Basic Information
Name | Mitochondrial distribution and morphology protein 10 (Mitochondrial inheritance component MDM10) |
Uniprot ID | P18409 |
Systematic gene name | YAL010C |
Standard gene name | MDM10 |
Gene names | MDM10 YAL010C FUN37 |
Description from SGD | YAL010C MDM10 SGDID:S000000008, Chr I from 135665-134184, Genome Release 64-3-1, reverse complement, Verified ORF, "Subunit of both the ERMES and the SAM complex; component of ERMES complex which acts as a molecular tether between the mitochondria and the ER, necessary for efficient phospholipid exchange between organelles and for mitophagy; SAM/TOB complex component that functions in the assembly of outer membrane beta-barrel proteins; involved in mitochondrial inheritance and morphology; ERMES complex is often co-localized with peroxisomes and concentrated areas of pyruvate dehydrogenase" |
Protein length | 493 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLPYMDQVLR AFYQSTHWST QNSYEDITAT SRTLLDFRIP SAIHLQISNK
STPNTFNSLD FSTRSRINGS LSYLYSDAQQ LEKFMRNSTD IPLQDATETY
RQLQPNLNFS VSSANTLSSD NTTVDNDKKL LHDSKFVKKS LYYGRMYYPS
SDLEAMIIKR LSPQTQFMLK GVSSFKESLN VLTCYFQRDS HRNLQEWIFS
TSDLLCGYRV LHNFLTTPSK FNTSLYNNSS LSLGAEFWLG LVSLSPGCST
TLRYYTHSTN TGRPLTLTLS WNPLFGHISS TYSAKTGTNS TFCAKYDFNL
YSIESNLSFG CEFWQKKHHL LETNKNNNDK LEPISDELVD INPNSRATKL
LHENVPDLNS AVNDIPSTLD IPVHKQKLLN DLTYAFSSSL RKIDEERSTI
EKFDNKINSS IFTSVWKLST SLRDKTLKLL WEGKWRGFLI SAGTELVFTR
GFQESLSDDE KNDNAISISA TDTENGNIPV FPAKFGIQFQ YST
STPNTFNSLD FSTRSRINGS LSYLYSDAQQ LEKFMRNSTD IPLQDATETY
RQLQPNLNFS VSSANTLSSD NTTVDNDKKL LHDSKFVKKS LYYGRMYYPS
SDLEAMIIKR LSPQTQFMLK GVSSFKESLN VLTCYFQRDS HRNLQEWIFS
TSDLLCGYRV LHNFLTTPSK FNTSLYNNSS LSLGAEFWLG LVSLSPGCST
TLRYYTHSTN TGRPLTLTLS WNPLFGHISS TYSAKTGTNS TFCAKYDFNL
YSIESNLSFG CEFWQKKHHL LETNKNNNDK LEPISDELVD INPNSRATKL
LHENVPDLNS AVNDIPSTLD IPVHKQKLLN DLTYAFSSSL RKIDEERSTI
EKFDNKINSS IFTSVWKLST SLRDKTLKLL WEGKWRGFLI SAGTELVFTR
GFQESLSDDE KNDNAISISA TDTENGNIPV FPAKFGIQFQ YST
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[455, 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) |
[455, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[457, 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) |
[457, 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) |
[457, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |