Ubiquitin B

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

UBB
Available structures PDB Ortholog 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; MGI: 98888; HomoloGene: 75104; GeneCards: UBB; OMA:UBB - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p11.2 Start 16,380,798 bp End 16,382,745 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B2|11 38.46 cM Start 62,441,997 bp End 62,444,039 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pons pars reticulata pars compacta endothelial cell lateral nuclear group of thalamus middle temporal gyrus pancreatic ductal cell external globus pallidus bronchial epithelial cell retinal pigment epithelium Top expressed in neural tube primary oocyte blastocyst mesencephalon dentate gyrus of hippocampal formation granule cell rhombencephalon primary visual cortex cerebellar cortex superior frontal gyrus hypothalamus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding protein tag ubiquitin protein ligase binding Cellular component cytoplasm endocytic vesicle membrane cytosol mitochondrion neuron projection nucleus extracellular exosome plasma membrane nucleoplasm soma endosome membrane extracellular space 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 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 response Notch signaling pathway neuron projection morphogenesis regulation of mRNA stability protein polyubiquitination negative regulation of apoptotic process negative regulation of transcription by RNA polymerase II virion assembly positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator 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 intracellular transport of virus regulation of proteasomal protein catabolic process 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 by RNA polymerase II 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 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 22187 Ensembl ENSG00000170315 ENSMUSG00000019505 UniProt P0CG47 P0CG49 RefSeq (mRNA) NM_018955 NM_001281716 NM_001281717 NM_001281718 NM_001281719 NM_001281720 NM_011664 NM_001313984 RefSeq (protein) NP_001268645 NP_001268646 NP_001268647 NP_001268648 NP_001268649 NP_061828 NP_001300913 NP_035794 Location (UCSC) Chr 17: 16.38 – 16.38 Mb Chr 11: 62.44 – 62.44 Mb PubMed search
Wikidata
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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).

Further reading

• Conaway RC, Brower CS, Conaway JW (2002). "Emerging roles of ubiquitin in transcription regulation". Science. 296 (5571): 1254–1258. Bibcode:2002Sci...296.1254C. 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. Bibcode:1975Natur.255..423S. 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. S2CID 23901646.
• 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. doi:10.1016/S0021-9258(17)39652-7. 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). "Ubiquitination of Proteins". Posttranslational Modifications Part A. Methods in Enzymology. Vol. 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.