Ubiquitin B

Ubiquitin B

Ubiquitin B, also known as UBB, is a human gene.

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. [cite web | title = Entrez Gene: UBB ubiquitin B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*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 | 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 | 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=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=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 | 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 | 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=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 | 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=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 | 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 | 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=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 | 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 | author=Busch H |title=Ubiquitination of proteins. |journal=Meth. Enzymol. |volume=106 |issue= |pages= 238–62 |year= 1984 |pmid= 6092831 |doi=
*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 | 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=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=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • Ubiquitin — is a highly conserved regulatory protein that is expressed in eukaryotes. Ubiquitination (or ubiquitylation) refers to the post translational modification of a protein by the covalent attachment (via an isopeptide bond) of one or more ubiquitin… …   Wikipedia

  • Ubiquitin — Bändermodell …   Deutsch Wikipedia

  • Ubiquitin C — Ubiquitin C, also known as UBC, is a human gene.cite web | title = Entrez Gene: UBC ubiquitin C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=7316| accessdate = ] PBB Summary section title = summary text …   Wikipedia

  • ubiquitin — ubiquitin. См. убикитин. (Источник: «Англо русский толковый словарь генетических терминов». Арефьев В.А., Лисовенко Л.А., Москва: Изд во ВНИРО, 1995 г.) …   Молекулярная биология и генетика. Толковый словарь.

  • ubiquitin — A protein (8.5 kD) found in all eukaryotic cells. Can be linked to the lysine side chains of proteins by formation of an amide bond to its C terminal glycine in an ATP requiring process. The protein/ubiquitin complex is subject to rapid… …   Dictionary of molecular biology

  • Ubiquitin carboxy-terminal hydrolase L1 — (UCH L1) (EC number|3.1.2.15) is a deubiqutinating enzyme. PBB Summary section title = summary text = UCHL1 is a member of a gene family whose products hydrolyze small C terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression… …   Wikipedia

  • Ubiquitin-activating enzyme — Ubiquitin activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of …   Wikipedia

  • Ubiquitin-conjugating enzyme — Ubiquitin conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin carrier enzymes , perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome.The ubiquitination process… …   Wikipedia

  • Ubiquitin-Protein-Ligase Parkin — Masse/Länge Primärstruktur 465 Aminosäuren …   Deutsch Wikipedia

  • Ubiquitin ligase — A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that covalently attaches ubiquitin to a lysine on a target protein via an isopeptide bond. In general, the ubiquitin ligase is involved in polyubiquitination: A second ubiquitin …   Wikipedia

Share the article and excerpts

Direct link
… Do a right-click on the link above
and select “Copy Link”