CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006107
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoinositide phosphatase SAC1 
Protein Synonyms/Alias
 Recessive suppressor of secretory defect 
Gene Name
 SAC1 
Gene Synonyms/Alias
 RSD1; YKL212W 
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
22FFKLAEGKGTNDAVIubiquitination[1]
246AENPESEKIHVFSFLubiquitination[2]
358LLIDHLEKLGLSNEDubiquitination[2]
613LKYAQSPKFSKPDPLacetylation[3]
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]
 [3] 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] 
Functional Description
 Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton. 
Sequence Annotation
 DOMAIN 115 454 SAC.  
Keyword
 3D-structure; Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 623 AA 
Protein Sequence
MTGPIVYVQN ADGIFFKLAE GKGTNDAVIH LANQDQGVRV LGAEEFPVQG EVVKIASLMG 60
FIKLKLNRYA IIANTVEETG RFNGHVFYRV LQHSIVSTKF NSRIDSEEAE YIKLLELHLK 120
NSTFYFSYTY DLTNSLQRNE KVGPAASWKT ADERFFWNHY LTEDLRNFAH QDPRIDSFIQ 180
PVIYGYAKTV DAVLNATPIV LGLITRRSIF RAGTRYFRRG VDKDGNVGNF NETEQILLAE 240
NPESEKIHVF SFLQTRGSVP IYWAEINNLK YKPNLVLGEN SLDATKKHFD QQKELYGDNY 300
LVNLVNQKGH ELPVKEGYES VVHALNDPKI HYVYFDFHHE CRKMQWHRVK LLIDHLEKLG 360
LSNEDFFHKV IDSNGNTVEI VNEQHSVVRT NCMDCLDRTN VVQSVLAQWV LQKEFESADV 420
VATGSTWEDN APLLTSYQNL WADNADAVSV AYSGTGALKT DFTRTGKRTR LGAFNDFLNS 480
ASRYYQNNWT DGPRQDSYDL FLGGFRPHTA SIKSPFPDRR PVYIQLIPMI ICAALTVLGA 540
TIFFPKDRFT SSKNLLYFAG ASIVLALSTK FMFKNGIQFV NWPKLVDVGF LVVHQTHDKE 600
QQFKGLKYAQ SPKFSKPDPL KRD 623 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:SGD.
 GO:0030173; C:integral to Golgi membrane; IDA:SGD.
 GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
 GO:0035339; C:SPOTS complex; IDA:UniProtKB.
 GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:SGD.
 GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:SGD.
 GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:SGD.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD. 
Interpro
 IPR002013; Syja_N. 
Pfam
 PF02383; Syja_N 
SMART
  
PROSITE
 PS50275; SAC 
PRINTS