Basic Information

NameMeiotic sister chromatid recombination protein 1
Uniprot IDQ03104
Systematic gene nameYML128C
Standard gene nameMSC1
Gene namesMSC1 YML128C YM4987.07C
Description from SGDYML128C MSC1 SGDID:S000004597, Chr XIII from 16676-15135, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein of unknown function; mutant is defective in directing meiotic recombination events to homologous chromatids; the authentic, non-tagged protein is detected in highly purified mitochondria and is phosphorylated"
Protein length513
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MKQFKLVNAV SASFVLIGLV LANSDSVFDK WTQEDLADYL RDNKKSLEKY
ATDSIEDLKT EASQVWDKHA QPKPWWQVWS SDSSSVSNSN PGWFGYTGSS
DHPVSDWLFD TWSTDSLRNF LKKNGVDVDD AKASKDSLVK TAKENFNKIS
KSLKSSGYYP SSSYFDSWST KDLQNWLNDN GIDYDKAVQS KDELVQKVKE
NIYRTSEKAE QQRLGLLESL DLAHQQILDT SGQIKDTVFD KWSSDQLTNW
LESHKVNIDK NMAKKHDYLV RMAKENSANL KDDIYWYLDY MKRESSPFLT
KTPEYVGSVW DSSKNFLTNL YSKFRGKTDN VINDTFLVGL DSWPKDKLKM
FLDARGIKYS MLSTEHQLRE LVKKSRNEKL KILPKDYQKY FDNSNWSLDD
IKGWFADKKD DFQDSQTYST IMQDFDKVSK NTNDAKDQIA KTWSNTFQSW
SQEDLLQYLK SFGVPVKQTS TKDDLINLAK QNTQWLFGTV KEPAYKRYLH
NVKNWSKSIL GFN

Legend

  • X K-acetylation
  • X Phoshorylation
  • X Glycosylation
  • 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

[68, 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)
[137, 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)
[137, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[237, Phos]Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications)
[237, 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)
[237, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[243, Phos]Reinders J, Wagner K, Zahedit RP, et al (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Molecular and Cellular Proteomics 6:1896–1906. (Publication) (All modifications)
[243, 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)
[243, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[295, 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)
[333, Glyc]Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[394, 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)
[394, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[395, Glyc]Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[415, 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)
[415, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[417, 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)
[417, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)