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Protein

Polyubiquitin-B

Gene

UBB

Organism
Bos taurus (Bovine)
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.By similarity

Sites

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
Gene namesi
Name:UBB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 19

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396140Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396141Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396142Add
BLAST
Chaini229 – 30476UbiquitinPRO_0000396143Add
BLAST
Propeptidei305 – 3051PRO_0000396144

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki63 – 63Glycyl 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)
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

PRIDEiP0CG53.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HGSO149647EBI-5333021,EBI-740220From a different organism.
HSE1P387532EBI-5333021,EBI-1382From a different organism.
STAMQ927839EBI-5333021,EBI-752333From a different organism.
VPS27P403436EBI-5333021,EBI-20380From a different organism.

Protein-protein interaction databases

BioGridi158705. 1 interaction.
IntActiP0CG53. 10 interactions.
MINTiMINT-1486309.

Structurei

3D structure databases

ProteinModelPortaliP0CG53.
ModBaseiSearch...
MobiDBiSearch...

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

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 4 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00780000121932.
InParanoidiP0CG53.
KOiK04551.
OMAiVHENTRR.
OrthoDBiEOG7JDR1W.
TreeFamiTF300820.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CG53-1 [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

LRGGC
Length:305
Mass (Da):34,308
Last modified:August 10, 2010 - v1
Checksum:i1E6C7878AE958E68
GO

Sequence cautioni

The sequence BAC56573.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence BAC56573.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331S → F in CAA79146 (PubMed:8382528).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18245 mRNA. Translation: CAA79146.1.
AB099044 mRNA. Translation: BAC56534.1.
AB099083 mRNA. Translation: BAC56573.1. Sequence problems.
BC114001 mRNA. Translation: AAI14002.1.
M62429 mRNA. Translation: AAA30720.1.
PIRiI45964.
S29853.
RefSeqiNP_776558.1. NM_174133.2.
UniGeneiBt.111403.
Bt.2878.

Genome annotation databases

EnsembliENSBTAT00000022919; ENSBTAP00000022919; ENSBTAG00000017246.
GeneIDi281370.
KEGGibta:281370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18245 mRNA. Translation: CAA79146.1.
AB099044 mRNA. Translation: BAC56534.1.
AB099083 mRNA. Translation: BAC56573.1. Sequence problems.
BC114001 mRNA. Translation: AAI14002.1.
M62429 mRNA. Translation: AAA30720.1.
PIRiI45964.
S29853.
RefSeqiNP_776558.1. NM_174133.2.
UniGeneiBt.111403.
Bt.2878.

3D structure databases

ProteinModelPortaliP0CG53.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158705. 1 interaction.
IntActiP0CG53. 10 interactions.
MINTiMINT-1486309.

Proteomic databases

PRIDEiP0CG53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022919; ENSBTAP00000022919; ENSBTAG00000017246.
GeneIDi281370.
KEGGibta:281370.

Organism-specific databases

CTDi7314.

Phylogenomic databases

GeneTreeiENSGT00780000121932.
InParanoidiP0CG53.
KOiK04551.
OMAiVHENTRR.
OrthoDBiEOG7JDR1W.
TreeFamiTF300820.

Miscellaneous databases

NextBioi20805375.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a full-length cDNA encoding a bovine four tandem-repeat ubiquitin."
    Wempe F., Scheit K.H.
    Biochim. Biophys. Acta 1172:209-211(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Seminal vesicle.
  2. "Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
    Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.
    Mol. Reprod. Dev. 65:9-18(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum and Liver.
  4. "The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells."
    Schlesinger D.H., Goldstein G., Niall H.D.
    Biochemistry 14:2214-2218(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-74.
  5. "The biosynthesis of ubiquitin by parathyroid gland."
    Hamilton J.W., Rouse J.B.
    Biochem. Biophys. Res. Commun. 96:114-120(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-50.
  6. "Ganglioside binding proteins of calf brain with ubiquitin-like N-terminals."
    Zdebska E., Antoniewicz J., Nilsson B., Sandhoff K., Fuerst W., Janik P., Koscielak J.
    Eur. J. Biochem. 210:483-489(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Tissue: Brain.
  7. "Viral cytopathogenicity correlated with integration of ubiquitin-coding sequences."
    Meyers G., Tautz N., Dubovi E.J., Thiel H.-J.
    Virology 180:602-616(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-305.
    Tissue: Kidney.

Entry informationi

Entry nameiUBB_BOVIN
AccessioniPrimary (citable) accession number: P0CG53
Secondary accession number(s): O97577
, P02248, P02249, P02250, P62990, P80169, Q01235, Q24K23, Q28169, Q28170, Q29120, Q3T0V5, Q3ZCE3, Q862C1, Q862F4, Q862M4, Q862T5, Q862X8, Q91887, Q91888
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: April 1, 2015
This is version 40 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.