Basic Information

Name54S ribosomal protein L11, mitochondrial (Mitochondrial large ribosomal subunit protein uL10m) (YmL11)
Uniprot IDP36521
Systematic gene nameYDL202W
Standard gene nameMRPL11
Gene namesMRPL11 YDL202W D1070
Description from SGDYDL202W MRPL11 SGDID:S000002361, Chr IV from 98475-99224, Genome Release 64-3-1, Verified ORF, "Mitochondrial ribosomal protein of the large subunit; localizes to vacuole in response to H2O2"
Protein length249
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLQLRFMPGW VPRNGFFGLK ETIGTVHKRF YALASEQPSR KTVKPLDSRK
TFLIDTYKHL MENSSMIFFV HYNNLSKTED HHFRFKIKQT GGKLTKVRNN
LFEVYLRNSH LPDPCGFVKR KEQNWKHPLL PLLKGPTATI TYEDTNPQQV
AKLLKVLQSA QDKLMVIGAK VENEVLNVEK INTFKTLPTK PEMQSQLVSV
LQMLSGLGLV RTLENSSNAL YLTLKSHNDN QKPKEDVEST TDAESKGSK

Legend

  • X Phoshorylation
  • 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

[25, 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)
[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)
[152, 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)
[155, 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)
[239, Phos]Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications)
[239, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[241, Phos]Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications)
[241, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[245, Phos]Guo X, Niemi NM, Hutchins PD, et al (2017b) Ptc7p dephosphorylates select mitochondrial proteins to enhance metabolic function. Cell Reports 18:307–313. (Publication) (All modifications)
[245, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)