CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011115
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin ligase-binding protein BUL2 
Protein Synonyms/Alias
  
Gene Name
 BUL2 
Gene Synonyms/Alias
 YML111W; YM8339.08 
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
540SDEILRRKLDQLHINubiquitination[1]
563QSPSYDSKNMAPKENubiquitination[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, 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
 Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other permeases such as PMA1. The RSP5-BUL1/2 complex is also necessary for the heat- shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription and pressure-induced differential regulation of the 2 tryptophan permeases TAT1 and TAT2. 
Sequence Annotation
 MOTIF 129 133 PY-motif.
 MOD_RES 22 22 Phosphothreonine.
 MOD_RES 557 557 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 920 AA 
Protein Sequence
MTFTFSTSSR KNGRPPLKSV STEDNIHLLR KRRQQQLSSN STDNSLHPNS GQTPRASDSQ 60
DDDIRSASTT NLDRLRQERE ENSLEMDCTQ SRLSHRANML VDVLPSFEMY NALHRHIPQG 120
NVDPDRHDFP PSYQEVRTQR MTILPSNDNS VERSQLTAVP GSENACNNAT AHSLTNLHPL 180
QTQHLTINST RSGGQSLHSS SDTNISQIPF EDDLNDSDNI FIDKLYTLPK LSTPIEIDIR 240
ITKTASIPHE RPEEQSILKE YTSGDIIHGY CLIENRSSQP LKFEMFYVTL EAYISVIDRQ 300
KGKRTLKRFL RMVDLSASWS YTNITPSTGI NIVPGERDFD DAIIGLSNSR ELKPNTKYKK 360
FFMFKLPTQL LDVTCKQEQF SHCLLPPSFG IDKYKNNCKY SGIKVNSVLG CGHLGTKGSP 420
ILTLDMADDN LSINYTIDAK IVGKDKRTSK LNIMKEKEYN LRVMPFPFAG VTNQQNEKTC 480
LRQLKNLESL IEDRFEALNK IFKKLELNEA ISNVDIHDTD ISGTLDGNED LDSDEILRRK 540
LDQLHINNRI DDTASQSPSY DSKNMAPKEN LVETELRYKF KNKNKSNSSL FSHFLSSSET 600
GSSSTGPHVY NSGLIVLSVK KPQSTLPYWS PSLLRKTNKF EAKSEQEKEN WQRLMGMLPE 660
GVKTPLTKLD VHLTCIQSNN SAGHKPPEIS SVTTEFVVIT AKSDNSIPIK FCTELLMNEN 720
RLNKLKTKFL TYQKKVHEYR KKFEENHAKL NELYNRNRDH FTPKELLFTN FISDQINNDI 780
DSLAGLKVNI IDLHDIFKKQ IHTFEEENED IISKKGSSNP PSASSSNNNF LQATFSNGAS 840
TATKFTQQIV HEWEKVKPLQ YKRDVTVNLK LNPNIKETLV PNLETCLCCR FYCVRVNIKF 900
DNHLGSMKVD IPVDVKKLQI 920 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0000151; C:ubiquitin ligase complex; IMP:SGD.
 GO:0034450; F:ubiquitin-ubiquitin ligase activity; IGI:SGD.
 GO:0006513; P:protein monoubiquitination; IMP:SGD.
 GO:0000209; P:protein polyubiquitination; IMP:SGD. 
Interpro
 IPR022794; Bul1_C.
 IPR007520; Bul1_C_yeast.
 IPR007519; Bul1_N. 
Pfam
 PF04426; Bul1_C
 PF04425; Bul1_N 
SMART
  
PROSITE
  
PRINTS