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1 to 25 of 960  Show
  1. 1
    "The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily."
    Baker R.T., Board P.G.
    Nucleic Acids Res. 15:443-463(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Category: Sequences.
    Tissue: Blood.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "Lineage-specific homogenization of the polyubiquitin gene among human and great apes."
    Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.
    J. Mol. Evol. 57:737-744(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 7 other entries.

  3. 3
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4666 other entries.

  4. 4
    "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].
    Category: Sequences.
    Tissue: Brain, Liver and Lung.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50450 other entries.

  5. 5
    Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man."
    Schlesinger D.H., Goldstein G.
    Nature 255:423-424(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-74.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  7. 7
    "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."
    Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.
    J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 and mapped to 9 other entries.

  8. 8
    "Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
    Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
    Mol. Cell 21:737-748(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: Function, PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 other entries.

  9. 9
    "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis."
    Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.
    J. Biol. Chem. 279:53533-53543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-27.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 and mapped to 5 other entries.

  10. 10
    "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-63, MUTAGENESIS OF LYS-48 AND LYS-63.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 8 and mapped to 17 other entries.

  11. 11
    "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 7 other entries.

  12. 12
    "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)."
    Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.
    FEBS Lett. 585:2568-2574(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY UCHL3 (VARIANT UBB(+1)).
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 and mapped to 6 other entries.

  13. 13
    Cited for: IDENTIFICATION OF VARIANT UBB(+1).
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  14. 14
    "Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain."
    Fischer D.F., De Vos R.A., Van Dijk R., De Vrij F.M., Proper E.A., Sonnemans M.A., Verhage M.C., Sluijs J.A., Hobo B., Zouambia M., Steur E.N., Kamphorst W., Hol E.M., Van Leeuwen F.W.
    FASEB J. 17:2014-2024(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY (VARIANT UBB(+1)).
    Category: Expression, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  15. 15
    Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5 and mapped to 21 other entries.

  16. 16
    "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity."
    Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A., Banerjee S., Youle R.J.
    J. Cell Biol. 205:143-153(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5 and mapped to 21 other entries.

  17. 17
    Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 and mapped to 26 other entries.

  18. 18
    "Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis."
    Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N., Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.
    EMBO J. 34:307-325(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-65.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 other entries.

  19. 19
    Cited for: ADP-RIBOSYLATION AT GLY-76, MUTAGENESIS OF HIS-68; ARG-72; ARG-74 AND GLY-76.
    Category: Function, Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5 and mapped to 4 other entries.

  20. 20
    "IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2."
    Suzuki H., Chiba T., Kobayashi M., Takeuchi M., Suzuki T., Ichiyama A., Ikenoue T., Omata M., Furuichi K., Tanaka K.
    Biochem. Biophys. Res. Commun. 256:127-132(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939214, Reactome:R-HSA-939230, Reactome:R-HSA-939213.

    This publication is cited by 1 and mapped to 11 other entries.

  21. 21
    "Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP."
    Kroll M., Margottin F., Kohl A., Renard P., Durand H., Concordet J.P., Bachelerie F., Arenzana-Seisdedos F., Benarous R.
    J. Biol. Chem. 274:7941-7945(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939214, Reactome:R-HSA-939230, Reactome:R-HSA-939213.

    This publication is mapped to 55 other entries.

  22. 22
    "Control of mRNA decay by heat shock-ubiquitin-proteasome pathway."
    Laroia G., Cuesta R., Brewer G., Schneider R.J.
    Science 284:499-502(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939214, Reactome:R-HSA-939230, Reactome:R-HSA-939213.

    This publication is mapped to 54 other entries.

  23. 23
    "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
    Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
    Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939214, Reactome:R-HSA-939230, Reactome:R-HSA-939213.

    This publication is cited by 2 and mapped to 12 other entries.

  24. 24
    "HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin."
    Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z.
    Oncogene 18:2039-2046(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939214, Reactome:R-HSA-939230, Reactome:R-HSA-939213.

    This publication is mapped to 12 other entries.

  25. 25
    "Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2."
    Maki C.G.
    J. Biol. Chem. 274:16531-16535(1999) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: Pathway.
    Source: Reactome:R-HSA-939870, Reactome:R-HSA-939854, Reactome:R-HSA-939847.

    This publication is mapped to 7 other entries.

1 to 25 of 960  Show
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