CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006369
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 EH domain-containing and endocytosis protein 1 
Protein Synonyms/Alias
 Bud site selection protein 15 
Gene Name
 EDE1 
Gene Synonyms/Alias
 BUD15; YBL047C; YBL0501; YBL0520 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
157AQTVAGDKAKDIFLKubiquitination[1]
498NFGQSIIKEEPEEQEubiquitination[1]
674AQVLQVNKENETLAQubiquitination[2]
780KISVYLTKQKELNDYubiquitination[1]
782SVYLTKQKELNDYQKubiquitination[1]
808KYQDLSNKDTDLTDRacetylation[3]
892GQLPEDAKDIIAKSAubiquitination[1]
897DAKDIIAKSASNTDTubiquitination[1]
907SNTDTTTKEATSRGNubiquitination[1]
1083IEDGSTTKRANSNEDubiquitination[1]
1102SSIQESPKISAQPKAubiquitination[1]
1108PKISAQPKAKTINEEubiquitination[1]
1149EIPSATVKTLQTPYNubiquitination[1]
1304NSKAEPTKVATPSIPubiquitination[1]
1318PQQPIPLKNDPIVDAubiquitination[1]
1329IVDASLSKGPIVNRGubiquitination[1, 2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 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. 
Sequence Annotation
 DOMAIN 14 113 EH 1.
 DOMAIN 135 227 EH 2.
 DOMAIN 277 366 EH 3.
 DOMAIN 1338 1380 UBA.
 REGION 1217 1381 Able to bind biological membranes.
 MOD_RES 238 238 Phosphothreonine.
 MOD_RES 241 241 Phosphoserine.
 MOD_RES 244 244 Phosphoserine.
 MOD_RES 245 245 Phosphothreonine.
 MOD_RES 248 248 Phosphoserine.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 251 251 Phosphothreonine.
 MOD_RES 265 265 Phosphoserine.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 450 450 Phosphothreonine.
 MOD_RES 477 477 Phosphothreonine.
 MOD_RES 487 487 Phosphothreonine.
 MOD_RES 495 495 Phosphoserine.
 MOD_RES 848 848 Phosphoserine.
 MOD_RES 931 931 Phosphoserine.
 MOD_RES 950 950 Phosphoserine.
 MOD_RES 964 964 Phosphoserine.
 MOD_RES 1008 1008 Phosphoserine.
 MOD_RES 1012 1012 Phosphoserine.
 MOD_RES 1020 1020 Phosphoserine.
 MOD_RES 1046 1046 Phosphothreonine.
 MOD_RES 1069 1069 Phosphoserine.
 MOD_RES 1087 1087 Phosphoserine.
 MOD_RES 1093 1093 Phosphoserine.
 MOD_RES 1095 1095 Phosphoserine.
 MOD_RES 1096 1096 Phosphoserine.
 MOD_RES 1100 1100 Phosphoserine.
 MOD_RES 1111 1111 Phosphothreonine.
 MOD_RES 1181 1181 Phosphoserine.
 MOD_RES 1187 1187 Phosphoserine.
 MOD_RES 1307 1307 Phosphothreonine.
 MOD_RES 1343 1343 Phosphoserine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Endocytosis; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1381 AA 
Protein Sequence
MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ LLSQVWATVD 60
IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT QLASFSINQN PAPMQSGSAT 120
GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA QTVAGDKAKD IFLKARLPNQ TLGEIWALCD 180
RDASGVLDKS EFIMAMYLIQ LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL 240
SANSTGVSSL TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV 300
LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE LPDVIPNELL 360
QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV SAPAVNTQPT VPQVLPQNSN 420
NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT NNSFSYDNNN GQATLQQQQP QQPPPLTHSS 480
SGLKKFTPTS NFGQSIIKEE PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV 540
PNFSVFSMPA GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS 600
NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN LRSTHDQNVK 660
QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL TTDLQESQTK NAELKEQITN 720
LNSMTASLQS QLNEKQQQVK QERSMVDVNS KQLELNQVTV ANLQKEIDGL GEKISVYLTK 780
QKELNDYQKT VEEQHAQLQA KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL 840
QEMFDDLSQR KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS 900
NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES DVFDRDVPTL 960
GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE YGIPRSQSLT SSVANNAPQS 1020
VRDDVELPET LEERDTINNT ANRDNTGNLS HIPGEWEATP ATASTDVLSN ETTEVIEDGS 1080
TTKRANSNED GESVSSIQES PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT 1140
REIPSATVKT LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD 1200
EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL QMNAFTGTLT 1260
SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA EPTKVATPSI PQQPIPLKND 1320
PIVDASLSKG PIVNRGVATT PKSLAVEELS GMGFTEEEAH NALEKCNWDL EAATNFLLDS 1380
A 1381 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0005935; C:cellular bud neck; IDA:SGD.
 GO:0005934; C:cellular bud tip; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0043130; F:ubiquitin binding; IDA:SGD.
 GO:0006897; P:endocytosis; IMP:SGD.
 GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR000261; EPS15_homology.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 
Pfam
 PF00627; UBA 
SMART
 SM00054; EFh
 SM00027; EH
 SM00165; UBA 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50031; EH
 PS50030; UBA 
PRINTS