Q5U300 (UBA1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 79.
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 |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 1058 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein 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 By similarity. |
| Pathway | |
| Subunit structure | Monomer. Interacts with GAN (via BTB domain) By similarity. UniProtKB Q02053 |
| Post-translational modification | ISGylated 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 Ubl conjugation |
| 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_0000365096 | |||||
Regions | |||||||||
| Repeat | 63 – 199 | 137 | 1-1 | ||||||
| Repeat | 459 – 611 | 153 | 1-2 | ||||||
| Nucleotide binding | 478 – 507 | 30 | ATP By similarity UniProtKB Q02053 | ||||||
| Region | 63 – 611 | 549 | 2 approximate repeats | ||||||
Sites | |||||||||
| Active site | 632 | 1 | Glycyl thioester intermediate By similarity UniProtKB Q02053 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 13 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 21 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 24 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 46 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 55 | 1 | Phosphotyrosine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 671 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 800 | 1 | Phosphothreonine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 810 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 816 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 820 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 835 | 1 | Phosphoserine By similarity UniProtKB Q02053 | ||||||
| Modified residue | 980 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Brown Norway. Tissue: Kidney. |
| [3] | Maurya D.K., Bhargava P. Submitted (JAN-2009) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH474009 Genomic DNA. Translation: EDL97701.1. CH474009 Genomic DNA. Translation: EDL97702.1. BC085791 mRNA. Translation: AAH85791.1. |
| IPI | IPI00368347. |
| RefSeq | NP_001014102.1. NM_001014080.1. |
| UniGene | Rn.11800. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1Z7L based on UniProtKB Q02053. |
| ProteinModelPortal | Q5U300. |
| SMR | Q5U300. Positions 48-1057. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000033950. |
PTM databases | |
| PhosphoSite | Q5U300. |
Proteomic databases | |
| PaxDb | Q5U300. |
| PRIDE | Q5U300. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000031115; ENSRNOP00000033950; ENSRNOG00000019164. |
| GeneID | 314432. |
| KEGG | rno:314432. |
| UCSC | RGD:1359327. rat. |
Organism-specific databases | |
| CTD | 7317. |
| RGD | 1359327. Uba1. |
Phylogenomic databases | |
| eggNOG | COG0476. |
| GeneTree | ENSGT00390000016689. |
| HOGENOM | HOG000167329. |
| HOVERGEN | HBG054199. |
| InParanoid | Q5U300. |
| KO | K03178. |
| OMA | FESGDYV. |
| OrthoDB | EOG4QZ7K4. |
Enzyme and pathway databases | |
| UniPathway | UPA00143. |
Gene expression databases | |
| Genevestigator | Q5U300. |
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... |
Other | |
| NextBio | 667673. |
Entry information
| Entry name | UBA1_RAT | ||||||||
| Accession | Primary (citable) accession number: Q5U300 | ||||||||
| Entry history |
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| 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
