P52488 · UBA2_YEAST
- ProteinUbiquitin-activating enzyme E1-like
- GeneUBA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids636 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.
Miscellaneous
Present with 18800 molecules/cell in log phase SD medium.
Pathway
Protein modification; protein sumoylation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 28-33 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGGIG | ||||||
Binding site | 52 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 60-63 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NLNR | ||||||
Binding site | 76 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 121-126 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DNLAAR | ||||||
Binding site | 162 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 165 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 177 | Glycyl thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 435 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 438 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | SUMO activating enzyme complex | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | SUMO activating enzyme activity | |
Biological Process | protein sumoylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin-activating enzyme E1-like
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP52488
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 177 | Loss of function. | ||||
Sequence: C → A or S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000194979 | 1-636 | Ubiquitin-activating enzyme E1-like | |||
Sequence: MPRETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNSKLVPYQGNVMDISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNFLFNQLFASETSGNEDDNNQDWGTDDAEEIKRIKQETNELYELQKIIISRDASRIPEILNKLFIQDINKLLAIENLWKTRTKPVPLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQKLMDRYPKEQNHIEFDKDDADTLEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYTDLNMAFTAKASNLSQNRYLSNPKLAPPNKNCPVCSKVCRGVIKLSSDCLNKMKLSDFVVLIREKYSYPQDISLLDASNQRLLFDYDFEDLNDRTLSEINLGNGSIILFSDEEGDTMIRKAIELFLDVDDELPCNTCSLPDVEVPLIKANNSPSKNEEEEKNEKGADVVATTNSHGKDGIVILDDDEGEITIDAEPINGSKKRPVDTEISEAPSNKRTKLVNEPTNSDIVELD |
Post-translational modification
Multiubiquitinated in vivo.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterodimer of UBA2 and AOS1. The complex binds SMT3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P52488 | AOS1 Q06624 | 4 | EBI-19710, EBI-15107 | |
BINARY | P52488 | SMT3 Q12306 | 2 | EBI-19710, EBI-17490 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 581-636 | Disordered | ||||
Sequence: DGIVILDDDEGEITIDAEPINGSKKRPVDTEISEAPSNKRTKLVNEPTNSDIVELD | ||||||
Compositional bias | 602-616 | Basic and acidic residues | ||||
Sequence: GSKKRPVDTEISEAP | ||||||
Motif | 619-622 | Nuclear localization signal | ||||
Sequence: KRTK |
Sequence similarities
Belongs to the ubiquitin-activating E1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length636
- Mass (Da)71,259
- Last updated1996-10-01 v1
- ChecksumDBF800E1458B3B10
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 602-616 | Basic and acidic residues | ||||
Sequence: GSKKRPVDTEISEAP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z48725 EMBL· GenBank· DDBJ | CAA88617.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z30326 EMBL· GenBank· DDBJ | CAA82980.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U17263 EMBL· GenBank· DDBJ | AAB46626.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U32274 EMBL· GenBank· DDBJ | AAB64832.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006938 EMBL· GenBank· DDBJ | DAA12234.1 EMBL· GenBank· DDBJ | Genomic DNA |