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Details on Person UniProt:P0CG49 Ubb

Class:IdReferenceGeneProduct:937638
_chainChangeLogchain:1-76 added on Sat February 7 2015;chain:77-152 added on Sat February 7 2015;chain:153-228 added on Sat February 7 2015;chain:229-304 added on Sat February 7 2015;propeptide:- added on Sat February 7 2015
_displayNameUniProt:P0CG49 Ubb
_timestamp2026-02-20 21:35:46
chainchain:1-76
chain:77-152
chain:153-228
chain:229-304
propeptide:-
checksum0B8C7878AE958E68
commentFUNCTION 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.SUBCELLULAR LOCATION 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.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.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 For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.SIMILARITY Belongs to the ubiquitin family.
created[InstanceEdit:937368] Yung, CK
descriptionrecommendedName: Polyubiquitin-B component recommendedName: Ubiquitin /component
geneNameUbb
identifierP0CG49
isSequenceChangedFALSE
keywordADP-ribosylation
Cytoplasm
Isopeptide bond
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
Phosphoprotein
Reference proteome
Repeat
Ubl conjugation
modified[InstanceEdit:1042053] Yung, CK
[InstanceEdit:1220657] Yung, CK
[InstanceEdit:1300696] Yung, CK
[InstanceEdit:1301627] Yung, CK
[InstanceEdit:1551960] Weiser, JD
[InstanceEdit:1995863] Weiser, JD
[InstanceEdit:2132304] Weiser, JD
[InstanceEdit:2265580] Weiser, JD
[InstanceEdit:3445779] Weiser, JD
[InstanceEdit:5263031] Weiser, JD
[InstanceEdit:5433710] Weiser, JD
[InstanceEdit:5618415] Weiser, JD
[InstanceEdit:5634237] Weiser, JD
[InstanceEdit:5673015] Weiser, JD
[InstanceEdit:9027688] Weiser, JD
[InstanceEdit:9037114] Weiser, JD
[InstanceEdit:9637257] Weiser, JD
[InstanceEdit:9676415] Weiser, JD
[InstanceEdit:9773244] Weiser, Joel
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9983091] Weiser, Joel, 2026-02-20
nameUbb
referenceDatabase[ReferenceDatabase:2] UniProt
secondaryIdentifierUBB_MOUSE
P02248
P02249
P02250
P62991
Q29120
Q62317
Q64223
Q8VCH1
Q91887
Q91888
Q9CXY4
Q9CZM0
Q9D1R5
Q9D8D9
Q9ET23
Q9ET24
Q9Z0H9
sequenceLength305
species[Species:48892] Mus musculus
(referenceEntity)[EntityWithAccessionedSequence:940361] Ubiquitin (Ubb 3) [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:940363] Ubiquitin (Ubb 4) [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:940364] Ubiquitin (Ubb 1) [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:940366] Ubiquitin (Ubb 2) [nucleoplasm] [Mus musculus]
[EntityWithAccessionedSequence:940367] Ubiquitin (Ubb 1) [nucleoplasm] [Mus musculus]
[EntityWithAccessionedSequence:940380] Ubiquitin (Ubb 3) [nucleoplasm] [Mus musculus]
[EntityWithAccessionedSequence:940383] Ubiquitin (Ubb 2) [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:940385] Ubiquitin (Ubb 4) [nucleoplasm] [Mus musculus]
[EntityWithAccessionedSequence:9762991] Ubiquitin (Ubb 4) [lysosomal membrane] [Mus musculus]
[EntityWithAccessionedSequence:9763007] Ubiquitin (Ubb 2) [lysosomal membrane] [Mus musculus]
List all 36 refering instances
(referenceSequence)[ModifiedResidue:9932604] ubiquitinylated lysine at 276
[ModifiedResidue:9932615] ubiquitinylated lysine at 124
[ModifiedResidue:9932629] ubiquitinylated lysine at 48
[ModifiedResidue:9932653] ubiquitinylated lysine at 200
[ModifiedResidue:9973559] ubiquitinylated lysine at 291
[ModifiedResidue:9973568] ubiquitinylated lysine at 63
[ModifiedResidue:9973573] ubiquitinylated lysine at 139
[ModifiedResidue:9973583] ubiquitinylated lysine at 215
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No pathways have been reviewed or authored by UniProt:P0CG49 Ubb (937638)