Basic Information

NameAcyl-protein thioesterase 1 (EC 3.1.2.-)
Uniprot IDQ12354
Systematic gene nameYLR118C
Standard gene nameTML25
Gene namesTML25 YLR118C L2955
Description from SGDYLR118C TML25 SGDID:S000004108, Chr XII from 385408-384725, Genome Release 64-3-1, reverse complement, Verified ORF, "Acyl-protein thioesterase responsible for depalmitoylation of Gpa1p; green fluorescent protein (GFP)-fusion protein localizes to both the cytoplasm and nucleus and is induced in response to the DNA-damaging agent MMS"
Protein length227
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MNGLRVAAKI QPARQTIIFL HGLGDTGSGW GFLAQYLQQR DPAAFQHTNF
VFPNAPELHV TANGGALMPA WFDILEWDPS FSKVDSDGFM NSLNSIEKTV
KQEIDKGIKP EQIIIGGFSQ GAALALATSV TLPWKIGGIV ALSGFCSIPG
ILKQHKNGIN VKTPIFHGHG DMDPVVPIGL GIKAKQFYQD SCEIQNYEFK
VYKGMAHSTV PDELEDLASF IKKSLSS

Legend

  • X SUMOylation
  • 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

[185, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[208, 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)
[208, 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)
[208, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[208, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[209, 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)
[209, 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)
[209, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[209, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)