Ubiquitin B

Ubiquitin is a protein that in humans is encoded by the UBB gene.[3]

UBB
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2KHW, 2MBB, 2MRO, 2MSG, 4UEL, 4UF6, 4WLR, 4WUR, 4ZPZ, 5CAW, 3OJ3, 5DK8, 5CRA, 4ZFR, 5CVO, 3ZLZ, 4WHV, 4ZFT, 3ZNH, 5D0M, 2Y5B, 2KWV, 5D0K, 5DFL, 5CVM, 4WZP, 5EDV, 5CVN, 2KWU, 4XOF, 5BNB, 2N13, 4ZUX, 5IFR, 5IBK, 5KGF, 5JG6, 5K9P, 5E6J
Identifiers
Aliases	UBB, HEL-S-50, Ubiquitin B
External IDs	OMIM: 191339 HomoloGene: 75104 GeneCards: UBB
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p11.2 Start 16,380,798 bp[1] End 16,382,745 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • protein tag • ubiquitin protein ligase binding Cellular component • cytoplasm • endocytic vesicle membrane • cytosol • mitochondrion • neuron projection • cell nucleus • extracellular exosome • cell membrane • nucleoplasm • neuronal cell body • endosome membrane • extracellular • mitochondrial outer membrane • endoplasmic reticulum quality control compartment • vesicle • endoplasmic reticulum membrane • host cell Biological process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • negative regulation of epidermal growth factor receptor signaling pathway • interstrand cross-link repair • nucleotide-excision repair, DNA damage recognition • positive regulation of canonical Wnt signaling pathway • tumor necrosis factor-mediated signaling pathway • regulation of type I interferon production • positive regulation of protein monoubiquitination • TRIF-dependent toll-like receptor signaling pathway • Fc-epsilon receptor signaling pathway • endosomal transport • global genome nucleotide-excision repair • NIK/NF-kappaB signaling • G2/M transition of mitotic cell cycle • stress-activated MAPK cascade • transforming growth factor beta receptor signaling pathway • macroautophagy • negative regulation of canonical Wnt signaling pathway • DNA damage response, detection of DNA damage • nucleotide-excision repair, DNA gap filling • error-free translesion synthesis • regulation of tumor necrosis factor-mediated signaling pathway • stimulatory C-type lectin receptor signaling pathway • negative regulation of transforming growth factor beta receptor signaling pathway • JNK cascade • regulation of transcription from RNA polymerase II promoter in response to hypoxia • nucleotide-excision repair, DNA incision • I-kappaB kinase/NF-kappaB signaling • innate immune system • Notch signaling pathway • neuron projection morphogenesis • regulation of mRNA stability • protein polyubiquitination • negative regulation of apoptotic process • negative regulation of transcription from RNA polymerase II promoter • virion assembly • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator • activation of MAPK activity • positive regulation of NF-kappaB transcription factor activity • anaphase-promoting complex-dependent catabolic process • negative regulation of type I interferon production • nucleotide-binding oligomerization domain containing signaling pathway • positive regulation of protein ubiquitination • GO:0046795 intracellular transport of virus • regulation of proteasomal protein catabolic process • GO:0019067 viral life cycle • MyD88-dependent toll-like receptor signaling pathway • error-prone translesion synthesis • MAPK cascade • regulation of mitochondrial membrane potential • fibroblast growth factor receptor signaling pathway • ion transmembrane transport • glycogen biosynthetic process • regulation of neuron death • positive regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • translesion synthesis • transcription-coupled nucleotide-excision repair • mitochondrion transport along microtubule • T cell receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • positive regulation of transcription from RNA polymerase II promoter • regulation of signal transduction by p53 class mediator • positive regulation of epidermal growth factor receptor signaling pathway • Wnt signaling pathway • nucleotide-excision repair, DNA duplex unwinding • nucleotide-excision repair, DNA incision, 5'-to lesion • ERBB2 signaling pathway • Wnt signaling pathway, planar cell polarity pathway • nucleotide-excision repair, preincision complex assembly • proteasome-mediated ubiquitin-dependent protein catabolic process • cellular protein metabolic process • protein folding • negative regulation of G2/M transition of mitotic cell cycle • protein ubiquitination • protein deubiquitination • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process • entry of bacterium into host cell • transmembrane transport • regulation of necroptotic process • membrane organization • endoplasmic reticulum mannose trimming • cellular iron ion homeostasis • regulation of hematopoietic stem cell differentiation • protein targeting to peroxisome • male meiosis I • female meiosis I • male gonad development • female gonad development • cytokine-mediated signaling pathway • modification-dependent protein catabolic process • hypothalamus gonadotrophin-releasing hormone neuron development • adipose tissue development • fat pad development • interleukin-1-mediated signaling pathway • seminiferous tubule development • energy homeostasis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7314	n/a
Ensembl	ENSG00000170315	n/a
UniProt	P0CG47	n/a
RefSeq (mRNA)	NM_018955 NM_001281716 NM_001281717 NM_001281718 NM_001281719 NM_001281720	n/a
RefSeq (protein)	NP_001268645 NP_001268646 NP_001268647 NP_001268648 NP_001268649 NP_061828	n/a
Location (UCSC)	Chr 17: 16.38 – 16.38 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

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).[4][5]

References

1. GRCh38: Ensembl release 89: ENSG00000170315 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. 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.
4. 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. S2CID 10932825.
5. "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. S2CID 38822700.
• 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. S2CID 15764136.
• 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. S2CID 4159096.
• 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. doi:10.1002/j.1460-2075.1985.tb03693.x. 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). "[23] Ubiquitination of Proteins". Ubiquitination of proteins. Meth. Enzymol. Methods in Enzymology. 106. pp. 238–262. doi:10.1016/0076-6879(84)06025-0. ISBN 978-0-12-182006-0. PMID 6092831.
• 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. S2CID 21101636.
• 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. S2CID 33344164.
• 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. doi:10.1042/bj2990151. PMC 1138034. PMID 8166633.