Basic Information
Name | Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC 3.1.2.2) (Peroxisomal long-chain acyl-CoA thioesterase 1) |
Uniprot ID | P41903 |
Systematic gene name | YJR019C |
Standard gene name | TES1 |
Gene names | TES1 PTE1 YJR019C J1456 |
Description from SGD | YJR019C TES1 SGDID:S000003780, Chr X from 468281-467232, Genome Release 64-3-1, reverse complement, Verified ORF, "Peroxisomal acyl-CoA thioesterase; likely to be involved in fatty acid oxidation rather than fatty acid synthesis; conserved protein also found in human peroxisomes; TES1 mRNA levels increase during growth on fatty acids" |
Protein length | 349 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSASKMAMSN LEKILELVPL SPTSFVTKYL PAAPVGSKGT FGGTLVSQSL
LASLHTVPLN FFPTSLHSYF IKGGDPRTKI TYHVQNLRNG RNFIHKQVSA
YQHDKLIFTS MILFAVQRSK EHDSLQHWET IPGLQGKQPD PHRYEEATSL
FQKEVLDPQK LSRYASLSDR FQDATSMSKY VDAFQYGVME YQFPKDMFYS
ARHTDELDYF VKVRPPITTV EHAGDESSLH KHHPYRIPKS ITPENDARYN
YVAFAYLSDS YLLLTIPYFH NLPLYCHSFS VSLDHTIYFH QLPHVNNWIY
LKISNPRSHW DKHLVQGKYF DTQSGRIMAS VSQEGYVVYG SERDIRAKF
LASLHTVPLN FFPTSLHSYF IKGGDPRTKI TYHVQNLRNG RNFIHKQVSA
YQHDKLIFTS MILFAVQRSK EHDSLQHWET IPGLQGKQPD PHRYEEATSL
FQKEVLDPQK LSRYASLSDR FQDATSMSKY VDAFQYGVME YQFPKDMFYS
ARHTDELDYF VKVRPPITTV EHAGDESSLH KHHPYRIPKS ITPENDARYN
YVAFAYLSDS YLLLTIPYFH NLPLYCHSFS VSLDHTIYFH QLPHVNNWIY
LKISNPRSHW DKHLVQGKYF DTQSGRIMAS VSQEGYVVYG SERDIRAKF
Legend
- X Ubiquitination
- 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
[239, 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) |
[242, Phos] | Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications) |
[242, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |