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P0CG53 (UBB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyubiquitin-B

Cleaved into the following chain:

  1. Ubiquitin
Gene names
Name:UBB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

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.

Sequence similarities

Belongs to the ubiquitin family.

Contains 4 ubiquitin-like domains.

Sequence caution

The sequence BAC56573.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC56573.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 20150893. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396140
Chain77 – 15276Ubiquitin
PRO_0000396141
Chain153 – 22876Ubiquitin
PRO_0000396142
Chain229 – 30476Ubiquitin
PRO_0000396143
Propeptide3051
PRO_0000396144

Regions

Domain1 – 7676Ubiquitin-like 1
Domain77 – 15276Ubiquitin-like 2
Domain153 – 22876Ubiquitin-like 3
Domain229 – 30476Ubiquitin-like 4

Sites

Binding site541Activating enzyme
Binding site721Activating enzyme
Site681Essential for function

Amino acid modifications

Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Sequence conflict1331S → F in CAA79146. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0CG53 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 1E6C7878AE958E68

FASTA30534,308
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI 

       130        140        150        160        170        180 
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA 

       190        200        210        220        230        240 
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 

       250        260        270        280        290        300 
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 


LRGGC 

« Hide

References

« Hide 'large scale' references
[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(1993) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-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(1975) [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(1980) [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(1992) [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(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-305.
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI45964.
S29853.
RefSeqNP_776558.1. NM_174133.2.
XP_005220351.1. XM_005220294.1.
XP_005220352.1. XM_005220295.1.
UniGeneBt.111403.
Bt.2878.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158705. 1 interaction.
IntActP0CG53. 10 interactions.
MINTMINT-1486309.

Proteomic databases

PRIDEP0CG53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022919; ENSBTAP00000022919; ENSBTAG00000017246.
GeneID281370.
KEGGbta:281370.

Organism-specific databases

CTD7314.

Phylogenomic databases

GeneTreeENSGT00750000117491.
KOK04551.
OMAVHENTRR.
OrthoDBEOG7JDR1W.
TreeFamTF300820.

Family and domain databases

InterProIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 4 hits.
PROSITEPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805375.

Entry information

Entry nameUBB_BOVIN
AccessionPrimary (citable) accession number: P0CG53
Secondary accession number(s): O97577 expand/collapse secondary AC list , P02248, P02249, P02250, P62990, P80169, Q01235, Q24K23, Q28169, Q28170, Q29120, Q3T0V5, Q3ZCE3, Q862C1, Q862F4, Q862M4, Q862T5, Q862X8, Q91887, Q91888
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: June 11, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families