Basic Information
Name | Dynamin-like GTPase MGM1, mitochondrial (Mitochondrial division and morphology protein 17) (Mitochondrial genome maintenance protein 1) [Cleaved into: Dynamin-like GTPase MGM1 large isoform (l-MGM1); Dynamin-like GTPase MGM1 small isoform (s-MGM1)] |
Uniprot ID | P32266 |
Systematic gene name | YOR211C |
Standard gene name | MGM1 |
Gene names | MGM1 MDM17 YOR211C YOR50-1 |
Description from SGD | YOR211C MGM1 SGDID:S000005737, Chr XV from 741569-738924, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial GTPase, present in complex with Ugo1p and Fzo1p; required for mitochondrial morphology, fusion, and genome maintenance; promotes membrane bending; plays a direct role in formation and maintenance of lamellar, but not of tubular, cristae; exists as long and short form with different distributions; ratio of long to short forms is regulated by Psd1p; homolog of human OPA1 involved in autosomal dominant optic atrophy" |
Protein length | 881 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNASPVRLLI LRRQLATHPA ILYSSPYIKS PLVHLHSRMS NVHRSAHANA
LSFVITRRSI SHFPKIISKI IRLPIYVGGG MAAAGSYIAY KMEEASSFTK
DKLDRIKDLG ESMKEKFNKM FSGDKSQDGG HGNDGTVPTA TLIAATSLDD
DESKRQGDPK DDDDEDDDDE DDENDSVDTT QDEMLNLTKQ MIEIRTILNK
VDSSSAHLTL PSIVVIGSQS SGKSSVLESI VGREFLPKGS NMVTRRPIEL
TLVNTPNSNN VTADFPSMRL YNIKDFKEVK RMLMELNMAV PTSEAVSEEP
IQLTIKSSRV PDLSLVDLPG YIQVEAADQP IELKTKIRDL CEKYLTAPNI
ILAISAADVD LANSSALKAS KAADPKGLRT IGVITKLDLV DPEKARSILN
NKKYPLSMGY VGVITKTPSS INRKHLGLFG EAPSSSLSGI FSKGQHGQSS
GEENTNGLKQ IVSHQFEKAY FKENKKYFTN CQVSTKKLRE KLIKILEISM
SNALEPTSTL IQQELDDTSY LFKVEFNDRH LTPKSYLLNN IDVLKLGIKE
FQEKFHRNEL KSILRAELDQ KVLDVLATRY WKDDNLQDLS SSKLESDTDM
LYWHKKLELA SSGLTKMGIG RLSTMLTTNA ILKELDNILE STQLKNHELI
KDLVSNTAIN VLNSKYYSTA DQVENCIKPF KYEIDLEERD WSLARQHSIN
LIKEELRQCN SRYQAIKNAV GSKKLANVMG YLENESNLQK ETLGMSKLLL
ERGSEAIFLD KRCKVLSFRL KMLKNKCHST IEKDRCPEVF LSAVSDKLTS
TAVLFLNVEL LSDFFYNFPI ELDRRLTLLG DEQVEMFAKE DPKISRHIEL
QKRKELLELA LEKIDSILVF KKSYKGVSKN L
LSFVITRRSI SHFPKIISKI IRLPIYVGGG MAAAGSYIAY KMEEASSFTK
DKLDRIKDLG ESMKEKFNKM FSGDKSQDGG HGNDGTVPTA TLIAATSLDD
DESKRQGDPK DDDDEDDDDE DDENDSVDTT QDEMLNLTKQ MIEIRTILNK
VDSSSAHLTL PSIVVIGSQS SGKSSVLESI VGREFLPKGS NMVTRRPIEL
TLVNTPNSNN VTADFPSMRL YNIKDFKEVK RMLMELNMAV PTSEAVSEEP
IQLTIKSSRV PDLSLVDLPG YIQVEAADQP IELKTKIRDL CEKYLTAPNI
ILAISAADVD LANSSALKAS KAADPKGLRT IGVITKLDLV DPEKARSILN
NKKYPLSMGY VGVITKTPSS INRKHLGLFG EAPSSSLSGI FSKGQHGQSS
GEENTNGLKQ IVSHQFEKAY FKENKKYFTN CQVSTKKLRE KLIKILEISM
SNALEPTSTL IQQELDDTSY LFKVEFNDRH LTPKSYLLNN IDVLKLGIKE
FQEKFHRNEL KSILRAELDQ KVLDVLATRY WKDDNLQDLS SSKLESDTDM
LYWHKKLELA SSGLTKMGIG RLSTMLTTNA ILKELDNILE STQLKNHELI
KDLVSNTAIN VLNSKYYSTA DQVENCIKPF KYEIDLEERD WSLARQHSIN
LIKEELRQCN SRYQAIKNAV GSKKLANVMG YLENESNLQK ETLGMSKLLL
ERGSEAIFLD KRCKVLSFRL KMLKNKCHST IEKDRCPEVF LSAVSDKLTS
TAVLFLNVEL LSDFFYNFPI ELDRRLTLLG DEQVEMFAKE DPKISRHIEL
QKRKELLELA LEKIDSILVF KKSYKGVSKN L
Legend
- X K-Succinylation
- X Phoshorylation
- X Ubiquitination
- X SUMOylation
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
[274, K-succ] | Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications) |
[438, 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) |
[438, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[463, 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) |
[549, Ubi] | 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) |
[562, 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) |
[562, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[633, SUMO] | Paasch, F., den Brave, F., Psakhye, I., Pfander, B., Jentsch, S. (2018). Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins. J Biol Chem 293: 599-609. (Publication) (All modifications) |