PAH1/YMR165C Protein Information Help

Standard Name Pah1p 1
Systematic Name Ymr165cp
Alias Smp2p 2
ORF Classification Verified
Description Mg2+-dependent phosphatidate (PA) phosphatase; dephosphorylates PA to yield diacylglycerol; responsible for de novo lipid synthesis and formation of lipid droplets; phosphorylation by Pho80p-Pho85p decreases catalytic activity and alters Pah1p localization and abundance; phosphorylation by protein kinase A decreases catalytic efficiency; dephosphorylation by Nem1p-Spo7p anchors Pah1p to the membrane increasing substrate catalysis; homologous to mammalian lipins 1 and 2 (1, 3, 4, 5, 6, 7, 8)
Name Description Phosphatidic Acid phosphoHydrolase 1
Experimental Data
Molecules/cell 3910 9
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 862
Molecular Weight (Da) 95,030
Isoelectric Point (pI) 4.68

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Pah1p (InterPro)
Physical Interactions There are 44 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000135ABD | P32567
MIPS: YMR165C
NCBI: 218488 | 417782 | 6323817 | 825570 | NP_013888.1
GenBank/EMBL/DDBJ: DAA10061.1 | D01095 | Z49705
Amino Acid Sequence (or in FASTA format)
 
       1  MQYVGRALGS VSKTWSSINP ATLSGAIDVI VVEHPDGRLS CSPFHVRFGK
      51  FQILKPSQKK VQVFINEKLS NMPMKLSDSG EAYFVFEMGD QVTDVPDELL
     101  VSPVMSATSS PPQSPETSIL EGGTEGEGEG ENENKKKEKK VLEEPDFLDI
     151  NDTGDSGSKN SETTGSLSPT ESSTTTPPDS VEERKLVEQR TKNFQQKLNK
     201  KLTEIHIPSK LDNNGDLLLD TEGYKPNKNM MHDTDIQLKQ LLKDEFGNDS
     251  DISSFIKEDK NGNIKIVNPY EHLTDLSPPG TPPTMATSGS VLGLDAMESG
     301  STLNSLSSSP SGSDTEDETS FSKEQSSKSE KTSKKGTAGS GETEKRYIRT
     351  IRLTNDQLKC LNLTYGENDL KFSVDHGKAI VTSKLFVWRW DVPIVISDID
     401  GTITKSDALG HVLAMIGKDW THLGVAKLFS EISRNGYNIL YLTARSAGQA
     451  DSTRSYLRSI EQNGSKLPNG PVILSPDRTM AALRREVILK KPEVFKIACL
     501  NDIRSLYFED SDNEVDTEEK STPFFAGFGN RITDALSYRT VGIPSSRIFT
     551  INTEGEVHME LLELAGYRSS YIHINELVDH FFPPVSLDSV DLRTNTSMVP
     601  GSPPNRTLDN FDSEITSGRK TLFRGNQEEK FTDVNFWRDP LVDIDNLSDI
     651  SNDDSDNIDE DTDVSQQSNI SRNRANSVKT AKVTKAPQRN VSGSTNNNEV
     701  LAASSDVENA SDLVSSHSSS GSTPNKSTMS KGDIGKQIYL ELGSPLASPK
     751  LRYLDDMDDE DSNYNRTKSR RASSAAATSI DKEFKKLSVS KAGAPTRIVS
     801  KINVSNDVHS LGNSDTESRR EQSVNETGRN QLPHNSMDDK DLDSRVSDEF
     851  DDDEFDEDEF ED*

external links for Pah1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Pah1p
1) Han GS, et al.  (2006) The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J Biol Chem 281(14):9210-8
2) Irie K, et al.  (1993) A gene, SMP2, involved in plasmid maintenance and respiration in Saccharomyces cerevisiae encodes a highly charged protein. Mol Gen Genet 236(2-3):283-8
3) Santos-Rosa H, et al.  (2005) The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J 24(11):1931-41
4) Karanasios E, et al.  (2010) A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc Natl Acad Sci U S A 107(41):17539-44
5) Adeyo O, et al.  (2011) The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets. J Cell Biol 192(6):1043-55
6) Choi HS, et al.  (2012) Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism. J Biol Chem 287(14):11290-301
7) Su WM, et al.  (2012) Protein kinase A-mediated phosphorylation of Pah1p phosphatidate phosphatase functions in conjunction with the Pho85p-Pho80p and Cdc28p-cyclin B kinases to regulate lipid synthesis in yeast. J Biol Chem 287(40):33364-76
8) Grimsey N, et al.  (2008) Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2. J Biol Chem 283(43):29166-74
9) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41