Basic Information

NameMitochondrial presequence protease (EC 3.4.24.-) (Cytosolic metalloprotease 1) (Metalloprotease of 112 kDa)
Uniprot IDP32898
Systematic gene nameYDR430C
Standard gene nameCYM1
Gene namesCYM1 MOP112 YDR430C D9461.18
Description from SGDYDR430C CYM1 SGDID:S000002838, Chr IV from 1328470-1325501, Genome Release 64-3-1, reverse complement, Verified ORF, "Lysine-specific metalloprotease of the pitrilysin family; metalloprotease of the intermembrane space; degrades proteins and presequence peptides cleaved from imported proteins; required for normal mitochondrial morphology; mutation in human homolog PITRM1 is implicated in autosomal recessive spinocerebellar ataxias (ARCA)"
Protein length989
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLRFQRFASS YAQAQAVRKY PVGGIFHGYE VRRILPVPEL RLTAVDLVHS
QTGAEHLHID RDDKNNVFSI AFKTNPPDST GVPHILEHTT LCGSVKYPVR
DPFFKMLNKS LANFMNAMTG PDYTFFPFST TNPQDFANLR GVYLDSTLNP
LLKQEDFDQE GWRLEHKNIT DPESNIVFKG VVYNEMKGQI SNANYYFWSK
FQQSIYPSLN NSGGDPMKIT DLRYGDLLDF HHKNYHPSNA KTFTYGNLPL
VDTLKQLNEQ FSGYGKRARK DKLLMPIDLK KDIDVKLLGQ IDTMLPPEKQ
TKASMTWICG APQDTYDTFL LKVLGNLLMD GHSSVMYQKL IESGIGLEFS
VNSGVEPTTA VNLLTVGIQG VSDIEIFKDT VNNIFQNLLE TEHPFDRKRI
DAIIEQLELS KKDQKADFGL QLLYSILPGW TNKIDPFESL LFEDVLQRFR
GDLETKGDTL FQDLIRKYIV HKPCFTFSIQ GSEEFSKSLD DEEQTRLREK
ITALDEQDKK NIFKRGILLQ EKQNEKEDLS CLPTLQIKDI PRAGDKYSIE
QKNNTMSRIT DTNGITYVRG KRLLNDIIPF ELFPYLPLFA ESLTNLGTTT
ESFSEIEDQI KLHTGGISTH VEVTSDPNTT EPRLIFGFDG WSLNSKTDHI
FEFWSKILLE TDFHKNSDKL KVLIRLLASS NTSSVADAGH AFARGYSAAH
YRSSGAINET LNGIEQLQFI NRLHSLLDNE ETFQREVVDK LTELQKYIVD
TNNMNFFITS DSDVQAKTVE SQISKFMERL PHGSCLPNGP KTSDYPLIGS
KCKHTLIKFP FQVHYTSQAL LGVPYTHKDG SALQVMSNML TFKHLHREVR
EKGGAYGGGA SYSALAGIFS FYSYRDPQPL KSLETFKNSG RYILNDAKWG
VTDLDEAKLT IFQQVDAPKS PKGEGVTYFM SGVTDDMKQA RREQLLDVSL
LDVHRVAEKY LLNKEGVSTV IGPGIEGKTV SPNWEVKEL

Legend

  • X Phoshorylation
  • X Multiple modifications
  • 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

[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)
[645, 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)
[647, 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)
[887, 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)
[887, 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)
[919, 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)
[920, 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)
[920, 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)
[920, Phos]Ohlmeier S, Hiltunen JK, Bergmann U (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31:2869–2881. (Publication) (All modifications)
[920, 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)
[920, Phos]Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications)
[920, 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)
[920, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[920, 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)
[920, Phos]Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications)
[920, Phos]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[920, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[927, 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)
[927, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[928, 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)
[928, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[981, Phos]Ohlmeier S, Hiltunen JK, Bergmann U (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31:2869–2881. (Publication) (All modifications)
[981, 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)
[981, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)