CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011833
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein SFI1 
Protein Synonyms/Alias
 Suppressor of fermentation induced loss of stress resistance protein 1 
Gene Name
 SFI1 
Gene Synonyms/Alias
 YLL003W; L1373 
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
18TENLLRDKFVPETSPubiquitination[1]
868SVLDSTAKKQINLESacetylation[2]
869VLDSTAKKQINLESTacetylation[2]
Reference
 [1] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [2] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591] 
Functional Description
 Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication. 
Sequence Annotation
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 855 855 Phosphoserine.  
Keyword
 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 946 AA 
Protein Sequence
MGKFGTTNKS TENLLRDKFV PETSPTNIPT DVLIKQGQIT DSTESLIHGG AERYIVNALK 60
PIELNKTEGF FEDPPFHLPS PPVDSTNLEY EDVTDLPKNG LRYDLNDISV EVIEDLYRQI 120
EAFLVHFKLS RSFLQIFKNY VNILIQEGIN PLRDEYFTIL EDELKGFFTF NSVIEEILEI 180
FLIHPRNKFI ALSLAEYTYA KNKIRRHFNH WKTVCELNEE ANRFANQAKL RVQEAVFYIW 240
SDKTLKYSQM ANDEAESFRN TWLLFRSFQQ WITLTQTLKE QSRLADQAFL NKMFRKILKA 300
QEHWKHLETV NTDNIKKIFL RTTFHIWKLR HKEINYHGLE RRIFERIKQK VINYEYNKSI 360
AEKVRSFSLQ RKYLNKWEKK NIENEDKLGA LYELENKFIK QKFFRKLNRS FQHSQQEAIA 420
KSKLNQTLLR CVFEKMWLKR FEDHLHLYSI VSLKEANLVK RIFHSWKKLL YIDLKASDYS 480
RTNLLKSSLR SWKLEVKLKI FEQKCKKSIQ ASAYRTWRKR IQYGKISSEH VKTAFCAKYL 540
GVWKRRMLQM NSMNDEASKF YEEGLVNECL AIWKERLIKT KELEDRYNFL CKTHAILTVK 600
RTLMHIDNVH LLYTKLAPSM DRVKLSKAFL KWRKATRFKV RHKLNDILHV YEKSKERELQ 660
SQLFNAWRNR FCFYTEECNI QAISKRNYQL EKMVLKKFRE RLLEIVKSEE LADEVREEFV 720
LVKTFYIWKT HLDEIFYMST LLEQSEANKQ FIITSKFLKM WSLRFLKIKR NDETVEVFRH 780
RWDRATVRGL LLLWKNRSDS SPKRRKDFNL KHELKTPIRS DSQNASTIPG SERIKQHRME 840
AMKSHYSRAR RAIPSPVKSS SVLDSTAKKQ INLESTTGLN GSPTRGKPLR YSPRRTTRNM 900
PSKVDHIDFG RIPAVPFSLS ANSPKIDQDM DYIREHDKSP LSRKRQ 946 
Gene Ontology
 GO:0005825; C:half bridge of spindle pole body; IDA:SGD.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0051225; P:spindle assembly; IMP:SGD.
 GO:0007103; P:spindle pole body duplication associated with nuclear envelope; IMP:SGD. 
Interpro
 IPR013665; Sfi1.
 IPR018907; Spindle_body_associated_C. 
Pfam
 PF08457; Sfi1
 PF10638; Sfi1_C 
SMART
  
PROSITE
  
PRINTS