| UniProt ID | PAH1_YEAST | |
|---|---|---|
| UniProt AC | P32567 | |
| Protein Name | Phosphatidic acid phosphohydrolase 1 | |
| Gene Name | PAH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 862 | |
| Subcellular Localization |
Cytoplasm. Nucleus membrane Peripheral membrane protein. Endoplasmic reticulum membrane Peripheral membrane protein. |
|
| Protein Description | Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation.. | |
| Protein Sequence | MQYVGRALGSVSKTWSSINPATLSGAIDVIVVEHPDGRLSCSPFHVRFGKFQILKPSQKKVQVFINEKLSNMPMKLSDSGEAYFVFEMGDQVTDVPDELLVSPVMSATSSPPQSPETSILEGGTEGEGEGENENKKKEKKVLEEPDFLDINDTGDSGSKNSETTGSLSPTESSTTTPPDSVEERKLVEQRTKNFQQKLNKKLTEIHIPSKLDNNGDLLLDTEGYKPNKNMMHDTDIQLKQLLKDEFGNDSDISSFIKEDKNGNIKIVNPYEHLTDLSPPGTPPTMATSGSVLGLDAMESGSTLNSLSSSPSGSDTEDETSFSKEQSSKSEKTSKKGTAGSGETEKRYIRTIRLTNDQLKCLNLTYGENDLKFSVDHGKAIVTSKLFVWRWDVPIVISDIDGTITKSDALGHVLAMIGKDWTHLGVAKLFSEISRNGYNILYLTARSAGQADSTRSYLRSIEQNGSKLPNGPVILSPDRTMAALRREVILKKPEVFKIACLNDIRSLYFEDSDNEVDTEEKSTPFFAGFGNRITDALSYRTVGIPSSRIFTINTEGEVHMELLELAGYRSSYIHINELVDHFFPPVSLDSVDLRTNTSMVPGSPPNRTLDNFDSEITSGRKTLFRGNQEEKFTDVNFWRDPLVDIDNLSDISNDDSDNIDEDTDVSQQSNISRNRANSVKTAKVTKAPQRNVSGSTNNNEVLAASSDVENASDLVSSHSSSGSTPNKSTMSKGDIGKQIYLELGSPLASPKLRYLDDMDDEDSNYNRTKSRRASSAAATSIDKEFKKLSVSKAGAPTRIVSKINVSNDVHSLGNSDTESRREQSVNETGRNQLPHNSMDDKDLDSRVSDEFDDDEFDEDEFED | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 110 | Phosphorylation | PVMSATSSPPQSPET CCCCCCCCCCCCCCC | 35.92 | 21081492 | |
| 114 | Phosphorylation | ATSSPPQSPETSILE CCCCCCCCCCCEECC | 30.40 | 21081492 | |
| 158 | Phosphorylation | NDTGDSGSKNSETTG CCCCCCCCCCCCCCC | 32.39 | 21440633 | |
| 161 | Phosphorylation | GDSGSKNSETTGSLS CCCCCCCCCCCCCCC | 39.80 | 22369663 | |
| 163 | Phosphorylation | SGSKNSETTGSLSPT CCCCCCCCCCCCCCC | 35.96 | 23749301 | |
| 164 | Phosphorylation | GSKNSETTGSLSPTE CCCCCCCCCCCCCCC | 22.26 | 22369663 | |
| 166 | Phosphorylation | KNSETTGSLSPTESS CCCCCCCCCCCCCCC | 24.47 | 22369663 | |
| 168 | Phosphorylation | SETTGSLSPTESSTT CCCCCCCCCCCCCCC | 31.32 | 22369663 | |
| 170 | Phosphorylation | TTGSLSPTESSTTTP CCCCCCCCCCCCCCC | 45.16 | 22369663 | |
| 172 | Phosphorylation | GSLSPTESSTTTPPD CCCCCCCCCCCCCCC | 35.15 | 20377248 | |
| 173 | Phosphorylation | SLSPTESSTTTPPDS CCCCCCCCCCCCCCC | 24.44 | 22369663 | |
| 174 | Phosphorylation | LSPTESSTTTPPDSV CCCCCCCCCCCCCCH | 43.92 | 20377248 | |
| 175 | Phosphorylation | SPTESSTTTPPDSVE CCCCCCCCCCCCCHH | 38.97 | 23749301 | |
| 176 | Phosphorylation | PTESSTTTPPDSVEE CCCCCCCCCCCCHHH | 32.67 | 20377248 | |
| 180 | Phosphorylation | STTTPPDSVEERKLV CCCCCCCCHHHHHHH | 36.88 | 22369663 | |
| 203 | Phosphorylation | QKLNKKLTEIHIPSK HHHHHHHHHEECCCC | 41.60 | 21440633 | |
| 250 | Phosphorylation | KDEFGNDSDISSFIK HHHHCCCCCHHHHEE | 40.62 | 21440633 | |
| 254 | Phosphorylation | GNDSDISSFIKEDKN CCCCCHHHHEEECCC | 31.18 | 21440633 | |
| 311 | Phosphorylation | NSLSSSPSGSDTEDE HHCCCCCCCCCCCCC | 53.53 | 28889911 | |
| 327 | Phosphorylation | SFSKEQSSKSEKTSK CCCHHHCCCCCCCCC | 39.64 | 19779198 | |
| 340 | Phosphorylation | SKKGTAGSGETEKRY CCCCCCCCCHHHHHE | 30.87 | 28889911 | |
| 343 | Phosphorylation | GTAGSGETEKRYIRT CCCCCCHHHHHEEEE | 50.78 | 28889911 | |
| 354 | Phosphorylation | YIRTIRLTNDQLKCL EEEEEEECCCCEEEE | 27.22 | 19779198 | |
| 364 | Phosphorylation | QLKCLNLTYGENDLK CEEEEECCCCCCCEE | 28.54 | 19779198 | |
| 365 | Phosphorylation | LKCLNLTYGENDLKF EEEEECCCCCCCEEE | 26.13 | 19779198 | |
| 505 | Phosphorylation | ACLNDIRSLYFEDSD EECHHHHHHCCCCCC | 27.96 | 21440633 | |
| 507 | Phosphorylation | LNDIRSLYFEDSDNE CHHHHHHCCCCCCCC | 13.23 | 28889911 | |
| 511 | Phosphorylation | RSLYFEDSDNEVDTE HHHCCCCCCCCCCCC | 34.83 | 21551504 | |
| 546 | Phosphorylation | RTVGIPSSRIFTINT CEECCCCCCEEEEEC | 24.84 | 28889911 | |
| 594 | Phosphorylation | LDSVDLRTNTSMVPG CCCEECCCCCCCCCC | 50.58 | 28889911 | |
| 596 | Phosphorylation | SVDLRTNTSMVPGSP CEECCCCCCCCCCCC | 20.00 | 15665377 | |
| 597 | Phosphorylation | VDLRTNTSMVPGSPP EECCCCCCCCCCCCC | 21.61 | 28889911 | |
| 602 | Phosphorylation | NTSMVPGSPPNRTLD CCCCCCCCCCCCCCC | 30.98 | 22369663 | |
| 607 | Phosphorylation | PGSPPNRTLDNFDSE CCCCCCCCCCCCCCC | 45.14 | 21440633 | |
| 613 | Phosphorylation | RTLDNFDSEITSGRK CCCCCCCCCCCCCCC | 27.10 | 30377154 | |
| 617 | Phosphorylation | NFDSEITSGRKTLFR CCCCCCCCCCCEEEC | 42.11 | 23749301 | |
| 692 | Phosphorylation | KAPQRNVSGSTNNNE CCCCCCCCCCCCCCC | 30.49 | 20377248 | |
| 694 | Phosphorylation | PQRNVSGSTNNNEVL CCCCCCCCCCCCCEE | 22.06 | 22369663 | |
| 695 | Phosphorylation | QRNVSGSTNNNEVLA CCCCCCCCCCCCEEE | 45.55 | 21440633 | |
| 704 | Phosphorylation | NNEVLAASSDVENAS CCCEEEEECCCCCHH | 22.82 | 21440633 | |
| 705 | Phosphorylation | NEVLAASSDVENASD CCEEEEECCCCCHHH | 40.73 | 22369663 | |
| 711 | Phosphorylation | SSDVENASDLVSSHS ECCCCCHHHHHHCCC | 42.96 | 23749301 | |
| 715 | Phosphorylation | ENASDLVSSHSSSGS CCHHHHHHCCCCCCC | 29.63 | 22369663 | |
| 716 | Phosphorylation | NASDLVSSHSSSGST CHHHHHHCCCCCCCC | 21.65 | 22369663 | |
| 718 | Phosphorylation | SDLVSSHSSSGSTPN HHHHHCCCCCCCCCC | 28.31 | 22369663 | |
| 719 | Phosphorylation | DLVSSHSSSGSTPNK HHHHCCCCCCCCCCC | 33.04 | 22369663 | |
| 720 | Phosphorylation | LVSSHSSSGSTPNKS HHHCCCCCCCCCCCC | 39.51 | 21551504 | |
| 722 | Phosphorylation | SSHSSSGSTPNKSTM HCCCCCCCCCCCCCC | 42.51 | 22369663 | |
| 723 | Phosphorylation | SHSSSGSTPNKSTMS CCCCCCCCCCCCCCC | 34.11 | 22369663 | |
| 739 | Phosphorylation | GDIGKQIYLELGSPL CCCCCHHHHCCCCCC | 7.51 | 22890988 | |
| 744 | Phosphorylation | QIYLELGSPLASPKL HHHHCCCCCCCCCCC | 29.39 | 22369663 | |
| 748 | Phosphorylation | ELGSPLASPKLRYLD CCCCCCCCCCCCCCC | 30.19 | 22369663 | |
| 753 | Phosphorylation | LASPKLRYLDDMDDE CCCCCCCCCCCCCCC | 25.56 | 30377154 | |
| 762 | Phosphorylation | DDMDDEDSNYNRTKS CCCCCCCCCCCHHHH | 38.88 | 21440633 | |
| 764 | Phosphorylation | MDDEDSNYNRTKSRR CCCCCCCCCHHHHHH | 15.24 | 30377154 | |
| 767 | Phosphorylation | EDSNYNRTKSRRASS CCCCCCHHHHHHHHH | 29.72 | 21440633 | |
| 769 | Phosphorylation | SNYNRTKSRRASSAA CCCCHHHHHHHHHHH | 26.79 | 19684113 | |
| 773 | Phosphorylation | RTKSRRASSAAATSI HHHHHHHHHHHHHHH | 20.78 | 22369663 | |
| 774 | Phosphorylation | TKSRRASSAAATSID HHHHHHHHHHHHHHC | 22.42 | 22369663 | |
| 778 | Phosphorylation | RASSAAATSIDKEFK HHHHHHHHHHCHHHH | 22.84 | 22890988 | |
| 779 | Phosphorylation | ASSAAATSIDKEFKK HHHHHHHHHCHHHHH | 24.86 | 19823750 | |
| 800 | Phosphorylation | GAPTRIVSKINVSND CCCCEEEEEEECCCC | 26.00 | 23749301 | |
| 805 | Phosphorylation | IVSKINVSNDVHSLG EEEEEECCCCHHHCC | 23.87 | 22369663 | |
| 810 | Phosphorylation | NVSNDVHSLGNSDTE ECCCCHHHCCCCCHH | 37.51 | 22369663 | |
| 814 | Phosphorylation | DVHSLGNSDTESRRE CHHHCCCCCHHHHHH | 44.08 | 22369663 | |
| 816 | Phosphorylation | HSLGNSDTESRREQS HHCCCCCHHHHHHHH | 35.36 | 22369663 | |
| 818 | Phosphorylation | LGNSDTESRREQSVN CCCCCHHHHHHHHCC | 38.44 | 22369663 | |
| 823 | Phosphorylation | TESRREQSVNETGRN HHHHHHHHCCHHHCC | 23.35 | 20377248 | |
| 827 | Phosphorylation | REQSVNETGRNQLPH HHHHCCHHHCCCCCC | 35.92 | 21440633 | |
| 836 | Phosphorylation | RNQLPHNSMDDKDLD CCCCCCCCCCCCCHH | 22.13 | 21440633 | |
| 844 | Phosphorylation | MDDKDLDSRVSDEFD CCCCCHHHHHCCCCC | 41.71 | 28889911 | |
| 847 | Phosphorylation | KDLDSRVSDEFDDDE CCHHHHHCCCCCCCC | 30.25 | 17971454 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PAH1_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PAH1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphorylation of phosphatidate phosphatase regulates its membraneassociation and physiological functions in Saccharomyces cerevisiae:identification of SER(602), THR(723), AND SER(744) as the sitesphosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase."; Choi H.S., Su W.M., Morgan J.M., Han G.S., Xu Z., Karanasios E.,Siniossoglou S., Carman G.M.; J. Biol. Chem. 286:1486-1498(2011). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-602; THR-723 AND SER-744. | |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-311; SER-511;SER-546; SER-602; SER-705; SER-744; SER-748; SER-810; SER-814; THR-816AND SER-818, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810 AND SER-814, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602; SER-744 ANDSER-748, AND MASS SPECTROMETRY. | |
| "Control of phospholipid synthesis by phosphorylation of the yeastlipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase."; O'Hara L., Han G.S., Peak-Chew S., Grimsey N., Carman G.M.,Siniossoglou S.; J. Biol. Chem. 281:34537-34548(2006). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-110; SER-114; SER-168; SER-602;THR-723; SER-744 AND SER-748. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-596 AND SER-748, ANDMASS SPECTROMETRY. | |
