P36112

Name	MICOS complex subunit MIC60 (Altered inheritance of mitochondria protein 28) (Formation of crista junctions protein 1) (Found in mitochondrial proteome protein 13) (Mitofilin)
Uniprot ID	P36112
Systematic gene name	YKR016W
Standard gene name	MIC60
Gene names	MIC60 AIM28 FCJ1 FMP13 YKR016W
Description from SGD	YKR016W MIC60 SGDID:S000001724, Chr XI from 469717-471339, Genome Release 64-3-1, Verified ORF, "Component of the MICOS complex; MICOS (formerly MINOS or MitOS) is a mitochondrial inner membrane complex that extends into the intermembrane space and has a role in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane; Mic60p is also involved in import of intermembrane space (IMS) proteins, probably by positioning Mia40p relative to the TOM complex to receive incoming proteins; ortholog of mammalian mitofilin"
Protein length	540
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MMLRTTASRK IVLRRGLASI NTGTTVASKK ASHKFRNTLW TIALSATAFY
AGGIIYSQKN DKFGDFFSNN VPFAEDLLET YEHYHDRPTL FLEDSWDGLK
AKSNDLLSGL TGSSQTRRSN RENIEVKKIL SLEPLNIETE NSDPQLKEII
GSLNDLINSL NDSNLSIPES EFNSIKKSNQ NMLTNLSQLN ETLKEALSNY
MIQRTSEVIT ELNTQYENSK REFEKNLQKN LLQEVDEFKE NLTKQKDKEL
EEKLKANEEL LQAKHANEVG LLSITQVKEF NKIIKDKIEK ERNGRLAHLE
EINSEVNDLS KSIDRSSKIL SKNEALVQLT FQVDEIKSRI NNNNLPDVNI
DKELSRLKLL SNLLSTFNKK SCCDDGDCCS CKKGNKNEGK EGKISCKCKP
KTNPPSLLSV ALDELESTCS GKKILSNEQI YNRWNLLADD FKTASLLPPN
SGILGQLTAK VFSLFLFTKT GNPSNATDFD SVYARVGDNL RVSNLNDAVE
EVVSLKGWPH KVCESWIEDA RRKLEVQRLV EILDCEIRTL

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[19, 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)
[19, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[113, 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)
[113, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[128, 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)
[225, 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)
[229, 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)
[241, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[304, 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)
[304, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[310, 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)
[310, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[311, 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)
[352, 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)
[369, 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)
[369, 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)
[423, 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)
[475, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)