Ubiquitin B

Ubiquitin B
PDB rendering based on 1aar.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2KHW​, 2MBB​, 2MRO​, 2MSG​, 4UEL​, 4UF6​, 4WLR​, 4WUR​
Identifiers
Symbols	UBB ; RPS27A; UBA52; UBC
External IDs	OMIM: 191339 HomoloGene: 75104 GeneCards: UBB Gene
Gene ontology Molecular function • protein binding Cellular component • extracellular space • nucleus • nucleoplasm • mitochondrion • cytosol • plasma membrane • endosome membrane • endocytic vesicle membrane • neuron projection • neuronal cell body • extracellular exosome Biological process • G1/S transition of mitotic cell cycle • G2/M transition of mitotic cell cycle • negative regulation of transcription from RNA polymerase II promoter • activation of MAPK activity • protein polyubiquitination • mitotic cell cycle • stimulatory C-type lectin receptor signaling pathway • toll-like receptor signaling pathway • antigen processing and presentation of peptide antigen via MHC class I • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • carbohydrate metabolic process • glycogen biosynthetic process • glucose metabolic process • DNA repair • transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • apoptotic process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • epidermal growth factor receptor signaling pathway • transforming growth factor beta receptor signaling pathway • Notch signaling pathway • Notch receptor processing • I-kappaB kinase/NF-kappaB signaling • JNK cascade • circadian rhythm • fibroblast growth factor receptor signaling pathway • gene expression • regulation of necrotic cell death • programmed cell death • viral process • endosomal transport • viral life cycle • virion assembly • viral protein processing • cytokine-mediated signaling pathway • translesion synthesis • negative regulation of transforming growth factor beta receptor signaling pathway • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • regulation of protein ubiquitination • regulation of type I interferon production • negative regulation of type I interferon production • positive regulation of type I interferon production • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • ion transmembrane transport • TRIF-dependent toll-like receptor signaling pathway • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • Fc-epsilon receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • negative regulation of epidermal growth factor receptor signaling pathway • error-prone translesion synthesis • antigen processing and presentation of exogenous peptide antigen via MHC class I • DNA damage response, detection of DNA damage • regulation of apoptotic process • positive regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • small molecule metabolic process • innate immune response • positive regulation of transcription from RNA polymerase II promoter • mitochondrion transport along microtubule • neurotrophin TRK receptor signaling pathway • neuron projection morphogenesis • T cell receptor signaling pathway • positive regulation of NF-kappaB transcription factor activity • stress-activated MAPK cascade • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • regulation of mitochondrial membrane potential • transmembrane transport • membrane organization • regulation of proteasomal protein catabolic process • regulation of transcription from RNA polymerase II promoter in response to hypoxia • necroptotic process • nucleotide-binding oligomerization domain containing signaling pathway • error-free translesion synthesis • cellular response to hypoxia • intracellular transport of virus • negative regulation of canonical Wnt signaling pathway • positive regulation of canonical Wnt signaling pathway • apoptotic signaling pathway • programmed necrotic cell death • regulation of neuron death • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7314	n/a
Ensembl	ENSG00000170315	n/a
UniProt	P0CG47	n/a
RefSeq (mRNA)	NM_001281716	n/a
RefSeq (protein)	NP_001268645	n/a
Location (UCSC)	Chr 17: 16.38 – 16.38 Mb	n/a
PubMed search		n/a

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

• Conaway RC, Brower CS, Conaway JW (2002). "Emerging roles of ubiquitin in transcription regulation". Science 296 (5571): 1254–1258. doi:10.1126/science.1067466. PMID 12016299.
• Murphey RK, Godenschwege TA (2002). "New roles for ubiquitin in the assembly and function of neuronal circuits". Neuron 36 (1): 5–8. doi:10.1016/S0896-6273(02)00943-1. PMID 12367500.
• Mazzé FM, Degrève L (2006). "The role of viral and cellular proteins in the budding of human immunodeficiency virus". Acta Virol. 50 (2): 75–85. PMID 16808324.
• Schlesinger DH, Goldstein G (1975). "Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man". Nature 255 (5507): 423–4. doi:10.1038/255423a0. PMID 1128706.
• Adams SM, Sharp MG, Walker RA, et al. (1992). "Differential expression of translation-associated genes in benign and malignant human breast tumours". Br. J. Cancer 65 (1): 65–71. doi:10.1038/bjc.1992.12. PMC 1977345. PMID 1370760.
• Pancré V, Pierce RJ, Fournier F, et al. (1991). "Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL)". Eur. J. Immunol. 21 (11): 2735–41. doi:10.1002/eji.1830211113. PMID 1657614.
• Baker RT, Board PG (1991). "The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes". Nucleic Acids Res. 19 (5): 1035–1040. doi:10.1093/nar/19.5.1035. PMC 333777. PMID 1850507.
• Fornace AJ, Alamo I, Hollander MC, Lamoreaux E (1989). "Ubiquitin mRNA is a major stress-induced transcript in mammalian cells". Nucleic Acids Res. 17 (3): 1215–1230. doi:10.1093/nar/17.3.1215. PMC 331738. PMID 2537950.
• Lund PK, Moats-Staats BM, Simmons JG, et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". J. Biol. Chem. 260 (12): 7609–13. PMID 2581967.
• Einspanier R, Sharma HS, Scheit KH (1987). "Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells". Biochem. Biophys. Res. Commun. 147 (2): 581–587. doi:10.1016/0006-291X(87)90970-3. PMID 2820408.
• Wiborg O, Pedersen MS, Wind A, et al. (1985). "The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences". EMBO J. 4 (3): 755–9. PMC 554252. PMID 2988935.
• Baker RT, Board PG (1987). "The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily". Nucleic Acids Res. 15 (2): 443–463. doi:10.1093/nar/15.2.443. PMC 340445. PMID 3029682.
• Vijay-Kumar S, Bugg CE, Cook WJ (1987). "Structure of ubiquitin refined at 1.8 A resolution". J. Mol. Biol. 194 (3): 531–544. doi:10.1016/0022-2836(87)90679-6. PMID 3041007.
• Busch H (1984). "Ubiquitination of proteins". Meth. Enzymol. Methods in Enzymology 106: 238–262. doi:10.1016/0076-6879(84)06025-0. ISBN 978-0-12-182006-0. PMID 6092831. |chapter= ignored (help)
• Andersen MW, Ballal NR, Goldknopf IL, Busch H (1981). "Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24". Biochemistry 20 (5): 1100–1104. doi:10.1021/bi00508a009. PMID 6261785.
• Busch H, Goldknopf IL (1982). "Ubiquitin - protein conjugates". Mol. Cell. Biochem. 40 (3): 173–87. doi:10.1007/bf00224611. PMID 6275256.
• Treier M, Staszewski LM, Bohmann D (1994). "Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain". Cell 78 (5): 787–798. doi:10.1016/S0092-8674(94)90502-9. PMID 8087846.
• Cook WJ, Jeffrey LC, Kasperek E, Pickart CM (1994). "Structure of tetraubiquitin shows how multiubiquitin chains can be formed". J. Mol. Biol. 236 (2): 601–609. doi:10.1006/jmbi.1994.1169. PMID 8107144.
• Ramage R, Green J, Muir TW, et al. (1994). "Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin". Biochem. J. 299 (1): 151–8. PMC 1138034. PMID 8166633.