CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011878
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Epsin-1 
Protein Synonyms/Alias
  
Gene Name
 ENT1 
Gene Synonyms/Alias
 YDL161W 
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
103RENLYIIKTLKEFRHubiquitination[1]
148EERNMNIKGRNRKGRubiquitination[1]
189EEDERRRKQDEDYETubiquitination[1]
336PQQLQQQKQQEPLIQubiquitination[1]
354GNQSMTDKYSKLNELubiquitination[1]
357SMTDKYSKLNELLATubiquitination[1, 2]
385RIPAQHTKTGTFINSubiquitination[1]
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
Functional Description
 Binds to membranes enriched in phosphatidylinositol 3,5- bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation. 
Sequence Annotation
 DOMAIN 11 143 ENTH.
 REPEAT 165 184 UIM 1.
 REPEAT 189 208 UIM 2.
 REGION 447 454 Clathrin-binding.
 MOD_RES 160 160 Phosphothreonine.
 MOD_RES 163 163 Phosphoserine.
 MOD_RES 180 180 Phosphothreonine.
 MOD_RES 328 328 Phosphoserine.
 MOD_RES 364 364 Phosphothreonine.
 MOD_RES 366 366 Phosphothreonine.
 MOD_RES 384 384 Phosphothreonine.
 MOD_RES 386 386 Phosphothreonine.
 MOD_RES 388 388 Phosphothreonine.
 MOD_RES 395 395 Phosphothreonine; by PRK1.
 MOD_RES 415 415 Phosphothreonine; by PRK1.  
Keyword
 Complete proteome; Cytoplasm; Endocytosis; Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 454 AA 
Protein Sequence
MSKQFVRSAK NLVKGYSSTQ VLVRNATSND NHQVSKDSLI ELAEKSYDSA DFFEIMDMLD 60
KRLNDKGKYW RHIAKALTVI DYLIRFGSEN CVLWCRENLY IIKTLKEFRH EDDEGIDQGQ 120
IVRVKAKELT ALLSDDERLN EERNMNIKGR NRKGRRRRGT GRSDENDDDL QRAISASRLT 180
AEEDERRRKQ DEDYETALQL SKEEEELKRL QDLQRMQQQQ GQQQLQQPMY YDIFGNPITP 240
EEYAQFQLQQ QQQQQQQQLQ QQPMYYDVFG NPITPEELAQ FQQQQQLQEQ QYLASMQQQQ 300
QAMSNNPFAK SEQSSSSPKR NQLVAASSPQ QLQQQKQQEP LIQNRTGNQS MTDKYSKLNE 360
LLATGTGIDT FGNVGEARIP AQHTKTGTFI NSQGTGYRQV SDDPNHNPFL NSQYTGLPST 420
SVVPTQTGYG FGNQSQQQSQ NNGSNNRGYT LIDL 454 
Gene Ontology
 GO:0030479; C:actin cortical patch; TAS: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:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0030276; F:clathrin binding; TAS:SGD.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0000147; P:actin cortical patch assembly; IMP:SGD.
 GO:0007015; P:actin filament organization; IMP:SGD.
 GO:0006897; P:endocytosis; IMP:SGD. 
Interpro
 IPR008942; ENTH_VHS.
 IPR013809; Epsin-like_N.
 IPR001026; Epsin_dom_N.
 IPR003903; Ubiquitin-int_motif. 
Pfam
 PF01417; ENTH 
SMART
 SM00273; ENTH
 SM00726; UIM 
PROSITE
 PS50942; ENTH
 PS50330; UIM 
PRINTS