Basic Information

NameHeat shock protein SSC3, mitochondrial (Extracellular mutant protein 10)
Uniprot IDP39987
Systematic gene nameYEL030W
Standard gene nameECM10
Gene namesECM10 SSC3 YEL030W
Description from SGDYEL030W ECM10 SGDID:S000000756, Chr V from 94644-96578, Genome Release 64-3-1, Verified ORF, "Heat shock protein of the Hsp70 family; localized in mitochondrial nucleoids, plays a role in protein translocation, interacts with Mge1p in an ATP-dependent manner; overexpression induces extensive mitochondrial DNA aggregations; ECM10 has a paralog, SSC1, that arose from the whole genome duplication"
Protein length644
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLPSWKAFKA HNILRILTRF QSTKIPDAVI GIDLGTTNSA VAIMEGKVPR
IIENAEGSRT TPSVVAFTKD GERLVGEPAK RQSVINSENT LFATKRLIGR
RFEDAEVQRD INQVPFKIVK HSNGDAWVEA RNRTYSPAQI GGFILNKMKE
TAEAYLAKSV KNAVVTVPAY FNDAQRQATK DAGQIIGLNV LRVVNEPTAA
ALAYGLDKSE PKVIAVFDLG GGTFDISILD IDNGIFEVKS TNGDTHLGGE
DFDIYLLQEI ISHFKKETGI DLSNDRMAVQ RIREAAEKAK IELSSTLSTE
INLPFITADA AGPKHIRMPF SRVQLENITA PLIDRTVDPV KKALKDARIT
ASDISDVLLV GGMSRMPKVA DTVKKLFGKD ASKAVNPDEA VALGAAIQAA
VLSGEVTDVL LLDVTPLSLG IETLGGVFTK LIPRNSTIPN KKSQIFSTAA
SGQTSVEVKV FQGERELVKD NKLIGNFTLA GIPPAPKGTP QIEVTFDIDA
NGIINVSAKD LASHKDSSIT VAGASGLSDT EIDRMVNEAE RYKNQDRARR
NAIETANKAD QLANDTENSI KEFEGKLDKT DSQRLKDQIS SLRELVSRSQ
AGDEVNDDDV GTKIDNLRTS SMKLFEQLYK NSDNPETKNG RENK

Legend

  • X Phoshorylation
  • X K-acetylation
  • X K-Succinylation
  • X Monomethylation

Structure

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


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References

[58, 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)
[60, 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)
[60, 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)
[61, 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)
[69, 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)
[120, 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)
[122, 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)
[122, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[341, 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)
[342, 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)
[350, 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)
[350, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[352, 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)
[352, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[355, 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)
[355, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[364, 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)
[364, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[558, Mono-CH3]Caslavka Zempel, K.E.,  Vashisht, A.A.,  Barshop, W.D.,  Wohlschlegel, J.A.,  Clarke, S.G. (2016). Determining the mitochondrial methyl proteome in Saccharomyces cerevisiae using heavy methyl SILAC. Journal of Proteome Research 15(12): 4436-4451. (Publication) (All modifications)
[558, Mono-CH3]Wang, K., Zhou, Y.J., Liu, H., Cheng, K., Mao, J., Wang, F., Liu, W., Ye, M., Zhao, Z.K., Zou, H. (2015). Proteomic analysis of protein methylation in the yeast Saccharomyces cerevisiae. J Proteomics 114: 226-233. (Publication) (All modifications)