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Index > Protein center > UBB(Gene name) > Human
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  • UBB (Gene name),
  • Polyubiquitin-B (Protein name ),  UBB_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    UBB;
    Protein name:
    Polyubiquitin-B;
    Alternative:

    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    N/A
    Function:
    Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
    Subcellular Location:
    Ubiquitin Cytoplasm Nucleus
    Protein Attributes:
    Sequence length:
    229
    Sequence:
    50:
    MQIFVKTLTG | KTITLEVEPS | DTIENVKAKI | QDKEGIPPDQ | QRLIFAGKQL | 
    100:
    EDGRTLSDYN | IQKESTLHLV | LRLRGGMQIF | VKTLTGKTIT | LEVEPSDTIE | 
    150:
    NVKAKIQDKE | GIPPDQQRLI | FAGKQLEDGR | TLSDYNIQKE | STLHLVLRLR | 
    200:
    GGMQIFVKTL | TGKTITLEVE | PSDTIENVKA | KIQDKEGIPP | DQQRLIFAGK | 
    229:
    QLEDGRTLSD | YNIQKESTLH | LVLRLRGGC
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    SMR:
    MIM:
    KEGG:
    UniGene:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Human Polyubiquitin-B
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    ELISA Kit for Human Polyubiquitin-B
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    ELISA Kit for Human Polyubiquitin-B
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    ELISA Kit for Human Polyubiquitin-B
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    CLIA Kit for Human Polyubiquitin-B
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    CLIA Kit for Human Polyubiquitin-B
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    Polyclonal Antibody for Human Polyubiquitin-B
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    P0164Rb-h
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    Polyclonal Antibody for Human Polyubiquitin-B
    Polyclonal Antibody for Human Polyubiquitin-B
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    Polyclonal Antibody for Human Polyubiquitin-B
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    Packing:
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    Monoclonal Antibody for Human Polyubiquitin-B
    Monoclonal Antibody for Human Polyubiquitin-B
    Monoclonal Antibody for Human Polyubiquitin-B
    Monoclonal Antibody for Human Polyubiquitin-B
    Monoclonal Antibody for Human Polyubiquitin-B
    Protein for Human Polyubiquitin-B
    Protein for Human Polyubiquitin-B
    Protein for Human Polyubiquitin-B
    Protein for Human Polyubiquitin-B
    Protein for Human Polyubiquitin-B

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    References
    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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
      tissue: Blood.
    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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
    3. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      tissue: Brain.
      tissue: Liver.
      tissue: Lung.
    4. 5.
      Lubec G. , Chen W.-Q. , Sun Y.
      Submitted (2008-12) to the UniProtKB
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72;IDENTIFICATION BY MASS SPECTROMETRY
      tissue: Fetal brain cortex.
    5. 6.
      "Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man."
      Schlesinger D.H. , Goldstein G.
      Nature255:423-424(1975) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 1-74
    6. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54;UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48;IDENTIFICATION BY MASS SPECTROMETRY
    7. 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. Cell21:737-748(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63;IDENTIFICATION BY MASS SPECTROMETRY
    8. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: UBIQUITINATION AT LYS-27
    9. 10.
      "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
      Vasilescu J. , Zweitzig D.R. , Denis N.J. , Smith J.C. , Ethier M. , Haines D.S. , Figeys D.
      J. Proteome Res.6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48
      tissue: Lung adenocarcinoma.
    10. 11.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: UBIQUITINATION AT LYS-63;MUTAGENESIS OF LYS-48 AND LYS-63
    11. 12.
      "The emerging complexity of protein ubiquitination."
      Komander D.
      Biochem. Soc. Trans.37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: REVIEW;FUNCTION
    12. 13.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: CLEAVAGE BY UCHL3 (VARIANT UBB(+1))
    13. 14.
      "Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients."
      van Leeuwen F.W. , de Kleijn D.P. , van den Hurk H.H. , Neubauer A. , Sonnemans M.A. , Sluijs J.A. , Koycu S. , Ramdjielal R.D. , Salehi A. , Martens G.J. , Grosveld F.G. , Peter J. , Burbach H. , Hol E.M.
      Science279:242-247(1998) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION OF VARIANT UBB(+1)
    14. 15.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: TISSUE SPECIFICITY (VARIANT UBB(+1))
    15. 16.
      "Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65."
      Kazlauskaite A. , Kondapalli C. , Gourlay R. , Campbell D.G. , Ritorto M.S. , Hofmann K. , Alessi D.R. , Knebel A. , Trost M. , Muqit M.M.
      Biochem. J.460:127-139(2014) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT SER-65;MUTAGENESIS OF SER-65
    16. 17.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT SER-65;MUTAGENESIS OF SER-65
    17. 18.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT SER-65;MUTAGENESIS OF SER-65
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