Polyubikitiinin de novo synteesi , UBC (12q24.31) Ubikitiini C, HMG20

https://www.ncbi.nlm.nih.gov/gene/7316
 Tästä geenistä koodautuu polyubikitiiniedeltäjäproteiini. Sitä ilmenee eniten luuyrtimessöä ja sappirakossa ja 25 muussa kudoksessa.

Also known as

HMG20

Summary

This gene represents a ubiquitin gene, ubiquitin C. The encoded protein is a polyubiquitin precursor. Conjugation of ubiquitin monomers or polymers can lead to various effects within a cell, depending on the residues to which ubiquitin is conjugated. Ubiquitination has been associated with protein degradation, DNA repair, cell cycle regulation, kinase modification, endocytosis, and regulation of other cell signaling pathways. [provided by RefSeq, Aug 2010]

Expression

Ubiquitous expression in bone marrow (RPKM 1559.8), gall bladder (RPKM 1270.7) and 25 other tissues See more

Preferred Names

polyubiquitin-C, homopolymeric multiubiquitin protein chain:  685 aminoacids.
(9 ubiquitin  sequences, (1..76); (77..152);(153..228); 229..304);(305..380); (381..456); (457..532) (533..608); 609..684);  1 aminoacid. 

Peptide history and structure.
https://www.ncbi.nlm.nih.gov/protein/NP_066289.3

ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggmqif vktltgktit levepsdtie nvkakiqdke gippdqqrli
      121 fagkqledgr tlsdyniqke stlhlvlrlr ggmqifvktl tgktitleve psdtienvka
      181 kiqdkegipp dqqrlifagk qledgrtlsd yniqkestlh lvlrlrggmq ifvktltgkt
      241 itlevepsdt ienvkakiqd kegippdqqr lifagkqled grtlsdyniq kestlhlvlr
      301 lrggmqifvk tltgktitle vepsdtienv kakiqdkegi ppdqqrlifa gkqledgrtl
      361 sdyniqkest lhlvlrlrgg mqifvktltg ktitleveps dtienvkaki qdkegippdq
      421 qrlifagkql edgrtlsdyn iqkestlhlv lrlrggmqif vktltgktit levepsdtie
      481 nvkakiqdke gippdqqrli fagkqledgr tlsdyniqke stlhlvlrlr ggmqifvktl
      541 tgktitleve psdtienvka kiqdkegipp dqqrlifagk qledgrtlsd yniqkestlh
      601 lvlrlrggmq ifvktltgkt itlevepsdt ienvkakiqd kegippdqqr lifagkqled
      661 grtlsdyniq kestlhlvlr lrggv
//

Related articles in PubMed

1. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Kurauskas V, et al. Nat Commun, 2017 Jul 27. PMID 28747759, Free PMC Article
2. Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell-mimicking crowded solution. Munari F, et al. FEBS Lett, 2017 Apr. PMID 28267209, Free PMC Article
3. Ubiquitin recognition by the proteasome. Saeki Y. J Biochem, 2017 Feb 1. PMID 28069863
4. The emerging complexity of ubiquitin architecture. Ohtake F, et al. J Biochem, 2017 Feb 1. PMID 28011818
5. Regulation of primary cilia formation by the ubiquitin-proteasome system. Shearer RF, et al. Biochem Soc Trans, 2016 Oct 15. PMID 27911708 

See all (974) citations in PubMed

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

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. Regulation of transcriptional activators by DNA-binding domain (DBD) ubiquitination has shown that, when attached to the DBD of either p53 or IRF-1, ubiquitin is orientated towards, and makes contact with, the DNA.
2. Data show that ubiquitin variants (Ubvs) that bind to USP2 or USP21 (DUBs)contain a similar core functional epitope, or "hot spot," consisting mainly of positions that are conserved as the wild type sequence, but also some positions that prefer mutant sequences. (USP luokan DUB molekyylejä on 5/) 
3. Data show that the packing of ubiquitin can significantly alter the thermodynamics and kinetics of local conformational exchange.
4. Model of ASB9 in complex with its substrate, creatine kinase, reveals a mechanism for dynamic ubiquitin transfer.
5. The lysine48-lysine63 branched ubiquitin chain regulates NF-kappaB signaling.
6. Noncovalent ubiquitin interactions regulate the catalytic activity of ubiquitin writers. (Review)
7. The authors now report the crystal structure of a human Parkin-phosphoubiquitin complex, which shows that phosphoubiquitin binding induces movement in the 'in-between RING' (IBR) domain to reveal a cryptic ubiquitin-binding site.
8. Studies indicate a role for the ubiquitin-proteasome system (UPS) as a key regulator of ciliogenesis.
9. Chicago Sky Blue 6B (CSB6B) binds directly to the beta-groove of ubiquitin and could inhibit the binding of ubiquitin to chemokine (C-X-C motif) receptor 4 (CXCR4), a cell surface ubiquitin receptor.
10. Studies suggest that ubiquitin signals for the proteasome involved more that Lys48 (K48).