Basic Information

NameProbable alanine aminotransferase, mitochondrial (EC 2.6.1.2) (Glutamate pyruvate transaminase) (GPT) (Glutamic--alanine transaminase) (Glutamic--pyruvic transaminase)
Uniprot IDP52893
Systematic gene nameYLR089C
Standard gene nameALT1
Gene namesALT1 YLR089C L9449.15
Description from SGDYLR089C ALT1 SGDID:S000004079, Chr XII from 320015-318237, Genome Release 64-3-1, reverse complement, Verified ORF, "Alanine transaminase (glutamic pyruvic transaminase); involved in alanine biosynthesis and catabolism; TOR1-independent role in determining chronological lifespan; expression is induced in the presence of alanine; repression is mediated by Nrg1p; ALT1 has a paralog, ALT2, that arose from the whole genome duplication; Alt2p is catalytically inactive"
Protein length592
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLSLSAKNHF TVSNSITHVI KSYHIRTLTS SAEKMPHITT PFSTSASSTK
LKAFRKVRPV LQRHSSSWIV AQNHRRSLSG QSSLNDLRHL NRFPHHTLKT
SNNEFYPAEQ LTLEDVNENV LKAKYAVRGA IPMRAEELKA QLEKDPQSLP
FDRIINANIG NPQQLQQKPL TYYRQVLSLL QYPELLNQNE QQLVDSKLFK
LDAIKRAKSL MEDIGGSVGA YSSSQGVEGI RKSVAEFITK RDEGEISYPE
DIFLTAGASA AVNYLLSIFC RGPETGVLIP IPQYPLYTAT LALNNSQALP
YYLDENSGWS TNPEEIETVV KEAIQNEIKP TVLVVINPGN PTGAVLSPES
IAQIFEVAAK YGTVVIADEV YQENIFPGTK FHSMKKILRH LQREHPGKFD
NVQLASLHST SKGVSGECGQ RGGYMELTGF SHEMRQVILK LASISLCPVV
TGQALVDLMV RPPVEGEESF ESDQAERNSI HEKLITRAMT LYETFNSLEG
IECQKPQGAM YLFPKIDLPF KAVQEARHLE LTPDEFYCKK LLESTGICTV
PGSGFGQEPG TYHLRTTFLA PGLEWIKKWE SFHKEFFDQY RD

Legend

  • X Phoshorylation
  • X K-Succinylation
  • X Multiple modifications
  • X K-benzoylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[40, 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)
[40, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[77, 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)
[77, 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)
[77, 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)
[77, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[77, 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)
[77, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[77, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[79, 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)
[79, 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)
[79, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[79, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[82, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[83, 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)
[83, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[144, 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)
[200, K-succ]Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications)
[200, 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)
[415, 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)
[415, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[479, 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)
[483, 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)
[483, 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)
[511, 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)
[515, K-bz]Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications)
[521, 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)
[521, K-bz]Wang, D., Yan, F., Wu, P., Ge, K., Li, M., Li, T., Gao, Y., Peng, C., Chen, Y. (2022). Global profiling of regulatory elements in the histone benzoylation pathway. Nature Communications 13(1):1369 (Publication) (All modifications)
[539, 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)