Basic Information
Name | ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Nicotinamide nucleotide repair protein 2) |
Uniprot ID | P36059 |
Systematic gene name | YKL151C |
Standard gene name | NNR2 |
Gene names | NNR2 YKL151C YKL606 |
Description from SGD | YKL151C NNR2 SGDID:S000001634, Chr XI from 165930-164917, Genome Release 64-3-1, reverse complement, Verified ORF, "Widely-conserved NADHX dehydratase; converts (S)-NADHX to NADH in ATP-dependent manner; YKL151C promoter contains STREs (stress response elements) and expression is induced by heat shock or methyl methanesulfonate; downstream intergenic region drives antisense expression and mediates coordinated regulation of YKL151C and GPM1 phosphoglycerate mutase; protein abundance increases in response to DNA replication stress; homolog of Carkd in mammals and C-terminus of YjeF in E.coli" |
Protein length | 337 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLAELSHREL IKLAQKRCIP PLLPKFHKGQ SGGRVCIIGG CEDYTGAPYF
SANATALMGC DLTHVICEYN AGTVIKSYTP NLMVHPYLRM SNTKLDVDMD
EQRKKINSLL DRIHVVVIGP GLGRDPLMLK SIKDIIRYIL EKHEGKIPLV
IDADGLFLVT QDSEVKEMLK SYPKGRVILT PNVVEFKRLC DAIGKKGDSH
SEMGSLIAQE LNCIVVEKGQ SDKIFSPDSE KDMLTNSEEG SNKRVGGQGD
TLTGAISCML AFSRAMYDFK ICEQEEKGES SNDKPLKNWV DYAMLSCYAG
CTITRECSRL GFKAKGRAMQ TTDLNDRVGE VFAKLFG
SANATALMGC DLTHVICEYN AGTVIKSYTP NLMVHPYLRM SNTKLDVDMD
EQRKKINSLL DRIHVVVIGP GLGRDPLMLK SIKDIIRYIL EKHEGKIPLV
IDADGLFLVT QDSEVKEMLK SYPKGRVILT PNVVEFKRLC DAIGKKGDSH
SEMGSLIAQE LNCIVVEKGQ SDKIFSPDSE KDMLTNSEEG SNKRVGGQGD
TLTGAISCML AFSRAMYDFK ICEQEEKGES SNDKPLKNWV DYAMLSCYAG
CTITRECSRL GFKAKGRAMQ TTDLNDRVGE VFAKLFG
Legend
- X Phoshorylation
- X K-acetylation
- X Multiple modifications
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
[6, 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) |
[6, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[6, 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) |
[6, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[6, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[142, 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) |
[187, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[187, 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) |
[226, 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) |
[280, 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) |
[280, 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) |
[280, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[281, 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) |
[281, 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) |
[281, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[308, 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) |