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Protein

Polyubiquitin-C

Gene

Ubc

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

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Activating enzyme
Sitei68 – 681Essential for function
Binding sitei72 – 721Activating enzyme

GO - Molecular functioni

GO - Biological processi

  • circadian rhythm Source: Reactome
  • Notch signaling pathway Source: Reactome
  • ubiquitin homeostasis Source: MGI
Complete GO annotation...

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-1227986. Signaling by ERBB2.
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-400253. Circadian Clock.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-446652. Interleukin-1 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-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-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-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-912631. Regulation of signaling by CBL.
R-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.
R-MMU-937039. IRAK1 recruits IKK complex.
R-MMU-937042. IRAK2 mediated activation of TAK1 complex.
R-MMU-937072. TRAF6 mediated induction of TAK1 complex.
R-MMU-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-MMU-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
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:
Polyubiquitin-C
Cleaved into the following 3 chains:
Gene namesi
Name:Ubc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:98889. Ubc.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396192Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396193Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396194Add
BLAST
Chaini229 – 30476Ubiquitin-related 1PRO_0000396195Add
BLAST
Chaini305 – 38076UbiquitinPRO_0000396196Add
BLAST
Chaini381 – 45676UbiquitinPRO_0000396197Add
BLAST
Chaini457 – 53276UbiquitinPRO_0000396198Add
BLAST
Chaini533 – 60876UbiquitinPRO_0000396199Add
BLAST
Chaini609 – 68476UbiquitinPRO_0000396200Add
BLAST
Chaini685 – 73450Ubiquitin-related 2PRO_0000396201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65 – 651Phosphoserine; by PINK1By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Cross-linki82 – 82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki87 – 87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139 – 139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei141 – 1411PhosphoserineBy similarity

Post-translational modificationi

Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PARK2), 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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP0CG50.
PRIDEiP0CG50.

2D gel databases

REPRODUCTION-2DPAGEP62991.

PTM databases

iPTMnetiP0CG50.
PhosphoSiteiP0CG50.
SwissPalmiP0CG50.

Expressioni

Gene expression databases

BgeeiENSMUSG00000008348.
ExpressionAtlasiP0CG50. baseline and differential.
GenevisibleiP0CG50. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204403. 451 interactions.
IntActiP0CG50. 2 interactions.
STRINGi10090.ENSMUSP00000114180.

Structurei

Secondary structure

1
734
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi610 – 6156Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi620 – 6245Combined sources
Helixi631 – 64212Combined sources
Helixi646 – 6483Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi660 – 6634Combined sources
Helixi665 – 6673Combined sources
Beta strandi674 – 6796Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNVX-ray1.60B/C/E/F1-76[»]
3A1QX-ray2.20A/B/D/E1-76[»]
3A9JX-ray1.18A/B1-76[»]
3A9KX-ray1.40A/B1-76[»]
3VHTX-ray2.40C1-76[»]
3WWQX-ray1.90A/B/D/E/G/H/J/K609-684[»]
3WXGX-ray3.10B/E609-684[»]
C/F609-680[»]
4NQLX-ray2.30B/C609-684[»]
ProteinModelPortaliP0CG50.
SMRiP0CG50. Positions 1-711.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CG50.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 15276Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 22876Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 30476Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini305 – 38076Ubiquitin-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini381 – 45676Ubiquitin-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini457 – 53276Ubiquitin-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini533 – 60876Ubiquitin-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 68476Ubiquitin-like 9PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 9 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00810000125435.
InParanoidiP0CG50.
KOiK08770.
OMAiTTINIKY.
OrthoDBiEOG091G178I.
TreeFamiTF354256.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 9 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 9 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 10 hits.
PROSITEiPS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CG50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT
260 270 280 290 300
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
310 320 330 340 350
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA
360 370 380 390 400
GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS
410 420 430 440 450
DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV
460 470 480 490 500
LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
510 520 530 540 550
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE
560 570 580 590 600
PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
610 620 630 640 650
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR
660 670 680 690 700
LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLD
710 720 730
VEPSVTTKKV KQEDRRTFLT TVSKKSPPCA CSWV
Length:734
Mass (Da):82,550
Last modified:July 27, 2011 - v2
Checksum:iEDD9B8556FF81D5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751G → GGMQIFVKTLTGKTITLEVE PSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSD YNIQKESTLHLVLRLRGGMQ IFVKTLTGKTITLEVEPSDT IENVKAKIQDKEGIPPDQQR LIFAGKQLEGGRTLSDYNIQ KESTLHLVLRLRG in AAG00513 (PubMed:12107596).Curated
Sequence conflicti265 – 2651P → S in AAG00512 (PubMed:12107596).Curated
Sequence conflicti265 – 2651P → S in AAG00513 (PubMed:12107596).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285161 Genomic DNA. Translation: AAG00512.1.
AF285162 Genomic DNA. Translation: AAG00513.1.
AC138613 Genomic DNA. No translation available.
D50527 mRNA. Translation: BAA09096.1.
CCDSiCCDS19684.2.
PIRiA49007.
S11296.
RefSeqiNP_062613.3. NM_019639.4.
UniGeneiMm.331.
Mm.419997.

Genome annotation databases

EnsembliENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348.
ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348.
GeneIDi22190.
KEGGimmu:22190.
UCSCiuc008zri.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285161 Genomic DNA. Translation: AAG00512.1.
AF285162 Genomic DNA. Translation: AAG00513.1.
AC138613 Genomic DNA. No translation available.
D50527 mRNA. Translation: BAA09096.1.
CCDSiCCDS19684.2.
PIRiA49007.
S11296.
RefSeqiNP_062613.3. NM_019639.4.
UniGeneiMm.331.
Mm.419997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNVX-ray1.60B/C/E/F1-76[»]
3A1QX-ray2.20A/B/D/E1-76[»]
3A9JX-ray1.18A/B1-76[»]
3A9KX-ray1.40A/B1-76[»]
3VHTX-ray2.40C1-76[»]
3WWQX-ray1.90A/B/D/E/G/H/J/K609-684[»]
3WXGX-ray3.10B/E609-684[»]
C/F609-680[»]
4NQLX-ray2.30B/C609-684[»]
ProteinModelPortaliP0CG50.
SMRiP0CG50. Positions 1-711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204403. 451 interactions.
IntActiP0CG50. 2 interactions.
STRINGi10090.ENSMUSP00000114180.

PTM databases

iPTMnetiP0CG50.
PhosphoSiteiP0CG50.
SwissPalmiP0CG50.

2D gel databases

REPRODUCTION-2DPAGEP62991.

Proteomic databases

PaxDbiP0CG50.
PRIDEiP0CG50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348.
ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348.
GeneIDi22190.
KEGGimmu:22190.
UCSCiuc008zri.2. mouse.

Organism-specific databases

CTDi7316.
MGIiMGI:98889. Ubc.

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00810000125435.
InParanoidiP0CG50.
KOiK08770.
OMAiTTINIKY.
OrthoDBiEOG091G178I.
TreeFamiTF354256.

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-1227986. Signaling by ERBB2.
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-400253. Circadian Clock.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-446652. Interleukin-1 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-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-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-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-912631. Regulation of signaling by CBL.
R-MMU-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.
R-MMU-937039. IRAK1 recruits IKK complex.
R-MMU-937042. IRAK2 mediated activation of TAK1 complex.
R-MMU-937072. TRAF6 mediated induction of TAK1 complex.
R-MMU-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-MMU-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
R-MMU-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP0CG50.
PROiP0CG50.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000008348.
ExpressionAtlasiP0CG50. baseline and differential.
GenevisibleiP0CG50. MM.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 9 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 9 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 10 hits.
PROSITEiPS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBC_MOUSE
AccessioniPrimary (citable) accession number: P0CG50
Secondary accession number(s): E9QKI0
, P02248, P02249, P02250, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.