CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007022
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein BZZ1 
Protein Synonyms/Alias
 LAS17-binding protein 7 
Gene Name
 BZZ1 
Gene Synonyms/Alias
 LSB7; YHR114W 
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
331DYNSLQDKTQNELSKacetylation[1]
331DYNSLQDKTQNELSKubiquitination[2]
Reference
 [1] 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]
 [2] 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
 Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. 
Sequence Annotation
 DOMAIN 5 68 FCH.
 DOMAIN 493 555 SH3 1.
 DOMAIN 577 633 SH3 2.
 MOD_RES 327 327 Phosphoserine.
 MOD_RES 463 463 Phosphoserine.
 MOD_RES 472 472 Phosphoserine.
 MOD_RES 476 476 Phosphoserine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Phosphoprotein; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 633 AA 
Protein Sequence
MSADLSIGNE IKDSFKETHK WVQNNLKWLK DIEQFYRERA KLEKDYSERL SRLSAEYFNK 60
KSSTSVPISV GDTPTTTPGS IEAAGVVAWN EILSQTDMIS KDHDQLSTDF ENHVANQLSG 120
LFTKLDMTLS KINGFNNDMV NKKDNIYHEL EKAKKDYDEA CSTMEMARNR YTKASNDRNK 180
KKLDEKEMEM NKCKNEYLIK INQANRTKDK YYFQDVPEVL DLLQDVNEAK TLFLNDLWLK 240
AASVENDLGA NVSKRLQAAN SVVKQNKPSL NTAIFIKHNL KNWKEPQDFV YKPSPVWHDD 300
EKFAVPSSLE VEDLRIKLAK AENDYNSLQD KTQNELSKLS TLNKIKHEMK TNEDNINATK 360
FYDTLKEYLN VVSPFTSHET LKLQAEVQIE SIQNNVPEEY DLSTDNIDLS KTKKKSGIFS 420
KFKHNILNVD SKPSSGGSTG NGNGGPLHIT SLFNTSRRTR LGSAPNNAGE DSDNNSIRTT 480
STNNTKKTTQ NSSDDGKNKV LYAYVQKDDD EITITPGDKI SLVARDTGSG WTKINNDTTG 540
ETGLVPTTYI RISSAATVKA NDRGPAPEVP PPRRSTLPVR TMEAIYAYEA QGDDEISIDP 600
GDIITVIRGD DGSGWTYGEC DGLKGLFPTS YCK 633 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0007015; P:actin filament organization; IPI:SGD.
 GO:0006897; P:endocytosis; IGI:SGD.
 GO:0009651; P:response to salt stress; IGI:SGD. 
Interpro
 IPR001060; FCH_dom.
 IPR001452; SH3_domain. 
Pfam
 PF00611; FCH
 PF00018; SH3_1 
SMART
 SM00055; FCH
 SM00326; SH3 
PROSITE
 PS50133; FCH
 PS50002; SH3 
PRINTS