P52488 · UBA2_YEAST

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.

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TypeIDPosition(s)Description
Binding site28-33ATP (UniProtKB | ChEBI)
Binding site52ATP (UniProtKB | ChEBI)
Binding site60-63ATP (UniProtKB | ChEBI)
Binding site76ATP (UniProtKB | ChEBI)
Binding site121-126ATP (UniProtKB | ChEBI)
Binding site162Zn2+ (UniProtKB | ChEBI)
Binding site165Zn2+ (UniProtKB | ChEBI)
Active site177Glycyl thioester intermediate
Binding site435Zn2+ (UniProtKB | ChEBI)
Binding site438Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular ComponentSUMO activating enzyme complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular FunctionSUMO activating enzyme activity
Biological Processprotein sumoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin-activating enzyme E1-like
  • Alternative names
    • Polymerase-interacting protein 2
    • SMT3-activating enzyme subunit 2

Gene names

    • Name
      UBA2
    • Synonyms
      PIP2, UAL1
    • ORF names
      D9509.10
    • Ordered locus names
      YDR390C

Organism names

Accessions

  • Primary accession
    P52488
  • Secondary accessions
    • D6VT24

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis177Loss of function.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001949791-636Ubiquitin-activating enzyme E1-like

Post-translational modification

Multiubiquitinated in vivo.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Heterodimer of UBA2 and AOS1. The complex binds SMT3.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P52488AOS1 Q066244EBI-19710, EBI-15107
BINARY P52488SMT3 Q123062EBI-19710, EBI-17490

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region581-636Disordered
Compositional bias602-616Basic and acidic residues
Motif619-622Nuclear localization signal

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    636
  • Mass (Da)
    71,259
  • Last updated
    1996-10-01 v1
  • Checksum
    DBF800E1458B3B10
MPRETSLVTIIGEDSYKKLRSSRCLLVGAGGIGSELLKDIILMEFGEIHIVDLDTIDLSNLNRQFLFRQKDIKQPKSTTAVKAVQHFNNSKLVPYQGNVMDISTFPLHWFEQFDIIFNALDNLAARRYVNKISQFLSLPLIESGTAGFDGYMQPIIPGKTECFECTKKETPKTFPVCTIRSTPSQPIHCIVWAKNFLFNQLFASETSGNEDDNNQDWGTDDAEEIKRIKQETNELYELQKIIISRDASRIPEILNKLFIQDINKLLAIENLWKTRTKPVPLSDSQINTPTKTAQSASNSVGTIQEQISNFINITQKLMDRYPKEQNHIEFDKDDADTLEFVATAANIRSHIFNIPMKSVFDIKQIAGNIIPAIATTNAIVAGASSLISLRVLNLLKYAPTTKYTDLNMAFTAKASNLSQNRYLSNPKLAPPNKNCPVCSKVCRGVIKLSSDCLNKMKLSDFVVLIREKYSYPQDISLLDASNQRLLFDYDFEDLNDRTLSEINLGNGSIILFSDEEGDTMIRKAIELFLDVDDELPCNTCSLPDVEVPLIKANNSPSKNEEEEKNEKGADVVATTNSHGKDGIVILDDDEGEITIDAEPINGSKKRPVDTEISEAPSNKRTKLVNEPTNSDIVELD

Sequence caution

The sequence CAA82980.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias602-616Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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