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== Function ==
== Function ==


Ubiquitin, one of the most conserved proteins known. Ubiquitin is required for [[Adenosine triphosphate|ATP]]-dependent, non-[[lysosome|lysosomal]] intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to [[histone H2A]] in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein ([[UBB+1]]) has been noticed in patients with [[Alzheimer's disease]], [[Down syndrome]], other [[tauopathy|tauopathies]] (e.g. [[Pick's disease]]) and [[trinucleotide repeat disorder|polyglutamine disease]] (e.g. [[Huntington's disease]])<ref name="pmid14597671">{{cite journal | author = Fischer DF, De Vos RA, Van Dijk R, De Vrij FM, Proper EA, Sonnemans MA, Verhage MC, Sluijs JA, Hobo B, Zouambia M, Steur EN, Kamphorst W, Hol EM, Van Leeuwen FW | title = Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain | journal = FASEB J | volume = 17 | issue = 14 | pages = 2014–2024 | year = 2003 | month = Nov | pmid = 14597671| pmc = | doi =10.1096/fj.03-0205com }}</ref>.<ref>{{cite web | title = Entrez Gene: UBB ubiquitin B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314| accessdate = }}</ref>
Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for [[Adenosine triphosphate|ATP]]-dependent, non-[[lysosome|lysosomal]] intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to [[histone H2A]] in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein ([[UBB+1]]) has been noticed in patients with [[Alzheimer's disease]], [[Down syndrome]], other [[tauopathy|tauopathies]] (e.g. [[Pick's disease]]) and [[trinucleotide repeat disorder|polyglutamine disease]] (e.g. [[Huntington's disease]])<ref name="pmid14597671">{{cite journal | author = Fischer DF, De Vos RA, Van Dijk R, De Vrij FM, Proper EA, Sonnemans MA, Verhage MC, Sluijs JA, Hobo B, Zouambia M, Steur EN, Kamphorst W, Hol EM, Van Leeuwen FW | title = Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain | journal = FASEB J | volume = 17 | issue = 14 | pages = 2014–2024 | year = 2003 | month = Nov | pmid = 14597671| pmc = | doi =10.1096/fj.03-0205com }}</ref>.<ref>{{cite web | title = Entrez Gene: UBB ubiquitin B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314| accessdate = }}</ref>


==References==
==References==

Revision as of 19:04, 12 October 2012

Template:PBB Ubiquitin is a protein that in humans is encoded by the UBB gene.[1]

Function

Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein (UBB+1) has been noticed in patients with Alzheimer's disease, Down syndrome, other tauopathies (e.g. Pick's disease) and polyglutamine disease (e.g. Huntington's disease)[2].[3]

References

  1. ^ Webb GC, Baker RT, Fagan K, Board PG (1990). "Localization of the human UbB polyubiquitin gene to chromosome band 17p11.1-17p12". Am J Hum Genet. 46 (2): 308–15. PMC 1684968. PMID 2154095. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ Fischer DF, De Vos RA, Van Dijk R, De Vrij FM, Proper EA, Sonnemans MA, Verhage MC, Sluijs JA, Hobo B, Zouambia M, Steur EN, Kamphorst W, Hol EM, Van Leeuwen FW (2003). "Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain". FASEB J. 17 (14): 2014–2024. doi:10.1096/fj.03-0205com. PMID 14597671. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  3. ^ "Entrez Gene: UBB ubiquitin B".

Further reading

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