Basic Information

NameNADP-specific glutamate dehydrogenase 2 (NADP-GDH 2) (EC 1.4.1.4) (NADP-dependent glutamate dehydrogenase 2)
Uniprot IDP39708
Systematic gene nameYAL062W
Standard gene nameGDH3
Gene namesGDH3 YAL062W FUN51
Description from SGDYAL062W GDH3 SGDID:S000000058, Chr I from 31567-32940, Genome Release 64-3-1, Verified ORF, "NADP(+)-dependent glutamate dehydrogenase; synthesizes glutamate from ammonia and alpha-ketoglutarate; rate of alpha-ketoglutarate utilization differs from Gdh1p; expression regulated by nitrogen and carbon sources; GDH3 has a paralog, GDH1, that arose from the whole genome duplication"
Protein length457
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MTSEPEFQQA YDEIVSSVED SKIFEKFPQY KKVLPIVSVP ERIIQFRVTW
ENDNGEQEVA QGYRVQFNSA KGPYKGGLRF HPSVNLSILK FLGFEQIFKN
ALTGLDMGGG KGGLCVDLKG KSDNEIRRIC YAFMRELSRH IGKDTDVPAG
DIGVGGREIG YLFGAYRSYK NSWEGVLTGK GLNWGGSLIR PEATGFGLVY
YTQAMIDYAT NGKESFEGKR VTISGSGNVA QYAALKVIEL GGIVVSLSDS
KGCIISETGI TSEQIHDIAS AKIRFKSLEE IVDEYSTFSE SKMKYVAGAR
PWTHVSNVDI ALPCATQNEV SGDEAKALVA SGVKFVAEGA NMGSTPEAIS
VFETARSTAT NAKDAVWFGP PKAANLGGVA VSGLEMAQNS QKVTWTAERV
DQELKKIMIN CFNDCIQAAQ EYSTEKNTNT LPSLVKGANI ASFVMVADAM
LDQGDVF

Legend

  • X Phoshorylation
  • X Ubiquitination
  • 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

[69, 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)
[75, 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)
[90, 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)
[289, 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)
[289, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[292, 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)
[294, 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)
[357, 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)