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P34216

- EDE1_YEAST

UniProt

P34216 - EDE1_YEAST

Protein

EH domain-containing and endocytosis protein 1

Gene

EDE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. ubiquitin binding Source: SGD

    GO - Biological processi

    1. endocytosis Source: SGD
    2. endoplasmic reticulum unfolded protein response Source: SGD

    Keywords - Biological processi

    Endocytosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28947-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EH domain-containing and endocytosis protein 1
    Alternative name(s):
    Bud site selection protein 15
    Gene namesi
    Name:EDE1
    Synonyms:BUD15
    Ordered Locus Names:YBL047C
    ORF Names:YBL0501, YBL0520
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL047c.
    SGDiS000000143. EDE1.

    Subcellular locationi

    Cytoplasm 7 Publications
    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.

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. cellular bud neck Source: SGD
    3. cellular bud tip Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    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 RSP5.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561W → A: Abnormal spatiotemporal behavior. 1 Publication
    Mutagenesisi176 – 1761W → A: Abnormal spatiotemporal behavior. 1 Publication
    Mutagenesisi319 – 3191W → A: Abnormal spatiotemporal behavior. 1 Publication
    Mutagenesisi1352 – 13521M → A: Reduced ubiquitin-binding. 1 Publication
    Mutagenesisi1370 – 13701L → A: Reduced ubiquitin-binding. 1 Publication
    Mutagenesisi1374 – 13741T → A: Enhanced ubiquitin-binding. 1 Publication
    Mutagenesisi1378 – 13781L → A: Reduced ubiquitin-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13811381EH domain-containing and endocytosis protein 1PRO_0000202457Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei238 – 2381Phosphothreonine1 Publication
    Modified residuei241 – 2411Phosphoserine4 Publications
    Modified residuei244 – 2441Phosphoserine2 Publications
    Modified residuei245 – 2451Phosphothreonine2 Publications
    Modified residuei248 – 2481Phosphoserine2 Publications
    Modified residuei249 – 2491Phosphoserine1 Publication
    Modified residuei251 – 2511Phosphothreonine1 Publication
    Modified residuei265 – 2651Phosphoserine1 Publication
    Modified residuei419 – 4191Phosphoserine1 Publication
    Modified residuei450 – 4501Phosphothreonine1 Publication
    Modified residuei477 – 4771Phosphothreonine1 Publication
    Modified residuei487 – 4871Phosphothreonine1 Publication
    Modified residuei495 – 4951Phosphoserine2 Publications
    Modified residuei848 – 8481Phosphoserine1 Publication
    Modified residuei931 – 9311Phosphoserine2 Publications
    Modified residuei950 – 9501Phosphoserine1 Publication
    Modified residuei964 – 9641Phosphoserine1 Publication
    Modified residuei1008 – 10081Phosphoserine1 Publication
    Modified residuei1012 – 10121Phosphoserine1 Publication
    Modified residuei1020 – 10201Phosphoserine1 Publication
    Modified residuei1046 – 10461Phosphothreonine1 Publication
    Modified residuei1069 – 10691Phosphoserine1 Publication
    Modified residuei1087 – 10871Phosphoserine2 Publications
    Modified residuei1093 – 10931Phosphoserine4 Publications
    Modified residuei1095 – 10951Phosphoserine1 Publication
    Modified residuei1096 – 10961Phosphoserine2 Publications
    Modified residuei1100 – 11001Phosphoserine4 Publications
    Modified residuei1111 – 11111Phosphothreonine1 Publication
    Modified residuei1181 – 11811Phosphoserine1 Publication
    Modified residuei1187 – 11871Phosphoserine1 Publication
    Modified residuei1307 – 13071Phosphothreonine2 Publications
    Modified residuei1343 – 13431Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP34216.
    PaxDbiP34216.
    PeptideAtlasiP34216.

    Expressioni

    Gene expression databases

    GenevestigatoriP34216.

    Interactioni

    Subunit structurei

    Interacts (via UBA domain) with monoubiquitin and ENT1 (via asparagine-proline-phenylalanine tripeptide motif called NPF). Interacts with PAL1 and SYP1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SYP1P256237EBI-21243,EBI-21900

    Protein-protein interaction databases

    BioGridi32650. 160 interactions.
    DIPiDIP-5817N.
    IntActiP34216. 22 interactions.
    MINTiMINT-627966.
    STRINGi4932.YBL047C.

    Structurei

    Secondary structure

    1
    1381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1341 – 135010
    Turni1351 – 13533
    Helixi1356 – 136510
    Helixi1370 – 13789

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G3QNMR-A1339-1381[»]
    ProteinModelPortaliP34216.
    SMRiP34216. Positions 10-79, 138-225, 271-352, 1339-1381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34216.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 113100EH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 22793EH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini277 – 36690EH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1338 – 138043UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1217 – 1381165Able to bind biological membranesAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili593 – 882290Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi550 – 57526Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the VDP/USO1/EDE1 family.Curated
    Contains 3 EH domains.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG301764.
    GeneTreeiENSGT00750000117388.
    HOGENOMiHOG000112328.
    OMAiRELDYQE.
    OrthoDBiEOG7XWPWW.

    Family and domain databases

    Gene3Di1.10.238.10. 3 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PfamiPF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    SM00027. EH. 3 hits.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 3 hits.
    PS50031. EH. 3 hits.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P34216-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ     50
    LLSQVWATVD IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT 100
    QLASFSINQN PAPMQSGSAT GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA 150
    QTVAGDKAKD IFLKARLPNQ TLGEIWALCD RDASGVLDKS EFIMAMYLIQ 200
    LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL SANSTGVSSL 250
    TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV 300
    LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE 350
    LPDVIPNELL QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV 400
    SAPAVNTQPT VPQVLPQNSN NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT 450
    NNSFSYDNNN GQATLQQQQP QQPPPLTHSS SGLKKFTPTS NFGQSIIKEE 500
    PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV PNFSVFSMPA 550
    GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS 600
    NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN 650
    LRSTHDQNVK QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL 700
    TTDLQESQTK NAELKEQITN LNSMTASLQS QLNEKQQQVK QERSMVDVNS 750
    KQLELNQVTV ANLQKEIDGL GEKISVYLTK QKELNDYQKT VEEQHAQLQA 800
    KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL QEMFDDLSQR 850
    KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS 900
    NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES 950
    DVFDRDVPTL GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE 1000
    YGIPRSQSLT SSVANNAPQS VRDDVELPET LEERDTINNT ANRDNTGNLS 1050
    HIPGEWEATP ATASTDVLSN ETTEVIEDGS TTKRANSNED GESVSSIQES 1100
    PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT REIPSATVKT 1150
    LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD 1200
    EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL 1250
    QMNAFTGTLT SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA 1300
    EPTKVATPSI PQQPIPLKND PIVDASLSKG PIVNRGVATT PKSLAVEELS 1350
    GMGFTEEEAH NALEKCNWDL EAATNFLLDS A 1381
    Length:1,381
    Mass (Da):150,783
    Last modified:October 1, 1994 - v2
    Checksum:i626FD261DCBA7D99
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35808 Genomic DNA. Translation: CAA84867.1.
    X78214 Genomic DNA. Translation: CAA55048.1.
    Z23261 Genomic DNA. Translation: CAA80797.1.
    BK006936 Genomic DNA. Translation: DAA07071.1.
    PIRiS45781.
    RefSeqiNP_009506.1. NM_001178287.1.

    Genome annotation databases

    EnsemblFungiiYBL047C; YBL047C; YBL047C.
    GeneIDi852233.
    KEGGisce:YBL047C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35808 Genomic DNA. Translation: CAA84867.1 .
    X78214 Genomic DNA. Translation: CAA55048.1 .
    Z23261 Genomic DNA. Translation: CAA80797.1 .
    BK006936 Genomic DNA. Translation: DAA07071.1 .
    PIRi S45781.
    RefSeqi NP_009506.1. NM_001178287.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G3Q NMR - A 1339-1381 [» ]
    ProteinModelPortali P34216.
    SMRi P34216. Positions 10-79, 138-225, 271-352, 1339-1381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32650. 160 interactions.
    DIPi DIP-5817N.
    IntActi P34216. 22 interactions.
    MINTi MINT-627966.
    STRINGi 4932.YBL047C.

    Proteomic databases

    MaxQBi P34216.
    PaxDbi P34216.
    PeptideAtlasi P34216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL047C ; YBL047C ; YBL047C .
    GeneIDi 852233.
    KEGGi sce:YBL047C.

    Organism-specific databases

    CYGDi YBL047c.
    SGDi S000000143. EDE1.

    Phylogenomic databases

    eggNOGi NOG301764.
    GeneTreei ENSGT00750000117388.
    HOGENOMi HOG000112328.
    OMAi RELDYQE.
    OrthoDBi EOG7XWPWW.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28947-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P34216.
    NextBioi 970769.

    Gene expression databases

    Genevestigatori P34216.

    Family and domain databases

    Gene3Di 1.10.238.10. 3 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    Pfami PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    SM00027. EH. 3 hits.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 3 hits.
    PS50031. EH. 3 hits.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein."
      de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A.
      Yeast 10:1489-1496(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-961.
      Strain: ATCC 204508 / S288c.
    4. "Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes."
      Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.
      Yeast 9:1355-1371(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 579-1381.
      Strain: ATCC 204508 / S288c.
    5. "A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis."
      Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H., Haguenauer-Tsapis R.
      J. Cell Sci. 113:3309-3319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    6. "A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae."
      Ni L., Snyder M.
      Mol. Biol. Cell 12:2147-2170(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    7. "The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions."
      Aguilar R.C., Watson H.A., Wendland B.
      J. Biol. Chem. 278:10737-10743(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBIQUITIN AND ENT1, REGION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A modular design for the clathrin- and actin-mediated endocytosis machinery."
      Kaksonen M., Toret C.P., Drubin D.G.
      Cell 123:305-320(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION MUTANT.
    11. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    12. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238; SER-241; SER-244; THR-245; SER-248; SER-249; THR-487; SER-1093; SER-1096; SER-1100 AND THR-1307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    13. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Interaction between Epsin/Yap180 adaptors and the scaffolds Ede1/Pan1 is required for endocytosis."
      Maldonado-Baez L., Dores M.R., Perkins E.M., Drivas T.G., Hicke L., Wendland B.
      Mol. Biol. Cell 19:2936-2948(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-56; TRP-176 AND TRP-319.
    15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-265; SER-419; SER-495; SER-848; SER-931; SER-950; SER-1069; SER-1087; SER-1093; SER-1100; THR-1111 AND THR-1307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-244; THR-245; SER-248; THR-251; THR-450; THR-477; SER-495; SER-931; SER-964; SER-1008; SER-1012; SER-1020; THR-1046; SER-1087; SER-1093; SER-1095; SER-1096; SER-1100; SER-1181; SER-1187 AND SER-1343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Analysis of yeast endocytic site formation and maturation through a regulatory transition point."
      Carroll S.Y., Stimpson H.E., Weinberg J., Toret C.P., Sun Y., Drubin D.G.
      Mol. Biol. Cell 23:657-668(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PAL1.
    18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structural basis for monoubiquitin recognition by the Ede1 UBA domain."
      Swanson K.A., Hicke L., Radhakrishnan I.
      J. Mol. Biol. 358:713-724(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1339-1381 IN COMPLEX WITH MONOUBIQUITIN, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MONOUBIQUITIN, UBA DOMAIN, MUTAGENESIS OF MET-1352; LEU-1370; THR-1374 AND LEU-1378.
    20. "Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation."
      Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L., Hurley J.H., Traub L.M., Wendland B.
      EMBO J. 28:3103-3116(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYP1, SUBCELLULAR LOCATION, FUNCTION.
    21. "Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast."
      Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G.
      Mol. Biol. Cell 20:4640-4651(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiEDE1_YEAST
    AccessioniPrimary (citable) accession number: P34216
    Secondary accession number(s): D6VPV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1380 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3