Basic Information
Name | Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (EC 1.1.1.170) |
Uniprot ID | P53199 |
Systematic gene name | YGL001C |
Standard gene name | ERG26 |
Gene names | ERG26 YGL001C |
Description from SGD | YGL001C ERG26 SGDID:S000002969, Chr VII from 496502-495453, Genome Release 64-3-1, reverse complement, Verified ORF, "C-3 sterol dehydrogenase; catalyzes the second of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; human homolog NSDHL implicated in CK syndrome, and can complement yeast null mutant; molecular target of natural product and antifungal compound FR171456" |
Protein length | 349 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSKIDSVLII GGSGFLGLHL IQQFFDINPK PDIHIFDVRD LPEKLSKQFT
FNVDDIKFHK GDLTSPDDME NAINESKANV VVHCASPMHG QNPDIYDIVN
VKGTRNVIDM CKKCGVNILV YTSSAGVIFN GQDVHNADET WPIPEVPMDA
YNETKAIAED MVLKANDPSS DFYTVALRPA GIFGPGDRQL VPGLRQVAKL
GQSKFQIGDN NNLFDWTYAG NVADAHVLAA QKLLDPKTRT AVSGETFFIT
NDTPTYFWAL ARTVWKADGH IDKHVIVLKR PVAICAGYLS EWVSKMLGKE
PGLTPFRVKI VCAYRYHNIA KAKKLLGYTP RVGIEEGINK TLAWMDEGL
FNVDDIKFHK GDLTSPDDME NAINESKANV VVHCASPMHG QNPDIYDIVN
VKGTRNVIDM CKKCGVNILV YTSSAGVIFN GQDVHNADET WPIPEVPMDA
YNETKAIAED MVLKANDPSS DFYTVALRPA GIFGPGDRQL VPGLRQVAKL
GQSKFQIGDN NNLFDWTYAG NVADAHVLAA QKLLDPKTRT AVSGETFFIT
NDTPTYFWAL ARTVWKADGH IDKHVIVLKR PVAICAGYLS EWVSKMLGKE
PGLTPFRVKI VCAYRYHNIA KAKKLLGYTP RVGIEEGINK TLAWMDEGL
Legend
- X Ubiquitination
- X K-acetylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[44, 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) |
[273, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |