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Browse result for Polyubiquitination

※ introduction

    Polyubiquitination is the formation of a ubiquitin chain on a single lysine residue on the substrate protein. Following addition of a single ubiquitin moiety to a protein substrate, further ubiquitin molecules can be added to the first, yielding a polyubiquitin chain. These chains are made by linking the glycine residue of a ubiquitin molecule to a lysine of ubiquitin bound to a substrate. Ubiquitin has seven lysine residues and an N-terminus that may serve as points of ubiquitination; they are K6, K11, K27, K29, K33, K48, and K63. Lysine 48-linked chains were the first identified and are the best-characterised type of ubiquitin chain. K63 chains have also been well-characterised, whereas the function of other lysine chains, mixed chains, branched chains, N-terminal linear chains, and heterologous chains (mixtures of ubiquitin and other ubiquitin-like proteins) remains more unclear.

Reference
Wiki: Polyubiquitination



UniProt ACEntrez IDGene NameProtein NameOrganism
O004637188
TRAF5
TNF receptor-associated factor 5
Homo sapiens
P38398672
BRCA1
Breast cancer type 1 susceptibility protein
Homo sapiens
Q078204170
MCL1
Induced myeloid leukemia cell differentiation protein Mcl-1
Homo sapiens
Q131187071
KLF10
Krueppel-like factor 10
Homo sapiens
Q14790841
CASP8
Caspase-8 [Cleaved into: Casp
Homo sapiens
Q9Y2389940
DLEC1
Deleted in lung and esophageal cancer protein 1
Homo sapiens