Basic Information
Name | NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) |
Uniprot ID | P33327 |
Systematic gene name | YDL215C |
Standard gene name | GDH2 |
Gene names | GDH2 YDL215C D0892 |
Description from SGD | YDL215C GDH2 SGDID:S000002374, Chr IV from 73918-70640, Genome Release 64-3-1, reverse complement, Verified ORF, "NAD(+)-dependent glutamate dehydrogenase; degrades glutamate to ammonia and alpha-ketoglutarate; expression sensitive to nitrogen catabolite repression and intracellular ammonia levels; genetically interacts with GDH3 by suppressing stress-induced apoptosis" |
Protein length | 1092 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLFDNKNRGA LNSLNTPDIA SLSISSMSDY HVFDFPGKDL QREEVIDLLD
QQGFIPDDLI EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF
FAKSKFNGIQ PRLFSIKNKI ITNDNHAIFM ESNTGVSISD SQQKNFKFAS
DAVGNDTLEH GKDTIKKNRI EMDDSCPPYE LDSEIDDLFL DNKSQKNCRL
VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI ESISDKTMYK
VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR
YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH
DVEAALKQVE REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH
FVNRLGSDYQ NLLSQITIKR NDTTLLEIVE NLKRKLRNET LTQQTIINIM
SKHYTIISKL YKNFAQIHYY HNSTKDMEKT LSFQRLEKVE PFKNDQEFEA
YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS FRLDPSLVMT
KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK
NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD
AMIDILINDP LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP
WWKSFLTGKS PSLGGIPHDE YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ
TGGPDGDLGS NEILLSSPNE CYLAILDGSG VLCDPKGLDK DELCRLAHER
KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR NTFHTQIFKF
VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA
KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG
ERSALYKSYV VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI
NKLNDDLVAS QELWLNDLKL RNYLLLDKII PKILIDVAGP QSVLENIPES
YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF IGGLKREAEA SA
QQGFIPDDLI EQEVDWFYNS LGIDDLFFSR ESPQLISNII HSLYASKLDF
FAKSKFNGIQ PRLFSIKNKI ITNDNHAIFM ESNTGVSISD SQQKNFKFAS
DAVGNDTLEH GKDTIKKNRI EMDDSCPPYE LDSEIDDLFL DNKSQKNCRL
VSFWAPESEL KLTFVYESVY PNDDPAGVDI SSQDLLKGDI ESISDKTMYK
VSSNENKKLY GLLLKLVKER EGPVIKTTRS VENKDEIRLL VAYKRFTTKR
YYSALNSLFH YYKLKPSKFY LESFNVKDDD IIIFSVYLNE NQQLEDVLLH
DVEAALKQVE REASLLYAIP NNSFHEVYQR RQFSPKEAIY AHIGAIFINH
FVNRLGSDYQ NLLSQITIKR NDTTLLEIVE NLKRKLRNET LTQQTIINIM
SKHYTIISKL YKNFAQIHYY HNSTKDMEKT LSFQRLEKVE PFKNDQEFEA
YLNKFIPNDS PDLLILKTLN IFNKSILKTN FFITRKVAIS FRLDPSLVMT
KFEYPETPYG IFFVVGNTFK GFHIRFRDIA RGGIRIVCSR NQDIYDLNSK
NVIDENYQLA STQQRKNKDI PEGGSKGVIL LNPGLVEHDQ TFVAFSQYVD
AMIDILINDP LKENYVNLLP KEEILFFGPD EGTAGFVDWA TNHARVRNCP
WWKSFLTGKS PSLGGIPHDE YGMTSLGVRA YVNKIYETLN LTNSTVYKFQ
TGGPDGDLGS NEILLSSPNE CYLAILDGSG VLCDPKGLDK DELCRLAHER
KMISDFDTSK LSNNGFFVSV DAMDIMLPNG TIVANGTTFR NTFHTQIFKF
VDHVDIFVPC GGRPNSITLN NLHYFVDEKT GKCKIPYIVE GANLFITQPA
KNALEEHGCI LFKDASANKG GVTSSSMEVL ASLALNDNDF VHKFIGDVSG
ERSALYKSYV VEVQSRIQKN AELEFGQLWN LNQLNGTHIS EISNQLSFTI
NKLNDDLVAS QELWLNDLKL RNYLLLDKII PKILIDVAGP QSVLENIPES
YLKVLLSSYL SSTFVYQNGI DVNIGKFLEF IGGLKREAEA SA
Legend
- X Phoshorylation
- X SUMOylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[21, 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) |
[21, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[23, 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) |
[23, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[25, 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) |
[25, 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) |
[25, 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) |
[25, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[26, 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) |
[26, 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) |
[26, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[28, 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) |
[28, 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) |
[28, 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) |
[28, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[150, 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) |
[157, 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) |
[242, 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) |
[242, 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) |
[242, 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) |
[242, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[480, 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) |
[480, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[482, 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) |
[482, 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) |
[482, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[482, 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) |
[482, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[482, Phos] | Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jenö, P., Hall, M.N. (2010). The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Molecular Biology of the Cell 21(19): 3475-3486. (Publication) (All modifications) |
[482, 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) |
[482, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[504, 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) |
[510, Phos] | 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) |
[517, 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) |
[518, Phos] | 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) |
[524, 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) |
[1023, 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) |
[1023, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |