Basic Information

NameAltered inheritance rate of mitochondria protein 25
Uniprot IDP47140
Systematic gene nameYJR100C
Standard gene nameAIM25
Gene namesAIM25 YJR100C J1946
Description from SGDYJR100C AIM25 SGDID:S000003861, Chr X from 617334-616351, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondria protein of unknown function; interacts genetically with TOR1 to regulate chronological lifespan, and the response to both heat shock and oxidative stress; involved in maintaining the integrity of the mitochondrial network; negative regulator of mitophagy flux; non-tagged protein is detected in purified mitochondria in high-throughput studies; null mutant is viable and displays an elevated frequency of mitochondrial genome loss; similar to murine NOR1"
Protein length327
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MHRTAIFLTY RSCMRNFSTL SKTLTVSSGK VIRNGPFRRV IREKNQITKA
PSVKAFKENS NSGIIKVHDP IATTILNEPT VIIERQIEFM NVFLGFEQAN
RYAIMDVNGN KIASMMERDF SITKAIMRQF YRLHRPFLVD VFDNWGNVIM
TIKRPFSFIN SHIKTIIPPS AYVDNGSDST HYHDGKEGTT VGETIQNWHL
WRRRYELFQK DGVEGSTFDQ FGKIDAPFLS FDFPVTDADG KIMASVDRNW
VGLGREMFTD TGVYVVRFDS QRCFDNIYPT EMLSSQVLTL DQRAVLLANA
VSIDFDYFSR HSRQTGGFLS FGGGYDE

Legend

  • X Phoshorylation

Structure

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


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References

[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)
[177, 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)
[216, 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)
[217, 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)