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Protein

EH domain-containing and endocytosis protein 1

Gene

EDE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • ubiquitin binding Source: SGD

GO - Biological processi

  • actin cortical patch organization Source: SGD
  • endocytosis Source: SGD
  • endoplasmic reticulum unfolded protein response Source: SGD
  • positive regulation of cytokinesis Source: SGD
  • regulation of protein localization Source: SGD

Keywordsi

Biological processEndocytosis

Enzyme and pathway databases

BioCyciYEAST:G3O-28947-MONOMER
ReactomeiR-SCE-193648 NRAGE signals death through JNK
R-SCE-194840 Rho GTPase cycle
R-SCE-416482 G alpha (12/13) signalling events
R-SCE-8856825 Cargo recognition for clathrin-mediated endocytosis

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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL047C
SGDiS000000143 EDE1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi56W → A: Abnormal spatiotemporal behavior. 1 Publication1
Mutagenesisi176W → A: Abnormal spatiotemporal behavior. 1 Publication1
Mutagenesisi319W → A: Abnormal spatiotemporal behavior. 1 Publication1
Mutagenesisi1352M → A: Reduced ubiquitin-binding. 1 Publication1
Mutagenesisi1370L → A: Reduced ubiquitin-binding. 1 Publication1
Mutagenesisi1374T → A: Enhanced ubiquitin-binding. 1 Publication1
Mutagenesisi1378L → A: Reduced ubiquitin-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002024571 – 1381EH domain-containing and endocytosis protein 1Add BLAST1381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei238PhosphothreonineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei244PhosphoserineCombined sources1
Modified residuei245PhosphothreonineCombined sources1
Modified residuei248PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei251PhosphothreonineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei450PhosphothreonineCombined sources1
Modified residuei477PhosphothreonineCombined sources1
Modified residuei487PhosphothreonineCombined sources1
Modified residuei495PhosphoserineCombined sources1
Cross-linki674Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei848PhosphoserineCombined sources1
Modified residuei931PhosphoserineCombined sources1
Modified residuei950PhosphoserineCombined sources1
Modified residuei964PhosphoserineCombined sources1
Modified residuei1008PhosphoserineCombined sources1
Modified residuei1012PhosphoserineCombined sources1
Modified residuei1020PhosphoserineCombined sources1
Modified residuei1046PhosphothreonineCombined sources1
Modified residuei1069PhosphoserineCombined sources1
Modified residuei1087PhosphoserineCombined sources1
Modified residuei1093PhosphoserineCombined sources1
Modified residuei1095PhosphoserineCombined sources1
Modified residuei1096PhosphoserineCombined sources1
Modified residuei1100PhosphoserineCombined sources1
Modified residuei1111PhosphothreonineCombined sources1
Modified residuei1181PhosphoserineCombined sources1
Modified residuei1187PhosphoserineCombined sources1
Modified residuei1307PhosphothreonineCombined sources1
Cross-linki1329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei1343PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP34216
PaxDbiP34216
PRIDEiP34216

PTM databases

iPTMnetiP34216

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

GO - Molecular functioni

  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi32650, 252 interactors
DIPiDIP-5817N
IntActiP34216, 31 interactors
MINTiP34216
STRINGi4932.YBL047C

Structurei

Secondary structure

11381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1341 – 1350Combined sources10
Turni1351 – 1353Combined sources3
Helixi1356 – 1365Combined sources10
Helixi1370 – 1378Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G3QNMR-A1339-1381[»]
ProteinModelPortaliP34216
SMRiP34216
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34216

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 113EH 1PROSITE-ProRule annotationAdd BLAST100
Domaini135 – 227EH 2PROSITE-ProRule annotationAdd BLAST93
Domaini277 – 366EH 3PROSITE-ProRule annotationAdd BLAST90
Domaini1338 – 1380UBAPROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1217 – 1381Able to bind biological membranesAdd BLAST165

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili593 – 882Sequence analysisAdd BLAST290

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi550 – 575Ala-richAdd BLAST26

Sequence similaritiesi

Belongs to the VDP/USO1/EDE1 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00760000118985
HOGENOMiHOG000112328
InParanoidiP34216
KOiK12472
OMAiNDEWEQL
OrthoDBiEOG092C055E

Family and domain databases

InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR000261 EH_dom
IPR015940 UBA
IPR009060 UBA-like_sf
PfamiView protein in Pfam
PF12763 EF-hand_4, 3 hits
PF00627 UBA, 1 hit
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SM00027 EH, 3 hits
SM00165 UBA, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF47473 SSF47473, 3 hits
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 3 hits
PS50031 EH, 3 hits
PS50030 UBA, 1 hit

Sequencei

Sequence statusi: Complete.

P34216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ
60 70 80 90 100
LLSQVWATVD IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT
110 120 130 140 150
QLASFSINQN PAPMQSGSAT GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA
160 170 180 190 200
QTVAGDKAKD IFLKARLPNQ TLGEIWALCD RDASGVLDKS EFIMAMYLIQ
210 220 230 240 250
LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL SANSTGVSSL
260 270 280 290 300
TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV
310 320 330 340 350
LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE
360 370 380 390 400
LPDVIPNELL QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV
410 420 430 440 450
SAPAVNTQPT VPQVLPQNSN NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT
460 470 480 490 500
NNSFSYDNNN GQATLQQQQP QQPPPLTHSS SGLKKFTPTS NFGQSIIKEE
510 520 530 540 550
PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV PNFSVFSMPA
560 570 580 590 600
GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS
610 620 630 640 650
NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN
660 670 680 690 700
LRSTHDQNVK QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL
710 720 730 740 750
TTDLQESQTK NAELKEQITN LNSMTASLQS QLNEKQQQVK QERSMVDVNS
760 770 780 790 800
KQLELNQVTV ANLQKEIDGL GEKISVYLTK QKELNDYQKT VEEQHAQLQA
810 820 830 840 850
KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL QEMFDDLSQR
860 870 880 890 900
KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS
910 920 930 940 950
NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES
960 970 980 990 1000
DVFDRDVPTL GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE
1010 1020 1030 1040 1050
YGIPRSQSLT SSVANNAPQS VRDDVELPET LEERDTINNT ANRDNTGNLS
1060 1070 1080 1090 1100
HIPGEWEATP ATASTDVLSN ETTEVIEDGS TTKRANSNED GESVSSIQES
1110 1120 1130 1140 1150
PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT REIPSATVKT
1160 1170 1180 1190 1200
LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD
1210 1220 1230 1240 1250
EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL
1260 1270 1280 1290 1300
QMNAFTGTLT SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA
1310 1320 1330 1340 1350
EPTKVATPSI PQQPIPLKND PIVDASLSKG PIVNRGVATT PKSLAVEELS
1360 1370 1380
GMGFTEEEAH NALEKCNWDL EAATNFLLDS A
Length:1,381
Mass (Da):150,783
Last modified:October 1, 1994 - v2
Checksum:i626FD261DCBA7D99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiEDE1_YEAST
AccessioniPrimary (citable) accession number: P34216
Secondary accession number(s): D6VPV1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: March 28, 2018
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health