Basic Information

NameAmino-acid acetyltransferase, mitochondrial (EC 2.3.1.1) (Arginine-requiring protein 2) (Glutamate N-acetyltransferase) (N-acetylglutamate synthase) (AGS) (NAGS)
Uniprot IDP40360
Systematic gene nameYJL071W
Standard gene nameARG2
Gene namesARG2 YJL071W HRB574 J1091
Description from SGDYJL071W ARG2 SGDID:S000003607, Chr X from 306132-307856, Genome Release 64-3-1, Verified ORF, "Acetylglutamate synthase (glutamate N-acetyltransferase); mitochondrial enzyme that catalyzes the first step in the biosynthesis of the arginine precursor ornithine; forms a complex with Arg5,6p"
Protein length574
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MWRRIFAHEL KYDQPNASSK NLILSVLNTT ATKREAKDYL SKYTNDSGQH
NHCLFFIRDL HKVAPAILSQ FSSVIKRLGM LGLRPMFVIP PSPTHVNIQA
ELLDSIVTEA DLKPLHLKEG LTKSRTGLYH SVFSQESRFF DIGNSNFIPI
VKPYVYNEET ASEFMTKDVV KFMDCLCQGN IPHIDKFFIL NNAGGIPSGE
RNDNAHVFIN LSQELEHLSS SLSHNISTLT KREPRSQNLL HRMEVYVKKD
EISSLECEYH DHLENLLLMD KVLSNLAATA TGLITTVKAA ALSSDRKNPL
VYNLLTDRSL ISSSLPRFKK KDGEIDSPAN MFDDHAWYEL PSQQVNAAPS
NSDAVLVTTV LKKGVHIKTY DYKTLTQFNS IGLPKKFHVP EKGAKPSSNS
PKLDINKFKS IIDQSFKRSL DLHDYIKRIN GKIATIIVIG DYEGIAILTY
EGSEENSFVY LDKFAVLPHL KGSLGISDII FNLMFKKFPN EILWRSRKDN
VVNKWYFQRS VAVLDLSIDL DPEHCDEKQS QFKLFYYGNP QYAKRALRDK
KRLREFMRSV RDIKPSWENE KNIS

Legend

  • X Phoshorylation
  • X SUMOylation
  • X K-Succinylation

Structure

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


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References

[19, 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)
[19, 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]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]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[29, 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)
[29, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[30, 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)
[30, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[385, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)
[402, SUMO]Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications)
[417, 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)