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Protein

Polyubiquitin-B

Gene

Ubb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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

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.

Sites

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-508751 Circadian Clock

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
Gene namesi
Name:Ubb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • 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
PropeptideiPRO_00003961913051

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-linki103Glycyl 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

PaxDbiP0CG49
PRIDEiP0CG49

2D gel databases

REPRODUCTION-2DPAGEiP62991

PTM databases

iPTMnetiP0CG49
PhosphoSitePlusiP0CG49

Expressioni

Gene expression databases

BgeeiENSMUSG00000019505
ExpressionAtlasiP0CG49 baseline and differential
GenevisibleiP0CG49 MM

Interactioni

Protein-protein interaction databases

BioGridi204402, 11 interactors
IntActiP0CG49, 2 interactors
MINTiP0CG49
STRINGi10090.ENSMUSP00000019649

Structurei

3D structure databases

ProteinModelPortaliP0CG49
SMRiP0CG49
ModBaseiSearch...
MobiDBiSearch...

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

Repeat

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00810000125435
InParanoidiP0CG49
KOiK04551
OMAiVHENTRR
OrthoDBiEOG091G178I
PhylomeDBiP0CG49
TreeFamiTF300820

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
PRINTSiPR00348 UBIQUITIN
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

Sequencei

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
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

LRGGY
Length:305
Mass (Da):34,369
Last modified:August 10, 2010 - v1
Checksum:i0B8C7878AE958E68
GO

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:
EMBLi
GenBanki
DDBJi
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
CCDSiCCDS24826.1
PIRiS12583
RefSeqiNP_001300913.1, NM_001313984.1
NP_035794.1, NM_011664.4
UniGeneiMm.371592
Mm.487829

Genome annotation databases

EnsembliENSMUST00000019649; ENSMUSP00000019649; ENSMUSG00000019505
GeneIDi22187
KEGGimmu:22187
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: February 28, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health