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Sphingolipid long chain base-responsive protein PIL1

 PIL1_YEAST              Reviewed;         339 AA.
P53252; D6VUL8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
18-SEP-2019, entry version 150.
RecName: Full=Sphingolipid long chain base-responsive protein PIL1;
Name=PIL1; OrderedLocusNames=YGR086C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 45-56; 85-103; 166-192 AND 197-221, AND
IDENTIFICATION BY MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
FUNCTION, AND PHOSPHORYLATION BY PKH1 AND PHK2.
PubMed=15016821; DOI=10.1074/jbc.m400299200;
Zhang X., Lester R.L., Dickson R.C.;
"Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent
protein kinase-like kinase Pkh1p and downstream signaling pathways
Pkc1p and Ypk1p.";
J. Biol. Chem. 279:22030-22038(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND THR-233, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-230 AND
THR-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-16; SER-45;
SER-98; SER-163; THR-233 AND SER-299, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Negative regulator of cell wall integrity (CWI) in
unstressed cells, probably by inhibiting protein kinase PKH1/PHK2
activity and regulating their downstream CWI pathways PKC1-MAP
kinase pathway and protein kinase YPK1 pathway. Activity may be
regulated by the transient increase of sphingolipid long chain
bases (LCBs) during heat stress. {ECO:0000269|PubMed:15016821}.
-!- INTERACTION:
Q05050:EIS1; NbExp=3; IntAct=EBI-23225, EBI-28061;
Q12230:LSP1; NbExp=6; IntAct=EBI-23225, EBI-34978;
P35719:MRP8; NbExp=3; IntAct=EBI-23225, EBI-16255;
Q03407:PKH1; NbExp=4; IntAct=EBI-23225, EBI-32467;
-!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095}.
-!- PTM: Phosphorylated by PKH1 and PKH2. Phosphorylation is inhibited
by sphingolipid long chain bases (LCBs).
{ECO:0000269|PubMed:15016821}.
-!- MISCELLANEOUS: Present with 2157 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; Z72871; CAA97088.1; -; Genomic_DNA.
EMBL; BK006941; DAA08179.1; -; Genomic_DNA.
PIR; S64381; S64381.
RefSeq; NP_011600.3; NM_001181215.3.
SMR; P53252; -.
BioGrid; 33328; 264.
DIP; DIP-4618N; -.
IntAct; P53252; 45.
MINT; P53252; -.
STRING; 4932.YGR086C; -.
iPTMnet; P53252; -.
MaxQB; P53252; -.
PaxDb; P53252; -.
PRIDE; P53252; -.
EnsemblFungi; YGR086C_mRNA; YGR086C; YGR086C.
GeneID; 852977; -.
KEGG; sce:YGR086C; -.
EuPathDB; FungiDB:YGR086C; -.
SGD; S000003318; PIL1.
HOGENOM; HOG000214828; -.
InParanoid; P53252; -.
OMA; ALNDWTL; -.
BioCyc; YEAST:G3O-30798-MONOMER; -.
PRO; PR:P53252; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0071944; C:cell periphery; HDA:SGD.
GO; GO:0005737; C:cytoplasm; HDA:SGD.
GO; GO:0032126; C:eisosome; IDA:SGD.
GO; GO:0036286; C:eisosome filament; IBA:GO_Central.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
GO; GO:0005739; C:mitochondrion; HDA:SGD.
GO; GO:0005886; C:plasma membrane; HDA:SGD.
GO; GO:0008289; F:lipid binding; IDA:SGD.
GO; GO:0070941; P:eisosome assembly; IMP:SGD.
GO; GO:0006897; P:endocytosis; IMP:SGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:SGD.
GO; GO:0008104; P:protein localization; IMP:SGD.
GO; GO:0097446; P:protein localization to eisosome filament; IMP:SGD.
GO; GO:0009408; P:response to heat; IMP:SGD.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR028245; PIL1/LSP1.
PANTHER; PTHR31962; PTHR31962; 1.
Pfam; PF13805; Pil1; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Lipid droplet; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 339 Sphingolipid long chain base-responsive
protein PIL1.
/FTId=PRO_0000058441.
COMPBIAS 21 25 Poly-Pro.
COMPBIAS 279 323 Glu-rich.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 233 233 Phosphothreonine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:17761666,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
SEQUENCE 339 AA; 38349 MW; C86AE5ABB508EA03 CRC64;
MHRTYSLRNS RAPTASQLQN PPPPPSTTKG RFFGKGGLAY SFRRSAAGAF GPELSRKLSQ
LVKIEKNVLR SMELTANERR DAAKQLSIWG LENDDDVSDI TDKLGVLIYE VSELDDQFID
RYDQYRLTLK SIRDIEGSVQ PSRDRKDKIT DKIAYLKYKD PQSPKIEVLE QELVRAEAES
LVAEAQLSNI TRSKLRAAFN YQFDSIIEHS EKIALIAGYG KALLELLDDS PVTPGETRPA
YDGYEASKQI IIDAESALNE WTLDSAQVKP TLSFKQDYED FEPEEGEEEE EEDGQGRWSE
DEQEDGQIEE PEQEEEGAVE EHEQVGHQQS ESLPQQTTA


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