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P34216 (EDE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EH domain-containing and endocytosis protein 1
Alternative name(s):
Bud site selection protein 15
Gene names
Name:EDE1
Synonyms:BUD15
Ordered Locus Names:YBL047C
ORF Names:YBL0501, YBL0520
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1381 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.5 Ref.7 Ref.10 Ref.14 Ref.17 Ref.20 Ref.21

Subunit structure

Interacts (via UBA domain) with monoubiquitin and ENT1 (via asparagine-proline-phenylalanine tripeptide motif called NPF). Interacts with PAL1 and SYP1. Ref.7 Ref.17 Ref.19 Ref.20

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. Ref.5 Ref.6 Ref.8 Ref.14 Ref.17 Ref.20 Ref.21

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. Ref.5 Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the VDP/USO1/EDE1 family.

Contains 3 EH domains.

Contains 1 UBA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SYP1P256237EBI-21243,EBI-21900

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13811381EH domain-containing and endocytosis protein 1
PRO_0000202457

Regions

Domain14 – 113100EH 1
Domain135 – 22793EH 2
Domain277 – 36690EH 3
Domain1338 – 138043UBA
Region1217 – 1381165Able to bind biological membranes
Coiled coil593 – 882290 Potential
Compositional bias550 – 57526Ala-rich

Amino acid modifications

Modified residue2381Phosphothreonine Ref.12
Modified residue2411Phosphoserine Ref.11 Ref.12 Ref.15 Ref.16
Modified residue2441Phosphoserine Ref.12 Ref.16
Modified residue2451Phosphothreonine Ref.12 Ref.16
Modified residue2481Phosphoserine Ref.12 Ref.16
Modified residue2491Phosphoserine Ref.12
Modified residue2511Phosphothreonine Ref.16
Modified residue2651Phosphoserine Ref.15
Modified residue4191Phosphoserine Ref.15
Modified residue4501Phosphothreonine Ref.16
Modified residue4771Phosphothreonine Ref.16
Modified residue4871Phosphothreonine Ref.12
Modified residue4951Phosphoserine Ref.15 Ref.16
Modified residue8481Phosphoserine Ref.15
Modified residue9311Phosphoserine Ref.15 Ref.16
Modified residue9501Phosphoserine Ref.15
Modified residue9641Phosphoserine Ref.16
Modified residue10081Phosphoserine Ref.16
Modified residue10121Phosphoserine Ref.16
Modified residue10201Phosphoserine Ref.16
Modified residue10461Phosphothreonine Ref.16
Modified residue10691Phosphoserine Ref.15
Modified residue10871Phosphoserine Ref.15 Ref.16
Modified residue10931Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16
Modified residue10951Phosphoserine Ref.16
Modified residue10961Phosphoserine Ref.12 Ref.16
Modified residue11001Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16
Modified residue11111Phosphothreonine Ref.15
Modified residue11811Phosphoserine Ref.16
Modified residue11871Phosphoserine Ref.16
Modified residue13071Phosphothreonine Ref.12 Ref.15
Modified residue13431Phosphoserine Ref.16

Experimental info

Mutagenesis561W → A: Abnormal spatiotemporal behavior. Ref.14
Mutagenesis1761W → A: Abnormal spatiotemporal behavior. Ref.14
Mutagenesis3191W → A: Abnormal spatiotemporal behavior. Ref.14
Mutagenesis13521M → A: Reduced ubiquitin-binding. Ref.19
Mutagenesis13701L → A: Reduced ubiquitin-binding. Ref.19
Mutagenesis13741T → A: Enhanced ubiquitin-binding. Ref.19
Mutagenesis13781L → A: Reduced ubiquitin-binding. Ref.19

Secondary structure

........ 1381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P34216 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 626FD261DCBA7D99

FASTA1,381150,783
        10         20         30         40         50         60 
MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ LLSQVWATVD 

        70         80         90        100        110        120 
IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT QLASFSINQN PAPMQSGSAT 

       130        140        150        160        170        180 
GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA QTVAGDKAKD IFLKARLPNQ TLGEIWALCD 

       190        200        210        220        230        240 
RDASGVLDKS EFIMAMYLIQ LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL 

       250        260        270        280        290        300 
SANSTGVSSL TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV 

       310        320        330        340        350        360 
LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE LPDVIPNELL 

       370        380        390        400        410        420 
QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV SAPAVNTQPT VPQVLPQNSN 

       430        440        450        460        470        480 
NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT NNSFSYDNNN GQATLQQQQP QQPPPLTHSS 

       490        500        510        520        530        540 
SGLKKFTPTS NFGQSIIKEE PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV 

       550        560        570        580        590        600 
PNFSVFSMPA GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS 

       610        620        630        640        650        660 
NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN LRSTHDQNVK 

       670        680        690        700        710        720 
QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL TTDLQESQTK NAELKEQITN 

       730        740        750        760        770        780 
LNSMTASLQS QLNEKQQQVK QERSMVDVNS KQLELNQVTV ANLQKEIDGL GEKISVYLTK 

       790        800        810        820        830        840 
QKELNDYQKT VEEQHAQLQA KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL 

       850        860        870        880        890        900 
QEMFDDLSQR KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS 

       910        920        930        940        950        960 
NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES DVFDRDVPTL 

       970        980        990       1000       1010       1020 
GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE YGIPRSQSLT SSVANNAPQS 

      1030       1040       1050       1060       1070       1080 
VRDDVELPET LEERDTINNT ANRDNTGNLS HIPGEWEATP ATASTDVLSN ETTEVIEDGS 

      1090       1100       1110       1120       1130       1140 
TTKRANSNED GESVSSIQES PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT 

      1150       1160       1170       1180       1190       1200 
REIPSATVKT LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD 

      1210       1220       1230       1240       1250       1260 
EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL QMNAFTGTLT 

      1270       1280       1290       1300       1310       1320 
SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA EPTKVATPSI PQQPIPLKND 

      1330       1340       1350       1360       1370       1380 
PIVDASLSKG PIVNRGVATT PKSLAVEELS GMGFTEEEAH NALEKCNWDL EAATNFLLDS 


A 

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35808 Genomic DNA. Translation: CAA84867.1.
X78214 Genomic DNA. Translation: CAA55048.1.
Z23261 Genomic DNA. Translation: CAA80797.1.
BK006936 Genomic DNA. Translation: DAA07071.1.
PIRS45781.
RefSeqNP_009506.1. NM_001178287.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G3QNMR-A1339-1381[»]
ProteinModelPortalP34216.
SMRP34216. Positions 10-79, 138-225, 271-352, 1339-1381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32650. 160 interactions.
DIPDIP-5817N.
IntActP34216. 22 interactions.
MINTMINT-627966.
STRING4932.YBL047C.

Proteomic databases

MaxQBP34216.
PaxDbP34216.
PeptideAtlasP34216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL047C; YBL047C; YBL047C.
GeneID852233.
KEGGsce:YBL047C.

Organism-specific databases

CYGDYBL047c.
SGDS000000143. EDE1.

Phylogenomic databases

eggNOGNOG301764.
GeneTreeENSGT00750000117388.
HOGENOMHOG000112328.
OMARELDYQE.
OrthoDBEOG7XWPWW.

Enzyme and pathway databases

BioCycYEAST:G3O-28947-MONOMER.

Gene expression databases

GenevestigatorP34216.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. 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]
PfamPF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
SM00027. EH. 3 hits.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
PS50031. EH. 3 hits.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP34216.
NextBio970769.

Entry information

Entry nameEDE1_YEAST
AccessionPrimary (citable) accession number: P34216
Secondary accession number(s): D6VPV1
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references