Ubiquitin B: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ubiquitin''' is a [[protein]] that in humans is encoded by the ''UBB'' [[gene]].<ref name="pmid2154095">{{cite journal |vauthors=Webb GC, Baker RT, Fagan K, Board PG | title = Localization of the human UbB polyubiquitin gene to chromosome band 17p11.1-17p12 | journal = Am J Hum Genet | volume = 46 | issue = 2 | pages = 308–15 |date=Mar 1990 | pmid = 2154095 | pmc = 1684968 | doi = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_UBB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aar.
| PDB = {{PDB2|1aar}}, {{PDB2|1cmx}}, {{PDB2|1d3z}}, {{PDB2|1f9j}}, {{PDB2|1fxt}}, {{PDB2|1g6j}}, {{PDB2|1gjz}}, {{PDB2|1nbf}}, {{PDB2|1ogw}}, {{PDB2|1otr}}, {{PDB2|1p3q}}, {{PDB2|1q0w}}, {{PDB2|1q5w}}, {{PDB2|1s1q}}, {{PDB2|1sif}}, {{PDB2|1tbe}}, {{PDB2|1ubi}}, {{PDB2|1ubq}}, {{PDB2|1ud7}}, {{PDB2|1uzx}}, {{PDB2|1v80}}, {{PDB2|1v81}}, {{PDB2|1wr1}}, {{PDB2|1wr6}}, {{PDB2|1wrd}}, {{PDB2|1xd3}}, {{PDB2|1xqq}}, {{PDB2|1yd8}}, {{PDB2|1yiw}}, {{PDB2|1yj1}}, {{PDB2|1yx5}}, {{PDB2|1yx6}}, {{PDB2|1zgu}}, {{PDB2|2ayo}}, {{PDB2|2bgf}}, {{PDB2|2c7m}}, {{PDB2|2c7n}}, {{PDB2|2d3g}}, {{PDB2|2den}}, {{PDB2|2dx5}}, {{PDB2|2fcm}}, {{PDB2|2fcn}}, {{PDB2|2fcq}}, {{PDB2|2fcs}}, {{PDB2|2fid}}, {{PDB2|2fif}}, {{PDB2|2fuh}}, {{PDB2|2g3q}}, {{PDB2|2g45}}, {{PDB2|2gbj}}, {{PDB2|2gbk}}, {{PDB2|2gbm}}, {{PDB2|2gbn}}, {{PDB2|2gbr}}, {{PDB2|2gmi}}, {{PDB2|2hd5}}, {{PDB2|2hth}}, {{PDB2|2ibi}}, {{PDB2|2j7q}}, {{PDB2|2nr2}}, {{PDB2|2o6v}}, {{PDB2|2oob}}
| Name = Ubiquitin B
| HGNCid = 12463
| Symbol = UBB
| AltSymbols =; FLJ25987; MGC8385
| OMIM = 191339
| ECnumber = 
| Homologene = 75104
| MGIid = 
| GeneAtlas_image1 = PBB_GE_UBB_200633_at_tn.png
| Function =  
| Component =
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7314
    | Hs_Ensembl = ENSG00000170315
    | Hs_RefseqProtein = NP_061828
    | Hs_RefseqmRNA = NM_018955
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 16225092
    | Hs_GenLoc_end = 16226779
    | Hs_Uniprot = P62988
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =
  }}
}}
'''Ubiquitin B''', also known as '''UBB''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 |vauthors=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 |date=Nov 2003 | pmid = 14597671| pmc = | doi =10.1096/fj.03-0205com  }}</ref><ref>{{cite web | title = Entrez Gene: UBB ubiquitin B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal 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 has been noticed in patients with Alzheimer's and Down syndrome.<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==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Conaway RC, Brower CS, Conaway JW |title=Emerging roles of ubiquitin in transcription regulation |journal=Science |volume=296 |issue= 5571 |pages= 1254–1258 |year= 2002 |pmid= 12016299 |doi= 10.1126/science.1067466 }}
| citations =
*{{cite journal  |vauthors=Murphey RK, Godenschwege TA |title=New roles for ubiquitin in the assembly and function of neuronal circuits |journal=Neuron |volume=36 |issue= 1 |pages= 5–8 |year= 2002 |pmid= 12367500 |doi=10.1016/S0896-6273(02)00943-1 }}
*{{cite journal  | author=Conaway RC, Brower CS, Conaway JW |title=Emerging roles of ubiquitin in transcription regulation. |journal=Science |volume=296 |issue= 5571 |pages= 1254-8 |year= 2002 |pmid= 12016299 |doi= 10.1126/science.1067466 }}
*{{cite journal  |vauthors=Mazzé FM, Degrève L |title=The role of viral and cellular proteins in the budding of human immunodeficiency virus |journal=Acta Virol. |volume=50 |issue= 2 |pages= 75–85 |year= 2006 |pmid= 16808324 |doi=  }}
*{{cite journal  | author=Murphey RK, Godenschwege TA |title=New roles for ubiquitin in the assembly and function of neuronal circuits. |journal=Neuron |volume=36 |issue= 1 |pages= 5-8 |year= 2002 |pmid= 12367500 |doi=  }}
*{{cite journal  |vauthors=Schlesinger DH, Goldstein G |title=Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man |journal=Nature |volume=255 |issue= 5507 |pages= 423–4 |year= 1975 |pmid= 1128706 |doi= 10.1038/255423a0 }}
*{{cite journal  | author=Mazzé FM, Degrève L |title=The role of viral and cellular proteins in the budding of human immunodeficiency virus. |journal=Acta Virol. |volume=50 |issue= 2 |pages= 75-85 |year= 2006 |pmid= 16808324 |doi=  }}
*{{cite journal  | author=Adams SM |title=Differential expression of translation-associated genes in benign and malignant human breast tumours |journal=Br. J. Cancer |volume=65 |issue= 1 |pages= 65–71 |year= 1992 |pmid= 1370760 |doi=  10.1038/bjc.1992.12| pmc=1977345 |name-list-format=vanc| author2=Sharp MG  | author3=Walker RA  | display-authors=3  | last4=Brammar  | first4=WJ  | last5=Varley  | first5=JM }}
*{{cite journal  | author=Schlesinger DH, Goldstein G |title=Hybrid troponin reconstituted from vertebrate and arthropod subunits. |journal=Nature |volume=255 |issue= 5507 |pages= 423-4 |year= 1975 |pmid= 124018 |doi= }}
*{{cite journal  | author=Pancré V |title=Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL) |journal=Eur. J. Immunol. |volume=21 |issue= 11 |pages= 2735–41 |year= 1991 |pmid= 1657614 |doi=10.1002/eji.1830211113 |name-list-format=vanc| author2=Pierce RJ | author3=Fournier F  | display-authors=3  | last4=Mehtali  | first4=Majid  | last5=Delanoye  | first5=Anne  | last6=Capron  | first6=André  | last7=Auriault  | first7=Claude }}
*{{cite journal  | author=Adams SM, Sharp MG, Walker RA, ''et al.'' |title=Differential expression of translation-associated genes in benign and malignant human breast tumours. |journal=Br. J. Cancer |volume=65 |issue= 1 |pages= 65-71 |year= 1992 |pmid= 1370760 |doi=  }}
*{{cite journal  |vauthors=Baker RT, Board PG |title=The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1035–1040 |year= 1991 |pmid= 1850507 |doi=10.1093/nar/19.5.1035  | pmc=333777  }}
*{{cite journal | author=Pancré V, Pierce RJ, Fournier F, ''et al.'' |title=Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL). |journal=Eur. J. Immunol. |volume=21 |issue= 11 |pages= 2735-41 |year= 1991 |pmid= 1657614 |doi=  }}
*{{cite journal  |vauthors=Fornace AJ, Alamo I, Hollander MC, Lamoreaux E |title=Ubiquitin mRNA is a major stress-induced transcript in mammalian cells |journal=Nucleic Acids Res. |volume=17 |issue= 3 |pages= 1215–1230 |year= 1989 |pmid= 2537950 |doi=10.1093/nar/17.3.1215  | pmc=331738 }}
*{{cite journal  | author=Baker RT, Board PG |title=The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes. |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1035-40 |year= 1991 |pmid= 1850507 |doi=  }}
*{{cite journal  | author=Lund PK |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609–13 |year= 1985 |pmid= 2581967 |doi=  |name-list-format=vanc| author2=Moats-Staats BM | author3=Simmons JG  | display-authors=3  | last4=Hoyt  | first4=E  | last5=d'Ercole  | first5=AJ  | last6=Martin  | first6=F  | last7=Van Wyk  | first7=JJ }}
*{{cite journal | author=Webb GC, Baker RT, Fagan K, Board PG |title=Localization of the human UbB polyubiquitin gene to chromosome band 17p11.1-17p12. |journal=Am. J. Hum. Genet. |volume=46 |issue= 2 |pages= 308-15 |year= 1990 |pmid= 2154095 |doi=  }}
*{{cite journal  |vauthors=Einspanier R, Sharma HS, Scheit KH |title=Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells |journal=Biochem. Biophys. Res. Commun. |volume=147 |issue= 2 |pages= 581–587 |year= 1987 |pmid= 2820408 |doi=10.1016/0006-291X(87)90970-3 }}
*{{cite journal  | author=Fornace AJ, Alamo I, Hollander MC, Lamoreaux E |title=Ubiquitin mRNA is a major stress-induced transcript in mammalian cells. |journal=Nucleic Acids Res. |volume=17 |issue= 3 |pages= 1215-30 |year= 1989 |pmid= 2537950 |doi= }}
*{{cite journal  | author=Wiborg O |title=The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences |journal=EMBO J. |volume=4 |issue= 3 |pages= 755–9 |year= 1985 |pmid= 2988935 |doi=  | pmc=554252 |name-list-format=vanc| author2=Pedersen MS  | author3=Wind A  | display-authors=3  | last4=Berglund  | first4=LE | last5=Marcker  | first5=KA  | last6=Vuust  | first6=J }}
*{{cite journal  | author=Lund PK, Moats-Staats BM, Simmons JG, ''et al.'' |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609-13 |year= 1985 |pmid= 2581967 |doi=  }}
*{{cite journal  |vauthors=Baker RT, Board PG |title=The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily |journal=Nucleic Acids Res. |volume=15 |issue= 2 |pages= 443–463 |year= 1987 |pmid= 3029682 |doi=10.1093/nar/15.2.443  | pmc=340445 }}
*{{cite journal  | author=Einspanier R, Sharma HS, Scheit KH |title=Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells. |journal=Biochem. Biophys. Res. Commun. |volume=147 |issue= 2 |pages= 581-7 |year= 1987 |pmid= 2820408 |doi=  }}
*{{cite journal  |vauthors=Vijay-Kumar S, Bugg CE, Cook WJ |title=Structure of ubiquitin refined at 1.8 A resolution |journal=J. Mol. Biol. |volume=194 |issue= 3 |pages= 531–544 |year= 1987 |pmid= 3041007 |doi=10.1016/0022-2836(87)90679-6 }}
*{{cite journal | author=Wiborg O, Pedersen MS, Wind A, ''et al.'' |title=The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. |journal=EMBO J. |volume=4 |issue= 3 |pages= 755-9 |year= 1985 |pmid= 2988935 |doi=  }}
*{{cite journal  | author=Busch H |title=Ubiquitination of proteins |journal=Meth. Enzymol. |volume=106 |issue= |pages= 238–262 |year= 1984 |pmid= 6092831 |doi=10.1016/0076-6879(84)06025-0 | chapter=[23] Ubiquitination of Proteins | series=Methods in Enzymology  | isbn=978-0-12-182006-0  }}
*{{cite journal  | author=Baker RT, Board PG |title=The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily. |journal=Nucleic Acids Res. |volume=15 |issue= 2 |pages= 443-63 |year= 1987 |pmid= 3029682 |doi=  }}
*{{cite journal |vauthors=Andersen MW, Ballal NR, Goldknopf IL, Busch H |title=Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24 |journal=Biochemistry |volume=20 |issue= 5 |pages= 1100–1104 |year= 1981 |pmid= 6261785 |doi=10.1021/bi00508a009  }}
*{{cite journal  | author=Vijay-Kumar S, Bugg CE, Cook WJ |title=Structure of ubiquitin refined at 1.8 A resolution. |journal=J. Mol. Biol. |volume=194 |issue= 3 |pages= 531-44 |year= 1987 |pmid= 3041007 |doi=  }}
*{{cite journal  |vauthors=Busch H, Goldknopf IL |title=Ubiquitin - protein conjugates |journal=Mol. Cell. Biochem. |volume=40 |issue= 3 |pages= 173–87 |year= 1982 |pmid= 6275256 |doi=  10.1007/bf00224611}}
*{{cite journal | author=Busch H |title=Ubiquitination of proteins. |journal=Meth. Enzymol. |volume=106 |issue=  |pages= 238-62 |year= 1984 |pmid= 6092831 |doi=  }}
*{{cite journal  |vauthors=Treier M, Staszewski LM, Bohmann D |title=Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain |journal=Cell |volume=78 |issue= 5 |pages= 787–798 |year= 1994 |pmid= 8087846 |doi=10.1016/S0092-8674(94)90502-9  }}
*{{cite journal  | author=Andersen MW, Ballal NR, Goldknopf IL, Busch H |title=Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24. |journal=Biochemistry |volume=20 |issue= 5 |pages= 1100-4 |year= 1981 |pmid= 6261785 |doi=  }}
*{{cite journal  |vauthors=Cook WJ, Jeffrey LC, Kasperek E, Pickart CM |title=Structure of tetraubiquitin shows how multiubiquitin chains can be formed |journal=J. Mol. Biol. |volume=236 |issue= 2 |pages= 601–609 |year= 1994 |pmid= 8107144 |doi= 10.1006/jmbi.1994.1169 }}
*{{cite journal  | author=Busch H, Goldknopf IL |title=Ubiquitin - protein conjugates. |journal=Mol. Cell. Biochem. |volume=40 |issue= 3 |pages= 173-87 |year= 1982 |pmid= 6275256 |doi=  }}
*{{cite journal  | author=Ramage R |title=Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin |journal=Biochem. J. |volume=299 |issue=  1|pages= 151–8 |year= 1994 |pmid= 8166633 |doi=  | pmc=1138034  |name-list-format=vanc| author2=Green J  | author3=Muir TW  | display-authors=3  | last4=Ogunjobi  | first4=OM  | last5=Love  | first5=S  | last6=Shaw  | first6=K  }}
*{{cite journal  | author=Treier M, Staszewski LM, Bohmann D |title=Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. |journal=Cell |volume=78 |issue= 5 |pages= 787-98 |year= 1994 |pmid= 8087846 |doi=  }}
*{{cite journal | author=Cook WJ, Jeffrey LC, Kasperek E, Pickart CM |title=Structure of tetraubiquitin shows how multiubiquitin chains can be formed. |journal=J. Mol. Biol. |volume=236 |issue= 2 |pages= 601-9 |year= 1994 |pmid= 8107144 |doi= 10.1006/jmbi.1994.1169 }}
*{{cite journal  | author=Ramage R, Green J, Muir TW, ''et al.'' |title=Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin. |journal=Biochem. J. |volume=299 ( Pt 1) |issue= |pages= 151-8 |year= 1994 |pmid= 8166633 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=7314}}
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{{gene-17-stub}}

Latest revision as of 10:28, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

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 (Mar 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.
  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 (Nov 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.
  3. ↑ "Entrez Gene: UBB ubiquitin B".

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=Ubiquitin_B&oldid=1418401"