CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011312
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Epsin-2 
Protein Synonyms/Alias
  
Gene Name
 ENT2 
Gene Synonyms/Alias
 YLR206W 
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
14RSAKNMMKGYSSTQVubiquitination[1]
182SYQDDLEKALEESRIubiquitination[1]
225SKEEEELKQLQELQRubiquitination[2]
381RQQQEQLKLQQLQRQubiquitination[1]
426FQQQQPLKQTRTGNQubiquitination[2]
482NSQGTGYKQVTNEPKubiquitination[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, Villén 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. 
Sequence Annotation
 DOMAIN 11 143 ENTH.
 REPEAT 175 194 UIM 1.
 REPEAT 206 225 UIM 2.
 MOD_RES 165 165 Phosphothreonine.
 MOD_RES 167 167 Phosphoserine.
 MOD_RES 450 450 Phosphothreonine.
 MOD_RES 468 468 Phosphothreonine.
 MOD_RES 470 470 Phosphothreonine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Endocytosis; Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 613 AA 
Protein Sequence
MSKQFVRSAK NMMKGYSSTQ VLVRDATAND SRTPSIDTLD DLAQRSYDSV DFFEIMDMLD 60
KRLNDKGKYW RHVAKSLTVL DYLVRFGSEN CVLWCRENFY VIKTLREFRH ENESGFDEGQ 120
IIRVKAKELV SLLNDEERLR EERSMNTRNR RANRAARPRP RRQRTRSNPH DSSPSYQDDL 180
EKALEESRIT AQEDEQRRRE LAQYDDEDPD FQAALQLSKE EEELKQLQEL QRLQKQQQSL 240
SQFQAPLQQQ QPQQQPAYYD IFGNPISQDE YLQYQYQQDQ EQAMAQQRWL DQQQEQQQLA 300
EQQYFQQQQQ AAAAASALQQ QQTAANMQQQ QQQPADFQQP LPTGSNNPFS MDNLERQKQE 360
QQHAQLQRQQ EEARQQQEQL KLQQLQRQQQ EEAQLHQKRQ EEAQLQQQQA QLLQQQAQFQ 420
QQQPLKQTRT GNQSISDKYS DLNTLLATGT GIDTFGNTGE ARIPAQHTKT GTFINSQGTG 480
YKQVTNEPKN NPFLSNQYTG LPSTNIVPTQ TGYGFGNQPQ SPPTNSPQQN PTGISYSQPQ 540
QQQQPQQQPQ YMQNFQQQQP QYAQNFQQQP QYTQNYQQQP QYIQPHQQQQ QQQQQQQQQQ 600
GYTPDQGVSL IDL 613 
Gene Ontology
 GO:0030479; C:actin cortical patch; TAS: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