P34216 · EDE1_YEAST

Function

function

Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner.

Miscellaneous

Present with 1380 molecules/cell in log phase SD medium.

Features

Showing features for binding site.

113811002003004005006007008009001,0001,1001,2001,300
TypeIDPosition(s)Description
Binding site180Ca2+ (UniProtKB | ChEBI)
Binding site182Ca2+ (UniProtKB | ChEBI)
Binding site184Ca2+ (UniProtKB | ChEBI)
Binding site191Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentactin cortical patch
Cellular Componentcellular bud neck
Cellular Componentcellular bud tip
Cellular Componentcytoplasm
Cellular Componentmating projection tip
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functionubiquitin binding
Biological Processactin cortical patch organization
Biological Processendocytosis
Biological Processendoplasmic reticulum unfolded protein response
Biological Processendosomal transport
Biological Processpositive regulation of cytokinesis
Biological Processregulation of protein localization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    EH domain-containing and endocytosis protein 1
  • Alternative names
    • Bud site selection protein 15

Gene names

    • Name
      EDE1
    • Synonyms
      BUD15
    • ORF names
      YBL0501, YBL0520
    • Ordered locus names
      YBL047C

Organism names

Accessions

  • Primary accession
    P34216
  • Secondary accessions
    • D6VPV1

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Note: Localized to actin cortical patches concentrated in the developing bud tip in cells with small buds and at the mother-daughter neck in cells undergoing cytokinesis. Localization can be maintained in the absence of polymerized actin filaments.

Keywords

Phenotypes & Variants

Disruption phenotype

Random budding pattern and morphological defects. Defects in fluid-phase endocytosis and defective internalization of the pheromone alpha-factor and uracil permease. Deletion has only a small impact on actin cytoskeleton organization. Deletion shows synthetic growth defects with thermosensitive mutants of PAN1, END3 and RSP5.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis56Abnormal spatiotemporal behavior.
Mutagenesis176Abnormal spatiotemporal behavior.
Mutagenesis319Abnormal spatiotemporal behavior.
Mutagenesis1352Reduced ubiquitin-binding.
Mutagenesis1370Reduced ubiquitin-binding.
Mutagenesis1374Enhanced ubiquitin-binding.
Mutagenesis1378Reduced ubiquitin-binding.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

Type
IDPosition(s)Description
ChainPRO_00002024571-1381EH domain-containing and endocytosis protein 1
Modified residue238Phosphothreonine
Modified residue241Phosphoserine
Modified residue244Phosphoserine
Modified residue245Phosphothreonine
Modified residue248Phosphoserine
Modified residue249Phosphoserine
Modified residue251Phosphothreonine
Modified residue265Phosphoserine
Modified residue419Phosphoserine
Modified residue450Phosphothreonine
Modified residue477Phosphothreonine
Modified residue487Phosphothreonine
Modified residue495Phosphoserine
Cross-link674Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue848Phosphoserine
Modified residue931Phosphoserine
Modified residue950Phosphoserine
Modified residue964Phosphoserine
Modified residue1008Phosphoserine
Modified residue1012Phosphoserine
Modified residue1020Phosphoserine
Modified residue1046Phosphothreonine
Modified residue1069Phosphoserine
Modified residue1087Phosphoserine
Modified residue1093Phosphoserine
Modified residue1095Phosphoserine
Modified residue1096Phosphoserine
Modified residue1100Phosphoserine
Modified residue1111Phosphothreonine
Modified residue1181Phosphoserine
Modified residue1187Phosphoserine
Modified residue1307Phosphothreonine
Cross-link1329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue1343Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts (via UBA domain) with monoubiquitin and ENT1 (via asparagine-proline-phenylalanine tripeptide motif called NPF). Interacts with PAL1 and SYP1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P34216SYP1 P256237EBI-21243, EBI-21900

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, compositional bias, region, coiled coil.

Type
IDPosition(s)Description
Domain14-113EH 1
Domain47-82EF-hand 1
Domain135-227EH 2
Domain167-202EF-hand 2
Domain276-311EF-hand 3
Domain277-366EH 3
Compositional bias389-497Polar residues
Region389-535Disordered
Coiled coil593-882
Region898-919Disordered
Region933-1202Disordered
Compositional bias935-954Basic and acidic residues
Compositional bias957-992Polar residues
Compositional bias1003-1019Polar residues
Compositional bias1025-1039Basic and acidic residues
Compositional bias1062-1107Polar residues
Compositional bias1145-1167Polar residues
Compositional bias1174-1194Polar residues
Region1214-1285Disordered
Region1217-1381Able to bind biological membranes
Compositional bias1253-1284Polar residues
Region1298-1322Disordered
Domain1338-1380UBA

Sequence similarities

Belongs to the VDP/USO1/EDE1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,381
  • Mass (Da)
    150,783
  • Last updated
    1994-10-01 v2
  • Checksum
    626FD261DCBA7D99
MASITFRTPLSSQEQAFYNQKFHQLDTEDLGVVTGEAVRPLFASSGLPGQLLSQVWATVDIDNKGFLNLNEFSAALRMIAQLQNAPNQPISAALYESTPTQLASFSINQNPAPMQSGSATGNTNNTDIPALSSNDIAKFSQLFDRTAKGAQTVAGDKAKDIFLKARLPNQTLGEIWALCDRDASGVLDKSEFIMAMYLIQLCMSHHPSMNTPPAVLPTQLWDSIRLEPVVVNQPNRTTPLSANSTGVSSLTRHSTISRLSTGAFSNAASDWSLSFEKKQQFDAIFDSLDKQHAGSLSSAVLVPFFLSSRLNQETLATIWDLADIHNNAEFTKLEFAIAMFLIQKKNAGVELPDVIPNELLQSPALGLYPPNPLPQQQSAPQIAIPSRASKPSLQDMPHQVSAPAVNTQPTVPQVLPQNSNNGSLNDLLALNPSFSSPSPTKAQTVVQNNTNNSFSYDNNNGQATLQQQQPQQPPPLTHSSSGLKKFTPTSNFGQSIIKEEPEEQEQLRESSDTFSAQPPPVPKHASSPVKRTASTTLPQVPNFSVFSMPAGAATSAATGAAVGAAVGAAALGASAFSRSSNNAFKNQDLFADGEASAQLSNATTEMANLSNQVNSLSKQASITNDKKSRATQELKRVTEMKNSIQIKLNNLRSTHDQNVKQTEQLEAQVLQVNKENETLAQQLAVSEANYHAAESKLNELTTDLQESQTKNAELKEQITNLNSMTASLQSQLNEKQQQVKQERSMVDVNSKQLELNQVTVANLQKEIDGLGEKISVYLTKQKELNDYQKTVEEQHAQLQAKYQDLSNKDTDLTDREKQLEERNRQIEEQENLYHQHVSKLQEMFDDLSQRKASFEKADQELKERNIEYANNVRELSERQMNLAMGQLPEDAKDIIAKSASNTDTTTKEATSRGNVHEDTVSKFVETTVENSNLNVNRVKDDEEKTERTESDVFDRDVPTLGSQSDSENANTNNGTQSGNETANPNLTETLSDRFDGDLNEYGIPRSQSLTSSVANNAPQSVRDDVELPETLEERDTINNTANRDNTGNLSHIPGEWEATPATASTDVLSNETTEVIEDGSTTKRANSNEDGESVSSIQESPKISAQPKAKTINEEFPPIQELHIDESDSSSSDDDEFEDTREIPSATVKTLQTPYNAQPTSSLEIHTEQVIKYPAPGTSPSHNEGNSKKASTNSILPVKDEFDDEFAGLEQAAVEEDNGADSESEFENVANAGSMEQFETIDHKDLDDELQMNAFTGTLTSSSNPTIPKPQVQQQSTSDPAQVSNDEWDEIFAGFGNSKAEPTKVATPSIPQQPIPLKNDPIVDASLSKGPIVNRGVATTPKSLAVEELSGMGFTEEEAHNALEKCNWDLEAATNFLLDSA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias389-497Polar residues
Compositional bias935-954Basic and acidic residues
Compositional bias957-992Polar residues
Compositional bias1003-1019Polar residues
Compositional bias1025-1039Basic and acidic residues
Compositional bias1062-1107Polar residues
Compositional bias1145-1167Polar residues
Compositional bias1174-1194Polar residues
Compositional bias1253-1284Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z35808
EMBL· GenBank· DDBJ
CAA84867.1
EMBL· GenBank· DDBJ
Genomic DNA
X78214
EMBL· GenBank· DDBJ
CAA55048.1
EMBL· GenBank· DDBJ
Genomic DNA
Z23261
EMBL· GenBank· DDBJ
CAA80797.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006936
EMBL· GenBank· DDBJ
DAA07071.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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