Basic Information
Name | Putative esterase YMR210W (EC 3.1.1.-) |
Uniprot ID | Q03649 |
Systematic gene name | YMR210W |
Standard gene name | MGL2 |
Gene names | MGL2 YMR210W YM8261.04 |
Description from SGD | YMR210W MGL2 SGDID:S000004823, Chr XIII from 687516-688865, Genome Release 64-3-1, Verified ORF, "Monoacylglycerol and triacylglycerol lipase; MAG lipase with preference for palmitoyl-MAG; TAG lipase involved in TAG catabolism; minor role in medium-chain fatty acid ethyl ester biosynthesis; contains an alpha/beta hydrolase domain and a typical lipase motif (GXSXG); similar to acyltransferases, Eeb1p, Eht1p, and human ABHD1" |
Protein length | 449 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MRLKELLPNF LIVHQEVPED PIAFKSTDKR ENENKEITIP ELIDTKVPEL
ADGATDTLYG LLVNGHLQTA YGSFRHFDNI YKVQYKRMII KYPHGGEGTV
DFAVNGRSTK RRKVEKEYVP TSQPVFNGNL KRRYSYYSPD DPKLNSDDAK
PMLIILHGLT GGSRESYVRA IVHEITTKYD FEACVFNARG CCYSAITTPL
LYNGGWTNDI RYCVNDLRKR FPNRKFYMMG FSLGASIMTN YLGEESDRTK
IECAISVSNP FDLYNSAYFI NSTPMGSRFY SPALGHNLLR MVRNHLSTLE
ENPDFKDVIE KHLKKIRTVR QFDNLLTGPM FGYKNAEEYY KNASSYKRIP
GIRTPFIALH AQDDPIVGGD LPIDQIKSNP YTLLLETSTG GHVGWFKDRS
GRRWYAEPLC RFLKIFHDEI TVKGLKPDLE NVQLPDPNCE PIATTFRAN
ADGATDTLYG LLVNGHLQTA YGSFRHFDNI YKVQYKRMII KYPHGGEGTV
DFAVNGRSTK RRKVEKEYVP TSQPVFNGNL KRRYSYYSPD DPKLNSDDAK
PMLIILHGLT GGSRESYVRA IVHEITTKYD FEACVFNARG CCYSAITTPL
LYNGGWTNDI RYCVNDLRKR FPNRKFYMMG FSLGASIMTN YLGEESDRTK
IECAISVSNP FDLYNSAYFI NSTPMGSRFY SPALGHNLLR MVRNHLSTLE
ENPDFKDVIE KHLKKIRTVR QFDNLLTGPM FGYKNAEEYY KNASSYKRIP
GIRTPFIALH AQDDPIVGGD LPIDQIKSNP YTLLLETSTG GHVGWFKDRS
GRRWYAEPLC RFLKIFHDEI TVKGLKPDLE NVQLPDPNCE PIATTFRAN
Legend
- X Ubiquitination
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[82, 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) |
[131, 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) |
[135, 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) |
[135, 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) |
[135, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[138, 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) |