P0CG49 · UBB_MOUSE
- ProteinPolyubiquitin-B
- GeneUbb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids305 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
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 proteotoxic stress response and cell cycle; 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.
Miscellaneous
Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins eL40 and eS31, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 54 | Interacts with activating enzyme | ||||
Sequence: R | ||||||
Site | 68 | Essential for function | ||||
Sequence: H | ||||||
Site | 72 | Interacts with activating enzyme | ||||
Sequence: R |
GO annotations
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolyubiquitin-B
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP0CG49
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Ubiquitin
Mitochondrion outer membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000114801 | 1-76 | Ubiquitin | |||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Cross-link | 48 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 65 | Phosphoserine; by PINK1 | ||||
Sequence: S | ||||||
Modified residue | 76 | ADP-ribosylglycine | ||||
Sequence: G | ||||||
Cross-link | 76 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | ||||
Sequence: G | ||||||
Chain | PRO_0000396188 | 77-152 | Ubiquitin | |||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Cross-link | 82 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 87 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 103 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 105 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 124 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 139 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 141 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000396189 | 153-228 | Ubiquitin | |||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Chain | PRO_0000396190 | 229-304 | Ubiquitin | |||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Propeptide | PRO_0000396191 | 305 | ||||
Sequence: Y |
Post-translational modification
Ubiquitin
Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.
Ubiquitin
Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-76 | Ubiquitin-like 1 | ||||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Domain | 77-152 | Ubiquitin-like 2 | ||||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Domain | 153-228 | Ubiquitin-like 3 | ||||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG | ||||||
Domain | 229-304 | Ubiquitin-like 4 | ||||
Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG |
Sequence similarities
Belongs to the ubiquitin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length305
- Mass (Da)34,369
- Last updated2010-08-10 v1
- Checksum0B8C7878AE958E68
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5SX22 | Q5SX22_MOUSE | Ubb | 236 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 31 | in Ref. 2; BAB29028 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 54 | in Ref. 2; BAB29028 | ||||
Sequence: R → S | ||||||
Sequence conflict | 61 | in Ref. 2; BAB29028 | ||||
Sequence: I → N | ||||||
Sequence conflict | 92 | in Ref. 2; BAB29028 | ||||
Sequence: E → G | ||||||
Sequence conflict | 117 | in Ref. 3; AAH19850 | ||||
Sequence: Q → H | ||||||
Sequence conflict | 147 | in Ref. 2; BAB28242 | ||||
Sequence: L → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X51703 EMBL· GenBank· DDBJ | CAA35999.1 EMBL· GenBank· DDBJ | mRNA | ||
AK012443 EMBL· GenBank· DDBJ | BAB28242.1 EMBL· GenBank· DDBJ | mRNA | ||
AK003190 EMBL· GenBank· DDBJ | BAB22630.1 EMBL· GenBank· DDBJ | mRNA | ||
AK013873 EMBL· GenBank· DDBJ | BAB29028.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019850 EMBL· GenBank· DDBJ | AAH19850.1 EMBL· GenBank· DDBJ | mRNA |