A4FV12 · A4FV12_BOVIN

  • Protein
    SUMO-activating enzyme subunit 2
  • Gene
    UBA2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.

Pathway

Protein modification; protein sumoylation.

Features

Showing features for binding site, active site.

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Type
IDPosition(s)Description
Binding site24-29ATP (UniProtKB | ChEBI)
Binding site48ATP (UniProtKB | ChEBI)
Binding site56-59ATP (UniProtKB | ChEBI)
Binding site72ATP (UniProtKB | ChEBI)
Binding site95-96ATP (UniProtKB | ChEBI)
Binding site117-122ATP (UniProtKB | ChEBI)
Binding site158Zn2+ (UniProtKB | ChEBI)
Binding site161Zn2+ (UniProtKB | ChEBI)
Active site173Glycyl thioester intermediate
Binding site441Zn2+ (UniProtKB | ChEBI)
Binding site444Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleoplasm
Cellular ComponentSUMO activating enzyme complex
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionprotein heterodimerization activity
Molecular Functionsmall protein activating enzyme binding
Molecular FunctionSUMO activating enzyme activity
Molecular FunctionSUMO binding
Molecular Functionubiquitin-like protein conjugating enzyme binding
Biological Processpositive regulation of protein sumoylation
Biological Processprotein sumoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    SUMO-activating enzyme subunit 2
  • EC number

Gene names

    • Name
      UBA2
    • Synonyms
      SAE2

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    A4FV12

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Cross-link190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain13-441THIF-type NAD/FAD binding fold
Region202-233Disordered
Compositional bias208-233Basic and acidic residues
Region287-306Disordered
Compositional bias288-306Polar residues
Domain452-538Ubiquitin/SUMO-activating enzyme ubiquitin-like
Domain549-630SUMO-activating enzyme subunit 2 C-terminal
Region551-628Disordered
Compositional bias563-586Polar residues
Compositional bias601-628Basic and acidic residues

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    640
  • Mass (Da)
    71,031
  • Last updated
    2007-04-17 v1
  • Checksum
    4B1946642E4AE5DA
MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEASWEPMEAEARARASNEDGDIKRVSTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETSASDQQNEPQLGLKDQQVLDVKSYACLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDAPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEGPSNNADISEEERSRKRKLDEKESVSAKRSRIEQAEELDEVIALD

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAA9SHV8A0AAA9SHV8_BOVINUBA2636
A0AAA9SUH8A0AAA9SUH8_BOVINUBA2607
A0A3Q1MG31A0A3Q1MG31_BOVINUBA2583

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias208-233Basic and acidic residues
Compositional bias288-306Polar residues
Compositional bias563-586Polar residues
Compositional bias601-628Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC123590
EMBL· GenBank· DDBJ
AAI23591.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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