Basic Information
Name | Membrane-anchored lipid-binding protein LAM1 (Lipid transfer protein anchored at membrane contact sites 1) (Yeast suicide protein 1) |
Uniprot ID | P38851 |
Systematic gene name | YHR155W |
Standard gene name | LAM1 |
Gene names | LAM1 YSP1 YHR155W |
Description from SGD | YHR155W LAM1 SGDID:S000001198, Chr VIII from 407103-410789, Genome Release 64-3-1, Verified ORF, "Putative sterol transfer protein; localizes to puncta in the cortical ER; probable role in retrograde transport of sterols from the plasma membrane to the ER; one of six StART-like domain-containing proteins in yeast that may be involved in sterol transfer between intracellular membranes; conserved across eukaryotes; contains GRAM, StART-like (VASt) and two PH-like domains" |
Protein length | 1228 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MHEHKAELRL ITVALNEAST DSPSFRASVN YFHTRMESLS SWMHSTVDYV
ENTYKPSFQD FQRIKETLFS QLLPSPILLS NGFVSNQPYT PLLVRDFTRD
VSDLSNTVMK IILGDENSQY TAALSALSSD AINPYFNKRK TFEYYQRKYD
SFLTDFLAAT NDGNTLIPQN LQNETFKLVD IKHKYIEASL DLTEAISLMK
VNLDKFLIET IDIVRKNNVI TTKDTKDVID ITPELTETLK DWTDWIESNL
QTLQALSSKL SEAKYAILKL SLARMKPSRL IQDYDLKSIQ NLKFNLPKSI
SNGNNSEEKG LSGWLYMKTT VGHDPKRVVW VRRWCFLQNN VFGVFSLSPS
KTYVEETDKF GILWITVEYL PKEPRNFCFK LRIQNPNCKT EEENTYIDII
LQAESIDELK SWINTLTSHK RIALSIKEEN DPRYQLARKK IEPQFFEFAS
SSSTSTDKLL TSFSSKTLTL VEELKKNYMS EDDIYSIIDN KAYHLRVIST
PIATQLTHLA LFSTFLSVSN YYPCATQANT WGTANWNDLS YLVNPLKGSS
VHKPATVSNS SRFSVSYPDY YPYSLKVDDI QFRSIFFSVN HDFLQVPKEL
VLLRYSSVWC PNNKQKFASM AFVTLNHIYV YLNISGFSYL RRIDLLDIDS
IEYDKSPKHV SSRMLHMQRG DGLRFNMSVF FTDRRAVASK LQFLIENKAM
HIPKGEKEVL EIFQELDEEI ENEKKIIKDN LSESEHYSKD YDYLLKSTYD
HHFENTNETP MELMSRKLRL EREAWCYFQD NFKVGSKTLF HVLFGDKSQV
FPSSLFLCKK GSNLNNNSYW ERIRRAKEDA SCQFELCRKL QFQLNRTSNF
IKDLLWLKDD NDNFKLVLQQ RVTKIKQGYY FEVEEGPIIV KFPLCHPLLL
RVRFIIAECI TSQGESLKKC DLAILYDFNY VESIDKLNTK VEKLWLFERI
HLNWALRYCK LEHSEINRKT REYLKKFNDR EKMSDVIKLC GFLGVLPKER
IENDEKAGDF MQPVYINYDF LSLSKIFTKL TVFYLSSVII KTMKVLLAMV
MVIFKCFSKV NKTLYYCLLI SAVTNLFFVG KSIHSYFSVK SAETLFQNYA
NGDQRGLQIM HRSLTVPDLN LLTRKMMDND QENPVFKRFD EDKNAYQYKG
TRQEIAIKRN QVLTELKILQ NTEKELVQGS YRKFIITERD KCITTQNEIF
DLWINDTKLQ DYCMACFAEY NRLSAIPV
ENTYKPSFQD FQRIKETLFS QLLPSPILLS NGFVSNQPYT PLLVRDFTRD
VSDLSNTVMK IILGDENSQY TAALSALSSD AINPYFNKRK TFEYYQRKYD
SFLTDFLAAT NDGNTLIPQN LQNETFKLVD IKHKYIEASL DLTEAISLMK
VNLDKFLIET IDIVRKNNVI TTKDTKDVID ITPELTETLK DWTDWIESNL
QTLQALSSKL SEAKYAILKL SLARMKPSRL IQDYDLKSIQ NLKFNLPKSI
SNGNNSEEKG LSGWLYMKTT VGHDPKRVVW VRRWCFLQNN VFGVFSLSPS
KTYVEETDKF GILWITVEYL PKEPRNFCFK LRIQNPNCKT EEENTYIDII
LQAESIDELK SWINTLTSHK RIALSIKEEN DPRYQLARKK IEPQFFEFAS
SSSTSTDKLL TSFSSKTLTL VEELKKNYMS EDDIYSIIDN KAYHLRVIST
PIATQLTHLA LFSTFLSVSN YYPCATQANT WGTANWNDLS YLVNPLKGSS
VHKPATVSNS SRFSVSYPDY YPYSLKVDDI QFRSIFFSVN HDFLQVPKEL
VLLRYSSVWC PNNKQKFASM AFVTLNHIYV YLNISGFSYL RRIDLLDIDS
IEYDKSPKHV SSRMLHMQRG DGLRFNMSVF FTDRRAVASK LQFLIENKAM
HIPKGEKEVL EIFQELDEEI ENEKKIIKDN LSESEHYSKD YDYLLKSTYD
HHFENTNETP MELMSRKLRL EREAWCYFQD NFKVGSKTLF HVLFGDKSQV
FPSSLFLCKK GSNLNNNSYW ERIRRAKEDA SCQFELCRKL QFQLNRTSNF
IKDLLWLKDD NDNFKLVLQQ RVTKIKQGYY FEVEEGPIIV KFPLCHPLLL
RVRFIIAECI TSQGESLKKC DLAILYDFNY VESIDKLNTK VEKLWLFERI
HLNWALRYCK LEHSEINRKT REYLKKFNDR EKMSDVIKLC GFLGVLPKER
IENDEKAGDF MQPVYINYDF LSLSKIFTKL TVFYLSSVII KTMKVLLAMV
MVIFKCFSKV NKTLYYCLLI SAVTNLFFVG KSIHSYFSVK SAETLFQNYA
NGDQRGLQIM HRSLTVPDLN LLTRKMMDND QENPVFKRFD EDKNAYQYKG
TRQEIAIKRN QVLTELKILQ NTEKELVQGS YRKFIITERD KCITTQNEIF
DLWINDTKLQ DYCMACFAEY NRLSAIPV
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[38, 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) |
[38, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[45, 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) |
[45, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[49, 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) |
[49, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[53, 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) |
[53, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[54, 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) |
[54, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[145, 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) |
[145, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[185, 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) |
[185, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[189, 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) |
[189, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[232, 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) |
[236, 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) |
[411, 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) |
[411, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[415, 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) |
[415, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[418, 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) |
[418, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[732, 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) |
[732, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[732, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[732, 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) |
[732, 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) |
[732, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[732, Phos] | 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) |
[732, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[734, 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) |
[734, Phos] | Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications) |
[734, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1036, 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) |
[1036, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[1037, 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) |
[1037, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |