P62975 (UBIQ_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 47.
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: Ubiquitin |
| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] |
| Taxonomic identifier | 9986 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 76 AA. |
| Sequence status | Complete. |
| 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 synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species. In some species there is a final amino-acid after the last repeat. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a). |
| Sequence similarities | Belongs to the ubiquitin family. Contains 1 ubiquitin-like domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| PTM | Acetylation Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 76 | 76 | Ubiquitin | PRO_0000114805 | |||||
Regions | |||||||||
| Domain | 1 – 76 | 76 | Ubiquitin-like | ||||||
Sites | |||||||||
| Binding site | 54 | 1 | Activating enzyme | ||||||
| Binding site | 72 | 1 | Activating enzyme | ||||||
| Site | 68 | 1 | Essential for function | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 48 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 57 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 65 | 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) | |||||||
Sequences
References
| [1] | "Structural characterization of rabbit brain ubiquitin." Wajih N., Siddiqi A.R., Kaiser R., Persson B., Zaidi Z.H., Joernvall H. Protein Seq. Data Anal. 5:31-32(1992) [PubMed: 1337207] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S28203. |
3D structure databases | |
| ProteinModelPortal | P62975. |
| SMR | P62975. Positions 1-76. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P62975. |
Proteomic databases | |
| PRIDE | P62975. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | maNOG18772. |
| GeneTree | ENSGT00550000074658. ENSGT00550000074763. |
| OrthoDB | EOG4PZJ82. EOG4WDDB6. |
Family and domain databases | |
| InterPro | IPR000626. Ubiquitin. IPR019954. Ubiquitin_CS. IPR019956. Ubiquitin_subgr. IPR019955. Ubiquitin_supergroup. [Graphical view] |
| Pfam | PF00240. ubiquitin. 1 hit. [Graphical view] |
| PRINTS | PR00348. UBIQUITIN. |
| SMART | SM00213. UBQ. 1 hit. [Graphical view] |
| PROSITE | PS00299. UBIQUITIN_1. 1 hit. PS50053. UBIQUITIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | UBIQ_RABIT | ||||||||
| Accession | Primary (citable) accession number: P62975 Secondary accession number(s): P02248 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