Q9SJT1 · SAE2_ARATH
- ProteinSUMO-activating enzyme subunit 2
- GeneSAE2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids700 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.
Pathway
Protein modification; protein sumoylation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 19-24 | ATP (UniProtKB | ChEBI) | |||
Binding site | 43 | ATP (UniProtKB | ChEBI) | |||
Binding site | 51-54 | ATP (UniProtKB | ChEBI) | |||
Binding site | 67 | ATP (UniProtKB | ChEBI) | |||
Binding site | 112-117 | ATP (UniProtKB | ChEBI) | |||
Binding site | 153 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 156 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 168 | Glycyl thioester intermediate | |||
Binding site | 432 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 435 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | plasmodesma | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | SUMO activating enzyme activity | |
Molecular Function | transferase activity | |
Biological Process | embryo development ending in seed dormancy | |
Biological Process | protein sumoylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSUMO-activating enzyme subunit 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SJT1
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Embryonic lethal.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 50 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylalanine | |||
Chain | PRO_0000396012 | 2-700 | SUMO-activating enzyme subunit 2 | ||
Modified residue | 678 | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 200-214 | Polar residues | |||
Region | 200-224 | Disordered | |||
Region | 614-700 | Disordered | |||
Compositional bias | 623-652 | Polar residues | |||
Compositional bias | 653-677 | Basic and acidic residues | |||
Sequence similarities
Belongs to the ubiquitin-activating E1 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9SJT1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length700
- Mass (Da)78,526
- Last updated2000-05-01 v1
- ChecksumB96A697287F1CC1B
Q9SJT1-2
- Name2
- Differences from canonical
- 532-606: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4IHI1 | F4IHI1_ARATH | SAE2 | 628 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 200-214 | Polar residues | |||
Alternative sequence | VSP_039565 | 532-606 | in isoform 2 | ||
Compositional bias | 623-652 | Polar residues | |||
Compositional bias | 653-677 | Basic and acidic residues | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006841 EMBL· GenBank· DDBJ | AAD23691.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC07181.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC07182.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117731 EMBL· GenBank· DDBJ | BAC42380.1 EMBL· GenBank· DDBJ | mRNA | ||
BT044606 EMBL· GenBank· DDBJ | ACI31306.1 EMBL· GenBank· DDBJ | mRNA | ||
AF510525 EMBL· GenBank· DDBJ | AAN03851.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AJ520102 EMBL· GenBank· DDBJ | CAD67688.1 EMBL· GenBank· DDBJ | mRNA |