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Mus musculus (Mouse)
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli


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.1 Publication


Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, 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.


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54Activating enzyme1
Sitei68Essential for function1
Binding sitei72Activating enzyme1

GO - Biological processi

  • adipose tissue development Source: MGI
  • circadian rhythm Source: Reactome
  • energy homeostasis Source: MGI
  • fat pad development Source: MGI
  • female gonad development Source: MGI
  • female meiosis I Source: MGI
  • hypothalamus gonadotrophin-releasing hormone neuron development Source: MGI
  • male gonad development Source: MGI
  • male meiosis I Source: MGI
  • mitochondrion transport along microtubule Source: MGI
  • neuron projection morphogenesis Source: MGI
  • positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • regulation of mitochondrial membrane potential Source: MGI
  • regulation of neuron death Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • seminiferous tubule development Source: MGI

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1253288. Downregulation of ERBB4 signaling.
R-MMU-1295596. Spry regulation of FGF signaling.
R-MMU-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-MMU-168638. NOD1/2 Signaling Pathway.
R-MMU-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-179409. APC-Cdc20 mediated degradation of Nek2A.
R-MMU-182971. EGFR downregulation.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-201681. TCF dependent signaling in response to WNT.
R-MMU-202424. Downstream TCR signaling.
R-MMU-205043. NRIF signals cell death from the nucleus.
R-MMU-209543. p75NTR recruits signalling complexes.
R-MMU-209560. NF-kB is activated and signals survival.
R-MMU-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-MMU-2173788. Downregulation of TGF-beta receptor signaling.
R-MMU-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-MMU-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-MMU-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-2559585. Oncogene Induced Senescence.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2672351. Stimuli-sensing channels.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-3134975. Regulation of innate immune responses to cytosolic DNA.
R-MMU-3322077. Glycogen synthesis.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-446652. Interleukin-1 family signaling.
R-MMU-450302. activated TAK1 mediates p38 MAPK activation.
R-MMU-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-4641263. Regulation of FZD by ubiquitination.
R-MMU-508751. Circadian Clock.
R-MMU-5205685. Pink/Parkin Mediated Mitophagy.
R-MMU-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5654727. Negative regulation of FGFR2 signaling.
R-MMU-5654732. Negative regulation of FGFR3 signaling.
R-MMU-5654733. Negative regulation of FGFR4 signaling.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5675221. Negative regulation of MAPK pathway.
R-MMU-5675482. Regulation of necroptotic cell death.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689877. Josephin domain DUBs.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-5689896. Ovarian tumor domain proteases.
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5696394. DNA Damage Recognition in GG-NER.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-6804757. Regulation of TP53 Degradation.
R-MMU-6804760. Regulation of TP53 Activity through Methylation.
R-MMU-6807004. Negative regulation of MET activity.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69231. Cyclin D associated events in G1.
R-MMU-69298. Association of licensing factors with the pre-replicative complex.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69541. Stabilization of p53.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8849469. PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-MMU-8856828. Clathrin-mediated endocytosis.
R-MMU-8863795. Downregulation of ERBB2 signaling.
R-MMU-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
R-MMU-8866654. E3 ubiquitin ligases ubiquitinate target proteins.
R-MMU-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-8939902. Regulation of RUNX2 expression and activity.
R-MMU-8941858. Regulation of RUNX3 expression and activity.
R-MMU-8948747. Regulation of PTEN localization.
R-MMU-8948751. Regulation of PTEN stability and activity.
R-MMU-8951664. Neddylation.
R-MMU-901032. ER Quality Control Compartment (ERQC).
R-MMU-9010553. Regulation of expression of SLITs and ROBOs.
R-MMU-912631. Regulation of signaling by CBL.
R-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-MMU-917937. Iron uptake and transport.
R-MMU-936440. Negative regulators of DDX58/IFIH1 signaling.
R-MMU-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-MMU-937041. IKK complex recruitment mediated by RIP1.
R-MMU-937042. IRAK2 mediated activation of TAK1 complex.
R-MMU-937072. TRAF6-mediated induction of TAK1 complex within TLR4 complex.
R-MMU-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleaved into the following chain:
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98888. Ubb.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001148011 – 76UbiquitinAdd BLAST76
ChainiPRO_000039618877 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396189153 – 228UbiquitinAdd BLAST76
ChainiPRO_0000396190229 – 304UbiquitinAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65Phosphoserine; by PINK1By similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Cross-linki82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei141PhosphoserineBy similarity1

Post-translational modificationi

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.By similarity
Ubiquitin: Mono-ADP-riblosylated 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.By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases


2D gel databases


PTM databases



Gene expression databases

ExpressionAtlasiP0CG49. baseline and differential.
GenevisibleiP0CG49. MM.


Protein-protein interaction databases

BioGridi204402. 10 interactors.
IntActiP0CG49. 2 interactors.


3D structure databases


Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 76Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST76
Domaini77 – 152Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST76
Domaini153 – 228Ubiquitin-like 3PROSITE-ProRule annotationAdd BLAST76
Domaini229 – 304Ubiquitin-like 4PROSITE-ProRule annotationAdd BLAST76

Sequence similaritiesi

Belongs to the ubiquitin family.Curated

Keywords - Domaini


Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.

Family and domain databases

InterProiView protein in InterPro
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-like_domsf.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
PfamiView protein in Pfam
PF00240. ubiquitin. 4 hits.
SMARTiView protein in SMART
SM00213. UBQ. 4 hits.
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiView protein in PROSITE
PS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.


Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CG49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
60 70 80 90 100
110 120 130 140 150
160 170 180 190 200
210 220 230 240 250
260 270 280 290 300

Mass (Da):34,369
Last modified:August 10, 2010 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31Q → R in BAB29028 (PubMed:16141072).Curated1
Sequence conflicti54R → S in BAB29028 (PubMed:16141072).Curated1
Sequence conflicti61I → N in BAB29028 (PubMed:16141072).Curated1
Sequence conflicti92E → G in BAB29028 (PubMed:16141072).Curated1
Sequence conflicti117Q → H in AAH19850 (PubMed:15489334).Curated1
Sequence conflicti147L → F in BAB28242 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
Links Updated
X51703 mRNA. Translation: CAA35999.1.
AK012443 mRNA. Translation: BAB28242.1.
AK003190 mRNA. Translation: BAB22630.1.
AK013873 mRNA. Translation: BAB29028.1.
BC019850 mRNA. Translation: AAH19850.1.
RefSeqiNP_001300913.1. NM_001313984.1.
NP_035794.1. NM_011664.4.

Genome annotation databases

EnsembliENSMUST00000019649; ENSMUSP00000019649; ENSMUSG00000019505.
UCSCiuc007jjg.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiUBB_MOUSE
AccessioniPrimary (citable) accession number: P0CG49
Secondary accession number(s): P02248
, P02249, P02250, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: December 20, 2017
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program


Keywords - Technical termi

Complete proteome, Reference proteome


  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families