Polybikitiini B, UBB (17p11.2) . Ubikitiinigeeni

https://www.ncbi.nlm.nih.gov/gene/7314

UBB ubiquitin B

Tämä geeni koodaa  kolmen ubikitiinin sekvenssiä. Proteiini esiintyy prekursorimuotoisena, pääteaminohappo kolmannen ubikitiiniakson jälkeen. Tästä proteiinista on havaittu esiintyvän poikkeuksellista muotoa AD taudissa ja Downin oireyhtymässä 

Also known as

HEL-S-50

Summary

This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. 

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. An aberrant form of this protein has been detected in patients with Alzheimer's disease and Down syndrome. Pseudogenes of this gene are located on chromosomes 1, 2, 13, and 17. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]

Expression

Ubiquitous expression in liver (RPKM 498.1), testis (RPKM 495.1) and 25 other tissues See more

Preferred Names

polyubiquitin-B

Names

epididymis secretory protein Li 50

polyubiquitin B

Peptide  history, structure.  
https://www.ncbi.nlm.nih.gov/protein/NP_001268645.1

Related articles in PubMed

1. Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB⁺¹. Chojnacki M, et al. FEBS Lett, 2016 Dec. PMID 27861798, Free PMC Article
2. New crystal form of human ubiquitin in the presence of magnesium. Camara-Artigas A, et al. Acta Crystallogr F Struct Biol Commun, 2016 Jan. PMID 26750481, Free PMC Article
3. Ubiquitin B in cervical cancer: critical for the maintenance of cancer stem-like cell characters. Tian Y, et al. PLoS One, 2013. PMID 24367661, Free PMC Article
4. Downregulation of ubiquitin level via knockdown of polyubiquitin gene Ubb as potential cancer therapeutic intervention. Oh C, et al. Sci Rep, 2013. PMID 24022007, Free PMC Article
5. Mutant ubiquitin decreases amyloid β plaque formation in a transgenic mouse model of Alzheimer's disease. van Tijn P, et al. Neurochem Int, 2012 Oct. PMID 22797007

See all (227) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. The polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB have been characterized.
2. The C-terminal five residues of Ub, RLRGG, are responsible for the interaction with the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease.
3. A new crystallographic structure of human ubiquitin solved from crystals grown in the presence of magnesium.
4. Data suggest that both human ubiquitin and HFBII (hydrophobin-II from Trichoderma reesei) exhibit a critical surface hydration level (or effective hydrophobic interface at the surface) at which percolation transition of water network occurs.
5. UbB was significantly increased in prolonged Trichostatin A-selected HeLa cells and it played a key role in the maintenance of cervical cancer stem-like cells
6. downregulation of ubiquitin through Ubb-KD is a potential anti-cancer treatment by inhibiting ubiquitination at multiple sites related to oncogenic pathways and by weakening the ability of cancer cells to overcome increased stress.
7. A significant decrease in amyloid beta deposition and plaque formation suggests a role for the ubiquitin-proteasome system in the amyloid pathology of Alzheimer's disease.
8. age-dependent accumulation of Ubb(+1) , and how Ubb(+1) -mediated proteasome inhibition may contribute to Alzheimer's disease. [review]
9. Studies indicate that biomedical research on ubiquitin moves into translational research and drug discovery.
10. Studies indicate that DUBs recycle ubiquitin by processing polyubiquitin chains to generate free ubiquitin, and can be regulated by ubiquitination or phosphorylation.