Q9SJT1 · SAE2_ARATH

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.

170050100150200250300350400450500550600650700
Type
IDPosition(s)Description
Binding site19-24ATP (UniProtKB | ChEBI)
Binding site43ATP (UniProtKB | ChEBI)
Binding site51-54ATP (UniProtKB | ChEBI)
Binding site67ATP (UniProtKB | ChEBI)
Binding site112-117ATP (UniProtKB | ChEBI)
Binding site153Zn2+ (UniProtKB | ChEBI)
Binding site156Zn2+ (UniProtKB | ChEBI)
Active site168Glycyl thioester intermediate
Binding site432Zn2+ (UniProtKB | ChEBI)
Binding site435Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular Componentplasmodesma
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular FunctionSUMO activating enzyme activity
Molecular Functiontransferase activity
Biological Processembryo development ending in seed dormancy
Biological Processprotein sumoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    SUMO-activating enzyme subunit 2
  • EC number
  • Alternative names
    • Protein EMBRYO DEFECTIVE 2764
    • Ubiquitin-like 1-activating enzyme E1B

Gene names

    • Name
      SAE2
    • Synonyms
      EMB2764
    • ORF names
      F3K23.23
    • Ordered locus names
      At2g21470

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9SJT1
  • Secondary accessions
    • Q84YI5
    • Q8GYC2
    • Q8LKN2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00003960122-700SUMO-activating enzyme subunit 2
Modified residue678Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterodimer of SAE1A or SAE1B and SAE2. The complex binds SUMO proteins via SAE2 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias200-214Polar residues
Region200-224Disordered
Region614-700Disordered
Compositional bias623-652Polar residues
Compositional bias653-677Basic and acidic residues

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    700
  • Mass (Da)
    78,526
  • Last updated
    2000-05-01 v1
  • Checksum
    B96A697287F1CC1B
MATQQQQSAIKGAKVLMVGAGGIGCELLKTLALSGFEDIHIIDMDTIEVSNLNRQFLFRRSHVGQSKAKVARDAVLRFRPNINIRSYHANVKNPEFDVDFFKQFDVVLNGLDNLDARRHVNRLCLAADVPLVESGTTGFLGQVTVHIKGKTECYECQTKPAPKTYPVCTITSTPTKFVHCIVWAKDLLFAKLFGDKNQDNDLNVRSNNSASSSKETEDVFERSEDEDIEQYGRKIYDHVFGSNIEAALSNEETWKNRRRPRPIYSKDVLPESLTQQNGSTQNCSVTDGDLMVSAMPSLGLKNPQELWGLTQNSLVFIEALKLFFAKRKKEIGHLTFDKDDQLAVEFVTAAANIRAESFGIPLHSLFEAKGIAGNIVHAVATTNAIIAGLIVIEAIKVLKKDVDKFRMTYCLEHPSKKLLLMPIEPYEPNPACYVCSETPLVLEINTRKSKLRDLVDKIVKTKLGMNLPLIMHGNSLLYEVGDDLDDIMVANYNANLEKYLSELPSPILNGSILTVEDLQQELSCKINVKHRFFSEILNPVLNSVWFLIILPSTFPKLFHFTESRNQDGLSLDIILGFSNVTIRRVLTMFETGRRLTHPLLILFCHREEFDEEKEPEGMVLSGWTPSPATNGESASTSNNENPVDVTESSSGSEPASKKRRLSETEASNHKKETENVESEDDDIMEVENPMMVSKKKIRVE

Q9SJT1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4IHI1F4IHI1_ARATHSAE2628

Sequence caution

The sequence AAN03851.1 differs from that shown. Reason: Miscellaneous discrepancy Sequencing errors.

Features

Showing features for compositional bias, alternative sequence.

Type
IDPosition(s)Description
Compositional bias200-214Polar residues
Alternative sequenceVSP_039565532-606in isoform 2
Compositional bias623-652Polar residues
Compositional bias653-677Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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