Ubiquitin B

PDB rendering based on 1aar.

Available structures
PDB	1aar, 1cmx, 1d3z, 1f9j, 1fxt, 1g6j, 1gjz, 1nbf, 1ogw, 1otr, 1p3q, 1q0w, 1q5w, 1s1q, 1sif, 1tbe, 1ubi, 1ubq, 1ud7, 1uzx, 1v80, 1v81, 1wr1, 1wr6, 1wrd, 1xd3, 1xqq, 1yd8, 1yiw, 1yj1, 1yx5, 1yx6, 1zgu, 2ayo, 2bgf, 2c7m, 2c7n, 2d3g, 2den, 2dx5, 2fcm, 2fcn, 2fcq, 2fcs, 2fid, 2fif, 2fuh, 2g3q, 2g45, 2gbj, 2gbk, 2gbm, 2gbn, 2gbr, 2gmi, 2hd5, 2hth, 2ibi, 2j7q, 2nr2, 2o6v, 2oob

Identifiers

Symbols

UBB; FLJ25987; MGC8385; RPS27A; UBA52; UBC

External IDs

OMIM: 191339 HomoloGene: 75104 GeneCards: UBB Gene

Gene Ontology
Molecular function	• protein binding
Cellular component	• nucleus • nucleoplasm • nucleoplasm • cytoplasm • cytosol • cytosol • plasma membrane • endosome membrane • endosome membrane • endocytic vesicle membrane
Biological process	• cell cycle checkpoint • G1/S transition of mitotic cell cycle • S phase of mitotic cell cycle • activation of MAPK activity • M/G1 transition of mitotic cell cycle • mitotic cell cycle • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • DNA repair • apoptosis • apoptosis • anti-apoptosis • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • epidermal growth factor receptor signaling pathway • I-kappaB kinase/NF-kappaB cascade • JNK cascade • Toll signaling pathway • induction of apoptosis by extracellular signals • viral reproduction • cellular membrane organization • RNA metabolic process • mRNA metabolic process • endosome transport • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • negative regulation of type I interferon production • toll-like receptor 1 signaling pathway • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • negative regulation of epidermal growth factor receptor signaling pathway • regulation of apoptosis • positive regulation of I-kappaB kinase/NF-kappaB cascade • innate immune response • nerve growth factor receptor signaling pathway • 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 mitotic cell cycle • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_018955

n/a

RefSeq (protein)

NP_061828

n/a

Location (UCSC)

Chr 17:
16.28 – 16.29 Mb

n/a

PubMed search

[1]

n/a

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

Function

Ubiquitin, one of the most conserved proteins known. 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

^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1684968.
^ 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.
^ "Entrez Gene: UBB ubiquitin B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314.

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). "Hybrid troponin reconstituted from vertebrate and arthropod subunits". Nature 255 (5507): 423–4. doi:10.1038/255424a0. PMID 124018.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1977345.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=333777.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=331738.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=554252.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=340445.
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: 238–262. doi:10.1016/0076-6879(84)06025-0. ISBN 9780121820060. 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. 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 ( Pt 1): 151–8. PMC 1138034. PMID 8166633. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1138034.

PDB gallery

1aar: STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)

1cmx: STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

1d3z: UBIQUITIN NMR STRUCTURE

1f9j: STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN

1fxt: STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX

1g6j: STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES

1gjz: SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN

1nbf: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

1ogw: SYNTHETIC UBIQUITIN WITH FLUORO-LEU AT 50 AND 67

1otr: Solution Structure of a CUE-Ubiquitin Complex

1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9

1q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex

1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers

1s1q: TSG101(UEV) domain in complex with Ubiquitin

1sif: Crystal structure of a multiple hydrophobic core mutant of ubiquitin

1tbe: STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED

1ubi: SYNTHETIC STRUCTURAL AND BIOLOGICAL STUDIES OF THE UBIQUITIN SYSTEM. PART 1

1ubq: STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION

1ud7: SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D7

1uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN

1v80: Solution structures of ubiquitin at 30 bar and 3 kbar

1v81: Solution structures of ubiquitin at 30 bar and 3 kbar

1wr1: The complex sturcture of Dsk2p UBA with ubiquitin

1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin

1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin

1xd3: Crystal structure of UCHL3-UbVME complex

1xqq: Simultaneous determination of protein structure and dynamics

1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

1yiw: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin

1yj1: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin

1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex

1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex

1zgu: Solution structure of the human Mms2-Ubiquitin complex

2ayo: Structure of USP14 bound to ubquitin aldehyde

2bgf: NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA

2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN

2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN

2d3g: Double sided ubiquitin binding of Hrs-UIM

2den: Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin

2dx5: The complex structure between the mouse EAP45-GLUE domain and ubiquitin

2fcm: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin with a Cubic Space Group

2fcn: X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group

2fcq: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group

2fcs: X-ray Crystal Structure of a Chemically Synthesized [L-Gln35]Ubiquitin with a Cubic Space Group

2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex

2g3q: Solution Structure of Ede1 UBA-ubiquitin complex

2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin

2gbj: Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.

2gbk: Crystal Structure of the 9-10 MoaD Insertion Mutant of Ubiquitin

2gbm: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

2gbn: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

2gbr: Crystal Structure of the 35-36 MoaD Insertion Mutant of Ubiquitin

2gmi: Mms2/Ubc13~Ubiquitin

2hd5: USP2 in complex with ubiquitin

2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain

2ibi: Covalent Ubiquitin-USP2 Complex

2j7q: CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE

2nr2: The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native states ensembles of proteins

2o6v: Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin

Ubiquitin B

Function

References

Further reading