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P0CG47 Proteins Ubiquitin-like domain Repeats
Uniprot ID:P0CG47
Protein name: Polyubiquitin-B [Cleaved into: Ubiquitin]
Gene : UBB
Protein Family:Ubiquitin family
Squence Length : 229
Sequnce
>P0CG47 230 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
Domains
DOMAIN 1 76 Ubiquitin-like 1 DOMAIN 77 152 Ubiquitin-like 2 DOMAIN 153 228 Ubiquitin-like 3
Ubiquitin-like sequence regions
1 - 76 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQ 77 - 152 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQ 153 - 228 IFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC
Function
"Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling"
Binding Site
BINDING 54 54 Activating enzyme. BINDING 72 72 Activating enzyme
Mutation
"48 48 K->R: No effect on HLTF-mediated polyubiquitination of PCNA 63 63 K->R: Abolishes HLTF-mediated polyubiquitination of PCNA 65 65 S->A: Prevents phosphorylation in case of mitophagy 65 65 S->D: Phosphomimetic mutant that binds and activates PRKN 68 68 H->G: Loss of DTX3L-mediated polyubiquitination of histone H3 and H4 72 72 R->G: No effect on ADP-ribosylation 72 72 R->K: No effect on ADP-ribosylation, when associated with K-74 74 74 R->G: No effect on ADP-ribosylation 74 74 R->K: No effect on ADP-ribosylation, when associated with K-72 76 76 G->A: Loss of ADP-ribosylation"