B8N7E5 · RSP5_ASPFN

Function

function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.26 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for active site.

1812100200300400500600700800
TypeIDPosition(s)Description
Active site780Glycyl thioester intermediate

GO annotations

AspectTerm
Cellular Componentcellular bud tip
Cellular Componentcytosolic ribosome
Cellular Componentendosome membrane
Cellular ComponentGolgi apparatus
Cellular Componentnucleus
Cellular ComponentRSP5-BUL ubiquitin ligase complex
Cellular Componentubiquitin ligase complex
Molecular Functionphosphatidylinositol binding
Molecular Functionubiquitin binding
Molecular Functionubiquitin protein ligase activity
Biological Processchromatin organization
Biological Processlate endosome to vacuole transport via multivesicular body sorting pathway
Biological Processmitochondria-associated ubiquitin-dependent protein catabolic process
Biological Processmitochondrion organization
Biological Processnonfunctional rRNA decay
Biological Processpoly(A)+ mRNA export from nucleus
Biological Processpositive regulation of fatty acid biosynthetic process
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processpositive regulation of receptor-mediated endocytosis
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processprotein K63-linked ubiquitination
Biological Processregulation of actin cytoskeleton organization
Biological Processregulation of dolichol biosynthetic process
Biological Processregulation of ergosterol biosynthetic process
Biological Processregulation of mRNA export from nucleus
Biological Processregulation of multivesicular body size
Biological Processregulation of nitrogen utilization
Biological Processregulation of phosphate metabolic process
Biological Processregulation of protein localization
Biological Processregulation of ribosomal large subunit export from nucleus
Biological Processregulation of rRNA processing
Biological Processregulation of tRNA export from nucleus
Biological Processregulation of tRNA processing
Biological Processregulation of ubiquinone biosynthetic process
Biological Processribophagy
Biological Processubiquitin-dependent endocytosis
Biological Processubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable E3 ubiquitin-protein ligase hulA
  • EC number
  • Alternative names
    • HECT ubiquitin ligase A
    • HECT-type E3 ubiquitin transferase hulA

Gene names

    • Name
      hulA
    • ORF names
      AFLA_021670

Organism names

Accessions

  • Primary accession
    B8N7E5

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003957051-812Probable E3 ubiquitin-protein ligase hulA

Interaction

Subunit

Interacts with creD.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain1-109C2
Compositional bias131-168Polar residues
Region131-235Disordered
Compositional bias175-199Polar residues
Compositional bias208-224Polar residues
Domain226-259WW 1
Compositional bias250-271Polar residues
Region250-350Disordered
Compositional bias272-286Basic and acidic residues
Compositional bias288-325Polar residues
Domain330-363WW 2
Domain390-423WW 3
Domain479-812HECT

Sequence similarities

Belongs to the RSP5/NEDD4 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    812
  • Mass (Da)
    92,148
  • Last updated
    2009-03-03 v1
  • Checksum
    0D0244666099CC99
MTCSQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHMQPSTSSGLVPQVSASTPQPSPGPSQADPTASNPSLHPQRVPSTTRPSSTIVPANGPPAPPNGQQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSNNYNEQTSRTQREASMQLERRAHQSRMLPEDRTGASSPNLQENQQQAQTPPAGGSASAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGIIELTFAVDDEKFGERRTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPGALPKSHTCFNRLDLPPYKTNDVLEHKLSIAVEETLGFGQE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias131-168Polar residues
Compositional bias175-199Polar residues
Compositional bias208-224Polar residues
Compositional bias250-271Polar residues
Compositional bias272-286Basic and acidic residues
Compositional bias288-325Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EQ963474
EMBL· GenBank· DDBJ
EED54915.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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