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P34216

- EDE1_YEAST

UniProt

P34216 - EDE1_YEAST

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Protein

EH domain-containing and endocytosis protein 1

Gene
EDE1, BUD15, YBL047C, YBL0501, YBL0520
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
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.7 Publications

GO - Cellular componenti

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

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.

Miscellaneous databases

EvolutionaryTraceiP34216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 113100EH 1Add
BLAST
Domaini135 – 22793EH 2Add
BLAST
Domaini277 – 36690EH 3Add
BLAST
Domaini1338 – 138043UBAAdd
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 – 882290 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the VDP/USO1/EDE1 family.
Contains 3 EH domains.
Contains 1 UBA domain.

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 127 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.

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

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