13. protein K48-linked ubiquitination Source: UniProtKB
    14. protein polyubiquitination Source: UniProtKB
    15. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    16. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    17. toll-like receptor 3 signaling pathway Source: Reactome
    18. toll-like receptor 4 signaling pathway Source: Reactome
    19. toll-like receptor signaling pathway Source: Reactome
    20. transcription, DNA-templated Source: Reactome
    21. transcription initiation from RNA polymerase II promoter Source: Reactome
    22. transforming growth factor beta receptor signaling pathway Source: Reactome
    23. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    24. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    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_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    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_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP51668.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 D1 (EC:6.3.2.19)
    Alternative name(s):
    Stimulator of Fe transport
    Short name:
    SFT
    UBC4/5 homolog
    UbcH5
    Ubiquitin carrier protein D1
    Ubiquitin-conjugating enzyme E2(17)KB 1
    Ubiquitin-conjugating enzyme E2-17 kDa 1
    Ubiquitin-protein ligase D1
    Gene namesi
    Name:UBE2D1
    Synonyms:SFT, UBC5A, UBCH5, UBCH5A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:12474. UBE2D1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37124.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 147147Ubiquitin-conjugating enzyme E2 D1PRO_0000082460Add
    BLAST

    Proteomic databases

    MaxQBiP51668.
    PaxDbiP51668.
    PRIDEiP51668.

    PTM databases

    PhosphoSiteiP51668.

    Expressioni

    Tissue specificityi

    Ubiquitous. Up-regulated in livers of iron-overloaded patients with hereditary hemochromatosis.2 Publications

    Gene expression databases

    BgeeiP51668.
    CleanExiHS_UBE2D1.
    GenevestigatoriP51668.

    Organism-specific databases

    HPAiHPA003920.

    Interactioni

    Subunit structurei

    Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with RNF11.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OTUB1Q96FW14EBI-743540,EBI-1058491
    RNF11Q9Y3C54EBI-743540,EBI-396669
    RNF126Q9BV683EBI-743540,EBI-357322
    TRAF6Q9Y4K32EBI-743540,EBI-359276
    TRIM39Q9HCM93EBI-743540,EBI-739510
    XIAPP981703EBI-743540,EBI-517127
    ZNRF1Q8ND254EBI-743540,EBI-2129250

    Protein-protein interaction databases

    BioGridi113169. 250 interactions.
    DIPiDIP-44088N.
    IntActiP51668. 98 interactions.
    MINTiMINT-1433717.
    STRINGi9606.ENSP00000363019.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Beta strandi21 – 255
    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
    2C4PX-ray2.35A/B1-147[»]
    2YHOX-ray2.10B/D/F/H1-147[»]
    3OJ4X-ray3.40A/D1-147[»]
    3PTFX-ray2.70A/B1-147[»]
    4AP4X-ray2.21B/E1-147[»]
    ProteinModelPortaliP51668.
    SMRiP51668. Positions 1-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51668.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiP51668.
    KOiK06689.
    OMAiWQATISG.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiP51668.
    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]

    Sequencei

    Sequence statusi: Complete.

    P51668-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF    50
    FLTVHFPTDY PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS 100
    KVLLSICSLL CDPNPDDPLV PDIAQIYKSD KEKYNRHARE WTQKYAM 147
    Length:147
    Mass (Da):16,602
    Last modified:October 1, 1996 - v1
    Checksum:i2E96FD0179EE119D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78140 mRNA. Translation: CAA55019.1.
    AF257220 mRNA. Translation: AAM81086.1.
    AJ272367 mRNA. Translation: CAC82177.1.
    AK291901 mRNA. Translation: BAF84590.1.
    AJ293565 Genomic DNA. Translation: CAC82097.1.
    BT007041 mRNA. Translation: AAP35690.1.
    AC016396 Genomic DNA. No translation available.
    AC023170 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54169.1.
    BC005980 mRNA. Translation: AAH05980.1.
    BC015997 mRNA. Translation: AAH15997.1.
    AF020761 mRNA. No translation available.
    CCDSiCCDS7252.1.
    PIRiI39202.
    RefSeqiNP_003329.1. NM_003338.4.
    UniGeneiHs.129683.

    Genome annotation databases

    EnsembliENST00000373910; ENSP00000363019; ENSG00000072401.
    GeneIDi7321.
    KEGGihsa:7321.
    UCSCiuc001jke.2. human.

    Polymorphism databases

    DMDMi1717848.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78140 mRNA. Translation: CAA55019.1 .
    AF257220 mRNA. Translation: AAM81086.1 .
    AJ272367 mRNA. Translation: CAC82177.1 .
    AK291901 mRNA. Translation: BAF84590.1 .
    AJ293565 Genomic DNA. Translation: CAC82097.1 .
    BT007041 mRNA. Translation: AAP35690.1 .
    AC016396 Genomic DNA. No translation available.
    AC023170 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54169.1 .
    BC005980 mRNA. Translation: AAH05980.1 .
    BC015997 mRNA. Translation: AAH15997.1 .
    AF020761 mRNA. No translation available.
    CCDSi CCDS7252.1.
    PIRi I39202.
    RefSeqi NP_003329.1. NM_003338.4.
    UniGenei Hs.129683.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C4P X-ray 2.35 A/B 1-147 [» ]
    2YHO X-ray 2.10 B/D/F/H 1-147 [» ]
    3OJ4 X-ray 3.40 A/D 1-147 [» ]
    3PTF X-ray 2.70 A/B 1-147 [» ]
    4AP4 X-ray 2.21 B/E 1-147 [» ]
    ProteinModelPortali P51668.
    SMRi P51668. Positions 1-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113169. 250 interactions.
    DIPi DIP-44088N.
    IntActi P51668. 98 interactions.
    MINTi MINT-1433717.
    STRINGi 9606.ENSP00000363019.

    PTM databases

    PhosphoSitei P51668.

    Polymorphism databases

    DMDMi 1717848.

    Proteomic databases

    MaxQBi P51668.
    PaxDbi P51668.
    PRIDEi P51668.

    Protocols and materials databases

    DNASUi 7321.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373910 ; ENSP00000363019 ; ENSG00000072401 .
    GeneIDi 7321.
    KEGGi hsa:7321.
    UCSCi uc001jke.2. human.

    Organism-specific databases

    CTDi 7321.
    GeneCardsi GC10P060094.
    HGNCi HGNC:12474. UBE2D1.
    HPAi HPA003920.
    MIMi 602961. gene.
    neXtProti NX_P51668.
    PharmGKBi PA37124.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi P51668.
    KOi K06689.
    OMAi WQATISG.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi P51668.
    TreeFami TF101108.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    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_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    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_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P51668.

    Miscellaneous databases

    EvolutionaryTracei P51668.
    GeneWikii UBE2D1.
    GenomeRNAii 7321.
    NextBioi 28626.
    PROi P51668.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51668.
    CleanExi HS_UBE2D1.
    Genevestigatori P51668.

    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 human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53."
      Scheffner M., Huibregtse J.M., Howley P.M.
      Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis."
      Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K., Veltkamp C., Stremmel W.
      Blood 101:3288-3293(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    3. "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].
    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: Skeletal muscle.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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].
      Tissue: Bone marrow and Skin.
    8. "Functional expression cloning and characterization of SFT, a stimulator of Fe transport."
      Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.
      J. Cell Biol. 139:895-905(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, TISSUE SPECIFICITY.
    9. Erratum
      Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.
      J. Cell Biol. 147:205-205(1999)
    10. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
      Matsuzawa S., Reed J.C.
      Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
    11. "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase."
      Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.
      Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF11.
    12. "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.
    13. "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide."
      Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.
      Exp. Cell Res. 314:3605-3613(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "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.
    15. "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases."
      Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.
      Arch. Biochem. Biophys. 483:66-74(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "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: FUNCTION.
    17. "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.
    18. "The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor."
      Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J., Tontonoz P., Schwabe J.W.
      Genes Dev. 25:1262-1274(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MYLIP.

    Entry informationi

    Entry nameiUB2D1_HUMAN
    AccessioniPrimary (citable) accession number: P51668
    Secondary accession number(s): A6NLF6, A8K786
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 140 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

    Caution

    PubMed:9362508 cloned and sequenced SFT which consisted of UBE2D1 last coding exon along with intronic sequences on the 5'-end of this exon. A function in iron transport has been described.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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