P32368

Name	Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Recessive suppressor of secretory defect)
Uniprot ID	P32368
Systematic gene name	YKL212W
Standard gene name	SAC1
Gene names	SAC1 RSD1 YKL212W
Description from SGD	YKL212W SAC1 SGDID:S000001695, Chr XI from 34543-36414, Genome Release 64-3-1, Verified ORF, "Phosphatidylinositol phosphate phosphatase; role in early and medial Golgi PtdIns4P hydrolysis; regulated by Vps74p interaction; ER localized transmembrane protein which cycles through the Golgi; role in protein trafficking, processing, secretion, and cell wall maintenance; regulates sphingolipid biosynthesis by modulating PtdIns(4)P metabolism; PtdIns4P PPase activity is crucial for autophagosome-vacuole fusion during autophagy; human homolog SACM1L complements autophagy defects of the null"
Protein length	623
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MTGPIVYVQN ADGIFFKLAE GKGTNDAVIH LANQDQGVRV LGAEEFPVQG
EVVKIASLMG FIKLKLNRYA IIANTVEETG RFNGHVFYRV LQHSIVSTKF
NSRIDSEEAE YIKLLELHLK NSTFYFSYTY DLTNSLQRNE KVGPAASWKT
ADERFFWNHY LTEDLRNFAH QDPRIDSFIQ PVIYGYAKTV DAVLNATPIV
LGLITRRSIF RAGTRYFRRG VDKDGNVGNF NETEQILLAE NPESEKIHVF
SFLQTRGSVP IYWAEINNLK YKPNLVLGEN SLDATKKHFD QQKELYGDNY
LVNLVNQKGH ELPVKEGYES VVHALNDPKI HYVYFDFHHE CRKMQWHRVK
LLIDHLEKLG LSNEDFFHKV IDSNGNTVEI VNEQHSVVRT NCMDCLDRTN
VVQSVLAQWV LQKEFESADV VATGSTWEDN APLLTSYQNL WADNADAVSV
AYSGTGALKT DFTRTGKRTR LGAFNDFLNS ASRYYQNNWT DGPRQDSYDL
FLGGFRPHTA SIKSPFPDRR PVYIQLIPMI ICAALTVLGA TIFFPKDRFT
SSKNLLYFAG ASIVLALSTK FMFKNGIQFV NWPKLVDVGF LVVHQTHDKE
QQFKGLKYAQ SPKFSKPDPL KRD

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[22, Ubi]	Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[177, Phos]	Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[258, Phos]	Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[271, Phos]	Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[271, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[285, Phos]	Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[285, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[613, K-acetyl]	Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)