P0CG53 (UBB_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 20.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Polyubiquitin-B Cleaved into the following chain: | ||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 305 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 76 | 76 | Ubiquitin | PRO_0000396140 | |||||
| Chain | 77 – 152 | 76 | Ubiquitin | PRO_0000396141 | |||||
| Chain | 153 – 228 | 76 | Ubiquitin | PRO_0000396142 | |||||
| Chain | 229 – 304 | 76 | Ubiquitin | PRO_0000396143 | |||||
| Propeptide | 305 | 1 | PRO_0000396144 | ||||||
Regions | |||||||||
| Domain | 1 – 76 | 76 | Ubiquitin-like 1 | ||||||
| Domain | 77 – 152 | 76 | Ubiquitin-like 2 | ||||||
| Domain | 153 – 228 | 76 | Ubiquitin-like 3 | ||||||
| Domain | 229 – 304 | 76 | Ubiquitin-like 4 | ||||||
Sites | |||||||||
| Binding site | 54 | 1 | Activating enzyme | ||||||
| Binding site | 72 | 1 | Activating enzyme | ||||||
| Site | 68 | 1 | Essential for function | ||||||
Amino acid modifications | |||||||||
| Modified residue | 57 | 1 | Phosphoserine By similarity | ||||||
| Cross-link | 6 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 11 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 27 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 29 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 33 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 48 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | |||||||
| Cross-link | 63 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 76 | Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) | |||||||
Experimental info | |||||||||
| Sequence conflict | 133 | 1 | S → F in CAA79146. Ref.1 | ||||||
Sequences
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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] | 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. |
| [3] | "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. |
| [4] | "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. |
| [5] | "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. |
| [6] | "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. |
| [7] | "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] OF 149-305. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z18245 mRNA. Translation: CAA79146.1. BC114001 mRNA. Translation: AAI14002.1. M62429 mRNA. Translation: AAA30720.1. AB098769 mRNA. Translation: BAC56305.1. AB099044 mRNA. Translation: BAC56534.1. AB099083 mRNA. Translation: BAC56573.1. Different initiation. |
| IPI | IPI00786471. |
| PIR | I45964. S29853. |
| RefSeq | NP_776558.1. NM_174133.2. |
| UniGene | Bt.111403. Bt.2878. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P0CG53. 1 interaction. |
Proteomic databases | |
| PRIDE | P0CG53. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000022919; ENSBTAP00000022919; ENSBTAG00000017246. |
| GeneID | 281370. |
| KEGG | bta:281370. |
Organism-specific databases | |
| CTD | 7314. |
Phylogenomic databases | |
| GeneTree | ENSGT00550000074658. |
| OMA | VHENTRR. |
| OrthoDB | EOG4WDDB6. |
Family and domain databases | |
| InterPro | IPR000626. Ubiquitin. IPR019954. Ubiquitin_CS. IPR019956. Ubiquitin_subgr. IPR019955. Ubiquitin_supergroup. [Graphical view] |
| Pfam | PF00240. ubiquitin. 4 hits. [Graphical view] |
| PRINTS | PR00348. UBIQUITIN. |
| SMART | SM00213. UBQ. 4 hits. [Graphical view] |
| PROSITE | PS00299. UBIQUITIN_1. 4 hits. PS50053. UBIQUITIN_2. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20805375. |
Entry information
| Entry name | UBB_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P0CG53 Secondary accession number(s): O97577 Q91888 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
