MFN1
entrez
55669
canonical
uniprot
Q8IWA4
canonical
ensembl
ENSG00000171109
resolver
ensp
ENSP00000419926
resolver
ensp
ENSP00000420617
resolver
ensp
ENSP00000567727
resolver
genesymbol
MFN1
resolver
hgnc
HGNC:18262
resolver
uniprot
A0A0C4DFN1
resolver
uniprot
B2RAR1
resolver
uniprot
D3DNR6
resolver
uniprot
O15323
resolver
uniprot
O60639
resolver
uniprot
Q9BZB5
resolver
uniprot
Q9NWQ2
resolver
uniprot_entry
MFN1_HUMAN
resolver
uniprot_sec
A0A0C4DFN1
resolver
uniprot_sec
B2RAR1
resolver
uniprot_sec
D3DNR6
resolver
uniprot_sec
O15323
resolver
uniprot_sec
O60639
resolver
uniprot_sec
Q9BZB5
resolver
uniprot_sec
Q9NWQ2
resolver
amino_acid_sequence
MAEPVSPLKHFVLAKKAITAIFDQLLEFVTEGSHFVEATYKNPELDRIATEDDLVEMQGYKDKLSIIGEVLSRRHMKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHITNCFLSVEGTDGDKAYLMTEGSDEKKSVKTVNQLAHALHMDKDLKAGCLVRVFWPKAKCALLRDDLVLVDSPGTDVTTELDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERLSKPNIFILNNRWDASASEPEYMEDVRRQHMERCLHFLVEELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESGVALAEGFHARLQEFQNFEQIFEECISQSAVKTKFEQHTIRAKQILATVKNIMDSVNLAAEDKRHYSVEEREDQIDRLDFIRNQMNLLTLDVKKKIKEVTEEVANKVSCAMTDEICRLSVLVDEFCSEFHPNPDVLKIYKSELNKHIEDGMGRNLADRCTDEVNALVLQTQQEIIENLKPLLPAGIQDKLHTLIPCKKFDLSYNLNYHKLCSDFQEDIVFRFSLGWSSLVHRFLGPRNAQRVLLGLSEPIFQLPRSLASTPTAPTTPATPDNASQEELMITLVTGLASVTSRTSMGIIIVGGVIWKTIGWKLLSVSLTMYGALYLYERLSWTTHAKERAFKQQFVNYATEKLRMIVSSTSANCSHQVKQQIATTFARLCQQVDITQKQLEEEIARLPKEIDQLEKIQNNSKLLRNKAVQLENELENFTKQFLPSSNEES
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12475957, PubMed:12759376, PubMed:27920125, PubMed:28114303). Membrane clustering requires GTPase activity (PubMed:27920125). It may involve a major rearrangement of the coiled coil domains (PubMed:27920125, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:12475957, PubMed:12759376). Overexpression induces the formation of mitochondrial networks (in vitro) (PubMed:12759376). Has low GTPase activity (PubMed:27920125, PubMed:28114303). {ECO:0000269|PubMed:12475957, ECO:0000269|PubMed:12759376, ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303}.
uniprot
proteins
mass_dalton
84160
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="K->A: Decreases GTPase activity. Impairs mitochondrial fusion."; /evidence="ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303"; MUTAGEN 74; /note="R->P: Mildly decreases GTPase activity and impairs mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 88; /note="K->A: Abolishes GTPase activity. Abolishes dimerization."; /evidence="ECO:0000269|PubMed:27920125"; MUTAGEN 88; /note="K->T: Induces a strong decrease in mitochondrial clustering."; /evidence="ECO:0000269|PubMed:12759376"; MUTAGEN 99; /note="K->A: Mildly decreases GTPase activity."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 102; /note="P->L: Impairs protein folding. Decreases GTPase activity."; /evidence="ECO:0000269|PubMed:27920125"; MUTAGEN 107; /note="H->A: Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 109; /note="T->A: Acts as a dominant negative mutant; induces fragmentation of mitochondria."; /evidence="ECO:0000269|PubMed:12759376"; MUTAGEN 144; /note="H->A: Abolishes GTPase activity. Abolishes dimerization."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 173; /note="D->A: Decreases GTPase activity."; /evidence="ECO:0000269|PubMed:27920125"; MUTAGEN 189; /note="D->A: Causes mitochondrial clumping."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 209; /note="E->A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 238; /note="R->A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 239; /note="W->A: Abolishes GTP binding and GTPase activity. Loss of function in mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 245; /note="E->A: Decreases GTPase activity. Abolishes dimerization. Impairs mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 309; /note="G->P: Mildly decreases GTPase activity and impairs mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 328; /note="I->A: Slightly decreases GTPase activity."; /evidence="ECO:0000269|PubMed:27920125"; MUTAGEN 336; /note="K->N: Loss of function in mitochondrial fusion. Abolishes dimerization. Decreases GTPase activity."; /evidence="ECO:0000269|PubMed:27920125"; MUTAGEN 336; /note="K->P: Decreases GTPase activity and impairs mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 705; /note="L->P: Impairs protein folding. Decreases GTPase activity."; /evidence="ECO:0000269|PubMed:27920125, ECO:0000269|PubMed:28114303"; MUTAGEN 733; /note="F->P: Impairs protein folding."; /evidence="ECO:0000269|PubMed:27920125
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by non-degradative ubiquitin by PRKN (PubMed:23933751). Deubiquitination by USP30 inhibits mitochondrial fusion (By similarity). Ubiquitinated by MARCHF5 (PubMed:20103533). When mitochondria are depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7 and PRKN (PubMed:23933751). {ECO:0000250|UniProtKB:Q811U4, ECO:0000269|PubMed:20103533, ECO:0000269|PubMed:23933751}.
uniprot
proteins
protein_family
Dynamin/Fzo/YdjA family
uniprot
proteins
protein_family
Mitofusin subfamily
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
11181170
uniprot
proteins
pubmed
11751411
uniprot
proteins
pubmed
11950885
uniprot
proteins
pubmed
12475957
uniprot
proteins
pubmed
12759376
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
20103533
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23933751
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25008184
uniprot
proteins
pubmed
27920125
uniprot
proteins
pubmed
28114303
uniprot
proteins
pubmed
9230308
uniprot
proteins
sequence_length
741
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:12759376, ECO:0000305|PubMed:27920125}; Multi-pass membrane protein {ECO:0000305|PubMed:12759376}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11751411}.
uniprot
proteins
transmembrane_region
TRANSMEM 585..605; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 609..629; /note="Helical; Name=2"; /evidence="ECO:0000255
uniprot
proteins