CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005598
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bud site selection protein 14 
Protein Synonyms/Alias
  
Gene Name
 BUD14 
Gene Synonyms/Alias
 YAR014C; FUN2 
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
240DSGFQGEKDDLEEENubiquitination[1]
680NMSDPASKPNSLVQHubiquitination[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] 
Functional Description
 Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex. 
Sequence Annotation
 DOMAIN 259 320 SH3.
 MOD_RES 159 159 Phosphotyrosine.
 MOD_RES 160 160 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 177 177 Phosphothreonine.
 MOD_RES 212 212 Phosphoserine.
 MOD_RES 222 222 Phosphoserine.
 MOD_RES 376 376 Phosphoserine.
 MOD_RES 378 378 Phosphoserine.
 MOD_RES 401 401 Phosphoserine.
 MOD_RES 507 507 Phosphoserine.
 MOD_RES 655 655 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.
 MOD_RES 670 670 Phosphoserine.  
Keyword
 Cell cycle; Cell division; Complete proteome; Phosphoprotein; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 709 AA 
Protein Sequence
MSNKEEHVDE TSASGVKEVS SIAARHDNGY APSLITSTSG MDSFQSHALL NDPTLIEDYS 60
DIINNRPTSG SKLTLGNEDS ESMGGSVVVT PTSNKSSPFN SKLNILSNAA EKGHDVLRNR 120
DDDKELEEEN VEKHMHSNSK RDQRHYKENS SELPDSYDYS DSEFEDNLER RLQEIETDSV 180
DSADKDEVHF SVNNTMNPDV DDFSDGLKYA ISEDEDEEEN YSDDDDFDRK FQDSGFQGEK 240
DDLEEENDDY QPLSPPRELD PDKLYALYAF NGHDSSHCQL GQDEPCILLN DQDAYWWLVK 300
RITDGKIGFA PAEILETFPE RLARLNCWKN ENMSSQSVAS SDSKDDSISS GNKNQSDAES 360
IIPTPALNGY GKGNKSVSFN DVVGYADRFI DDAIEDTSLD SNDDGGEGNG QSYDDDVDND 420
KETKVTHRDE YTEAKLNFGK FQDDDTSDVV SDVSFSTSLN TPLNVKKVRR QDNKNESEPK 480
TSSSKDREDD YNANRYVGQE KSEPVDSDYD TDLKKVFEAP RMPFANGMAK SDSQNSLSTI 540
GEFSPSSSEW TNESPSTPIV EESSSIPSSR AIKDISQYIH AKSKIEETTN VENTEGQIQA 600
SLGSSGGMAN QTDAEQPKEE LEKHHSTPEE EKQSTLSLHS SSEEDFYMDE QRAVSSASIN 660
SSLSGSRALS NTNMSDPASK PNSLVQHLYA PVFDRMDVLM KQLDEIIRK 709 
Gene Ontology
 GO:0005935; C:cellular bud neck; IDA:SGD.
 GO:0005934; C:cellular bud tip; IDA:SGD.
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0000131; C:incipient cellular bud site; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0008599; F:protein phosphatase type 1 regulator activity; IDA:SGD.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007010; P:cytoskeleton organization; IGI:SGD.
 GO:0030837; P:negative regulation of actin filament polymerization; IDA:SGD.
 GO:0000903; P:regulation of cell shape during vegetative growth phase; IGI:SGD.
 GO:0032880; P:regulation of protein localization; IDA:SGD.
 GO:0006355; P:regulation of transcription, DNA-dependent; IGI:SGD. 
Interpro
 IPR001452; SH3_domain. 
Pfam
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS50002; SH3 
PRINTS