Q29504 (UBA1_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 101.
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-like modifier-activating enzyme 1 Alternative name(s): Ubiquitin-activating enzyme E1 | ||||
| Gene names |
| ||||
| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 1058 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP. |
| Pathway | |
| Subunit structure | Monomer By similarity. |
| Miscellaneous | There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site. |
| Sequence similarities | Belongs to the ubiquitin-activating E1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activityInferred from electronic annotation. Source: UniProtKB-KW small protein activating enzyme activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1058 | 1058 | Ubiquitin-like modifier-activating enzyme 1 | PRO_0000194936 | |||||
Regions | |||||||||
| Repeat | 63 – 199 | 137 | 1-1 | ||||||
| Repeat | 459 – 611 | 153 | 1-2 | ||||||
| Nucleotide binding | 478 – 507 | 30 | ATP By similarity | ||||||
| Region | 63 – 611 | 549 | 2 approximate repeats | ||||||
Sites | |||||||||
| Active site | 632 | 1 | Glycyl thioester intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 13 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 21 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 24 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 46 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 55 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 671 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 800 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 810 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 816 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 820 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 835 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 980 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Rabbit ubiquitin-activating enzyme E1: cDNA cloning, sequence and expression." Sun B., Jeyaseelan K., Chung M.C.M., Teo T.S. Gene 196:19-23(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U58653 mRNA. Translation: AAC48768.1. |
| RefSeq | NP_001075840.1. NM_001082371.2. |
| UniGene | Ocu.6207. |
3D structure databases | |
| ProteinModelPortal | Q29504. |
| SMR | Q29504. Positions 48-1057. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q29504. 7 interactions. |
| STRING | 9986.ENSOCUP00000007237. |
Proteomic databases | |
| PRIDE | Q29504. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100009225. |
Organism-specific databases | |
| CTD | 7317. |
Phylogenomic databases | |
| eggNOG | COG0476. |
| HOGENOM | HOG000167329. |
| HOVERGEN | HBG054199. |
| OrthoDB | EOG4QZ7K4. |
Enzyme and pathway databases | |
| UniPathway | UPA00143. |
Family and domain databases | |
| Gene3D | 1.10.3240.10. 1 hit. 3.40.50.720. 4 hits. |
| InterPro | IPR009036. Molybdenum_cofac_synth_MoeB. IPR016040. NAD(P)-bd_dom. IPR000594. ThiF_NAD_FAD-bd. IPR018965. Ub-activating_enz_e1_C. IPR023280. Ub-like_act_enz_cat_cys_dom. IPR000127. UBact_repeat. IPR019572. Ubiquitin-activating_enzyme. IPR018075. UBQ-activ_enz_E1. IPR018074. UBQ-activ_enz_E1_AS. IPR000011. UBQ/SUMO-activ_enz_E1-like. [Graphical view] |
| Pfam | PF00899. ThiF. 2 hits. PF09358. UBA_e1_C. 1 hit. PF10585. UBA_e1_thiolCys. 1 hit. PF02134. UBACT. 2 hits. [Graphical view] |
| PRINTS | PR01849. UBIQUITINACT. |
| SMART | SM00985. UBA_e1_C. 1 hit. [Graphical view] |
| SUPFAM | SSF69572. MoeB. 2 hits. |
| TIGRFAMs | TIGR01408. Ube1. 1 hit. |
| PROSITE | PS00536. UBIQUITIN_ACTIVAT_1. 1 hit. PS00865. UBIQUITIN_ACTIVAT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | UBA1_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q29504 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
