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Details on Person UniProt:P0CG47 UBB
| Class:Id | ReferenceGeneProduct:937481 |
|---|---|
| _chainChangeLog | chain:1-76 added on Fri February 6 2015;chain:77-152 added on Fri February 6 2015;chain:153-228 added on Fri February 6 2015;propeptide:- added on Fri February 6 2015 |
| _displayName | UniProt:P0CG47 UBB |
| _timestamp | 2026-02-20 21:35:46 |
| chain | chain:1-76 chain:77-152 chain:153-228 propeptide:- |
| checksum | 33011162F1C48BB1 |
| comment | FUNCTION 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.SUBUNIT Interacts with SKP1-KMD2A and SKP1-KMD2B complexes. Interacts with REV1 (PubMed:29778604).INTERACTION Phosphorylated at Ser-65 by PINK1 during mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291, PubMed:26161729). Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291, PubMed:26161729). 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 (PubMed:25527291).PTM 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.PTM (Microbial infection) Mono-ADP-ribosylated at Thr-66 by the C.violaceum CteC virulence factor. ADP-ribosylation causes the shutdown of polyubiquitin synthesis and disrupts the recognition and reversal of polyubiquitin.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.MISCELLANEOUS The mRNA encoding variant UBB(+1) is produced by an unknown mechanism involving the deletion of a GT dinucleotide in the close proximity of a GAGAG motif (PubMed:9422699). This variant mRNA is found in normal brain, but the encoded protein accumulates only in brain neurofibrillary tangles and neuritic plaques in Alzheimer disease and other tauopathies, as well as polyglutaminopathies (PubMed:14597671). UBB(+1) variant cannot be used for polyubiquitination, is not effectively degraded by the proteasome when ubiquitinated and ubiquitinated UBB(+1) is refractory to disassembly by deubiquitinating enzymes (DUBs). In healthy brain, UBB(+1) C-terminus can be cleaved by UCHL3 (PubMed:21762696).MISCELLANEOUS For a better understanding, features related to ubiquitin are only indicated for the first chain.SIMILARITY Belongs to the ubiquitin family. |
| created | [InstanceEdit:937368] Yung, CK |
| description | recommendedName: Polyubiquitin-B component recommendedName: Ubiquitin /component |
| geneName | UBB |
| identifier | P0CG47 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure ADP-ribosylation Cytoplasm Direct protein sequencing Isopeptide bond Membrane Mitochondrion Mitochondrion outer membrane Nucleus Phosphoprotein Reference proteome Repeat Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | UBB |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:4793752] ENSEMBL:ENSG00000170315 UBB [Homo sapiens] |
| secondaryIdentifier | UBB_HUMAN P02248 P02249 P02250 P62988 Q29120 Q6LBL4 Q6LDU5 Q8WYN8 Q91887 Q91888 Q9BWD6 Q9BX98 Q9UEF2 Q9UEG1 Q9UEK8 Q9UPK7 |
| sequenceLength | 229 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:939167] Ub-63-UBB(1-76) [endosome membrane] [Homo sapiens] [EntityWithAccessionedSequence:939168] Ub-215-UBB(153-228) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939171] UBB(153-228) [endocytic vesicle membrane] [Homo sapiens] [EntityWithAccessionedSequence:939193] Ub-215-UBB(153-228) [endosome membrane] [Homo sapiens] [EntityWithAccessionedSequence:939197] Ub-200-UBB(153-228) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939213] UBB(77-152) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939214] UBB(1-76) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939217] Ub-139-UBB(77-152) [endosome membrane] [Homo sapiens] [EntityWithAccessionedSequence:939224] Ub-63-UBB(1-76) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:939225] Ub-124-UBB(77-152) [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:939163] ubiquitinylated lysine at 215 [ModifiedResidue:939233] ubiquitinylated lysine at 139 [ModifiedResidue:939252] ubiquitinylated lysine at 63 [ModifiedResidue:941609] ubiquitinylated lysine at 200 [ModifiedResidue:941611] ubiquitinylated lysine at 124 [ModifiedResidue:941618] ubiquitinylated lysine at 48 [ModifiedResidue:3095905] ubiquitinylated lysine at 87 [ModifiedResidue:3095910] ubiquitinylated lysine at 11 [ModifiedResidue:3095922] ubiquitinylated lysine at 163 [ModifiedResidue:5689089] ubiquitinylated lysine at 82 |
| (secondReferenceSequence) | [InterChainCrosslinkedResidue:8853518] Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 90 and 76 [InterChainCrosslinkedResidue:8937080] Inter-chain Crosslink via ubiquitinylated lysine at unknown and 76 [InterChainCrosslinkedResidue:8937081] Inter-chain Crosslink via S-(glycyl)-L-cysteine (Cys-Gly) at 85 and 76 |
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No pathways have been reviewed or authored by UniProt:P0CG47 UBB (937481)
