Basic Information
| Name | Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) |
| Uniprot ID | P12887 |
| Systematic gene name | YML021C |
| Standard gene name | UNG1 |
| Gene names | UNG1 YML021C |
| Description from SGD | YML021C UNG1 SGDID:S000004483, Chr XIII from 230813-229734, Genome Release 64-3-1, reverse complement, Verified ORF, "Uracil-DNA glycosylase; required for repair of uracil in DNA formed by spontaneous cytosine deamination; efficiently excises uracil from single-stranded DNA in vivo; not required for strand-specific mismatch repair; cell-cycle regulated, expressed in late G1; localizes to mitochondria and nucleus" |
| Protein length | 359 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MWCMRRLPTN SVMTVARKRK QTTIEDFFGT KKSTNEAPNK KGKSGATFMT
ITNGAAIKTE TKAVAKEANT DKYPANSNAK DVYSKNLSSN LRTLLSLELE
TIDDSWFPHL MDEFKKPYFV KLKQFVTKEQ ADHTVFPPAK DIYSWTRLTP
FNKVKVVIIG QDPYHNFNQA HGLAFSVKPP TPAPPSLKNI YKELKQEYPD
FVEDNKVGDL THWASQGVLL LNTSLTVRAH NANSHSKHGW ETFTKRVVQL
LIQDREADGK SLVFLLWGNN AIKLVESLLG STSVGSGSKY PNIMVMKSVH
PSPLSASRGF FGTNHFKMIN DWLYNTRGEK MIDWSVVPGT SLREVQEANA
RLESESKDP
ITNGAAIKTE TKAVAKEANT DKYPANSNAK DVYSKNLSSN LRTLLSLELE
TIDDSWFPHL MDEFKKPYFV KLKQFVTKEQ ADHTVFPPAK DIYSWTRLTP
FNKVKVVIIG QDPYHNFNQA HGLAFSVKPP TPAPPSLKNI YKELKQEYPD
FVEDNKVGDL THWASQGVLL LNTSLTVRAH NANSHSKHGW ETFTKRVVQL
LIQDREADGK SLVFLLWGNN AIKLVESLLG STSVGSGSKY PNIMVMKSVH
PSPLSASRGF FGTNHFKMIN DWLYNTRGEK MIDWSVVPGT SLREVQEANA
RLESESKDP
Legend
- X SUMOylation
- X K-acetylation
- 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
| [58, 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) |
| [72, 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) |
| [93, 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) |
| [93, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [105, 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) |
| [105, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
| [223, 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) |
| [324, 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) |
| [324, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |