Basic Information

NameMitochondrial escape protein 2 (Protein RNA12)
Uniprot IDP32843
Systematic gene nameYMR302C
Standard gene nameYME2
Gene namesYME2 PRP12 RNA12 YMR302C YM9952.04C
Description from SGDYMR302C YME2 SGDID:S000004917, Chr XIII from 872625-870073, Genome Release 64-3-1, reverse complement, Verified ORF, "Integral inner mitochondrial membrane protein; role in maintaining mitochondrial nucleoid structure and number; mutants exhibit an increased rate of mitochondrial DNA escape; shows some sequence similarity to exonucleases"
Protein length850
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLLVRTTSLN VSRMPVPCLA RGIGILKGKY RLANLMNAQP SVRHVSSEIQ
QKDQQAGESN TATDTGVIHK SDEETLIYFD NVYARTTSVW NPTLWYNLLL
RNQSRDAVRE KIRNLASPPN NPIYGLELKS TIPVKRDGGV FATFVVPPKY
TKAQVNSLIQ QNTARESSKN LLSYFTRASA FPVKGSPWIE DLRRLPSTTI
VIKFQGPALT EEEIYSLFRR YGTIIDIFPP TAANNNVAKV RYRSFRGAIS
AKNCVSGIEI HNTVLHIQYE NIRRGHLVSN FFTNHTRIAI PVLFALLSIF
AVLVFDPIRE FSIEQKITHK YSLSWDNKFW KQLKTLTSST MTSIKYYWGG
PDDNHQRKHL WEERIEKVND LKMWLEENNN TFVVIRGPRG SGKHDLVMQH
TLQNRANVLY LDCDKLIKSR TDPMFLKNAA SQLGYFPIFP WIDSVTGVLD
LTVQGLTGQK TGLSETKESR FRNMLTTSLM SIRRIALKNY KAFVSTGDGT
VNVKEEDYLQ QHPEAKPVIV IDRFEGKSEI NGFVYKELSD WAAMLVQMNI
AHVIFLTETV ASNQRLSESL PNQVFKNLIL SDASKENSRN YVLSQLEDYL
YYNKKSKGEN VKEPESEKET AENNDSDSEA DTSVKKAEVI LNEKELQEID
ASLEPLGGRM LDLQAFVRRV KSGEEPSEAV DKMIEQASEQ ITQMFLSDKI
DSNKSAQAWE LIELLSANPV IPFHEIVNKP LFKAAPETGI MELENNGLIT
VSRDRGVLQE IRPAKPLYRA AFTYLINDPE LAKVLKTRYL LKVVGFETGR
IKKWEEELKP LGKVPDQKLF KTRLDYLSGK INASNAVITK CEEEIKNLSK

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

[620, Phos]Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[620, 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)
[620, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[632, Phos]Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[632, 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)
[632, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[652, 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)