EDE1/YBL047C Protein Information

Standard Name	Ede1p 1
Systematic Name	Ybl047cp
Alias	Bud15p 2
ORF Classification	Verified
Description	Endocytic protein; involved in a network of interactions with other endocytic proteins, binds membranes in a ubiquitin-dependent manner, may also bind ubiquitinated membrane-associated proteins; interacts with Cmk2 and functions upstream of CMK2 in regulating non-apoptotic cell death (1, 3, 4)
Name Description	EH Domains and Endocytosis 1

Experimental Data
Molecules/cell	1380 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,381
Molecular Weight (Da)	150,782
Isoelectric Point (pI)	4.44

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Ede1p (InterPro)
Physical Interactions	There are 66 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000053246 \| P34216 MIPS: YBL047C NCBI: 109157777 \| 313748 \| 463262 \| 536069 \| 586426 \| 6319424 \| NP_009506.1 GenBank/EMBL/DDBJ: DAA07071.1 \| X78214 \| Z23261 \| Z35808

Amino Acid Sequence (or in FASTA format)
1 MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ 51 LLSQVWATVD IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT 101 QLASFSINQN PAPMQSGSAT GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA 151 QTVAGDKAKD IFLKARLPNQ TLGEIWALCD RDASGVLDKS EFIMAMYLIQ 201 LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL SANSTGVSSL 251 TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV 301 LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE 351 LPDVIPNELL QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV 401 SAPAVNTQPT VPQVLPQNSN NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT 451 NNSFSYDNNN GQATLQQQQP QQPPPLTHSS SGLKKFTPTS NFGQSIIKEE 501 PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV PNFSVFSMPA 551 GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS 601 NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN 651 LRSTHDQNVK QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL 701 TTDLQESQTK NAELKEQITN LNSMTASLQS QLNEKQQQVK QERSMVDVNS 751 KQLELNQVTV ANLQKEIDGL GEKISVYLTK QKELNDYQKT VEEQHAQLQA 801 KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL QEMFDDLSQR 851 KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS 901 NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES 951 DVFDRDVPTL GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE 1001 YGIPRSQSLT SSVANNAPQS VRDDVELPET LEERDTINNT ANRDNTGNLS 1051 HIPGEWEATP ATASTDVLSN ETTEVIEDGS TTKRANSNED GESVSSIQES 1101 PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT REIPSATVKT 1151 LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD 1201 EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL 1251 QMNAFTGTLT SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA 1301 EPTKVATPSI PQQPIPLKND PIVDASLSKG PIVNRGVATT PKSLAVEELS 1351 GMGFTEEEAH NALEKCNWDL EAATNFLLDS A*

Amino Acid Sequence (or in FASTA format)

       1  MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ
      51  LLSQVWATVD IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT
     101  QLASFSINQN PAPMQSGSAT GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA
     151  QTVAGDKAKD IFLKARLPNQ TLGEIWALCD RDASGVLDKS EFIMAMYLIQ
     201  LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL SANSTGVSSL
     251  TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV
     301  LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE
     351  LPDVIPNELL QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV
     401  SAPAVNTQPT VPQVLPQNSN NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT
     451  NNSFSYDNNN GQATLQQQQP QQPPPLTHSS SGLKKFTPTS NFGQSIIKEE
     501  PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV PNFSVFSMPA
     551  GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS
     601  NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN
     651  LRSTHDQNVK QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL
     701  TTDLQESQTK NAELKEQITN LNSMTASLQS QLNEKQQQVK QERSMVDVNS
     751  KQLELNQVTV ANLQKEIDGL GEKISVYLTK QKELNDYQKT VEEQHAQLQA
     801  KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL QEMFDDLSQR
     851  KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS
     901  NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES
     951  DVFDRDVPTL GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE
    1001  YGIPRSQSLT SSVANNAPQS VRDDVELPET LEERDTINNT ANRDNTGNLS
    1051  HIPGEWEATP ATASTDVLSN ETTEVIEDGS TTKRANSNED GESVSSIQES
    1101  PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT REIPSATVKT
    1151  LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD
    1201  EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL
    1251  QMNAFTGTLT SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA
    1301  EPTKVATPSI PQQPIPLKND PIVDASLSKG PIVNRGVATT PKSLAVEELS
    1351  GMGFTEEEAH NALEKCNWDL EAATNFLLDS A*

external links for Ede1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Ede1p

1)	Gagny B, et al. (2000) A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis. J Cell Sci 113 ( Pt 18)():3309-19
2)	Ni L and Snyder M (2001) A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell 12(7):2147-70
3)	Aguilar RC, et al. (2003) The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J Biol Chem 278(12):10737-43
4)	Kim H, et al. (2012) Vacuolar H+-ATPase (V-ATPase) promotes vacuolar membrane permeabilization and nonapoptotic death in stressed yeast. J Biol Chem 287(23):19029-39
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41