MFN2
entrez
9927
canonical
uniprot
O95140
canonical
ensembl
ENSG00000116688
resolver
ensp
ENSP00000235329
resolver
ensp
ENSP00000502151
resolver
ensp
ENSP00000637459
resolver
ensp
ENSP00000637460
resolver
ensp
ENSP00000637464
resolver
ensp
ENSP00000637467
resolver
ensp
ENSP00000637473
resolver
genesymbol
MFN2
resolver
genesymbol_syn
CPRP1
resolver
genesymbol_syn
KIAA0214
resolver
hgnc
HGNC:16877
resolver
uniprot
A8K1B3
resolver
uniprot
O95572
resolver
uniprot
Q5JXC3
resolver
uniprot
Q5JXC4
resolver
uniprot
Q9H131
resolver
uniprot
Q9NSX8
resolver
uniprot_entry
MFN2_HUMAN
resolver
uniprot_sec
A8K1B3
resolver
uniprot_sec
O95572
resolver
uniprot_sec
Q5JXC3
resolver
uniprot_sec
Q5JXC4
resolver
uniprot_sec
Q9H131
resolver
uniprot_sec
Q9NSX8
resolver
amino_acid_sequence
MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHMAAREQQVYCEEMREERQDRLKFIDKQLELLAQDYKLRIKQITEEVERQVSTAMAEEIRRLSVLVDDYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAITNSLQTMQQDMIDGLKPLLPVSVRSQIDMLVPRQCFSLNYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALMGYNDQVQRPIPLTPANPSMPPLPQGSLTQEEFMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTKAKERAFKRQFVEHASEKLQLVISYTGSNCSHQVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2A2B (CMT2A2B) [MIM:617087]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2A2B is a severe form with autosomal recessive inheritance. {ECO:0000269|PubMed:18458227, ECO:0000269|PubMed:20008656, ECO:0000269|PubMed:20350294, ECO:0000269|PubMed:21715711, ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:26955893, ECO:0000269|PubMed:34193129}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Charcot-Marie-Tooth disease, axonal, type 2A2A (CMT2A2A) [MIM:609260]: An autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:15064763, ECO:0000269|PubMed:15549395, ECO:0000269|PubMed:16087932, ECO:0000269|PubMed:16762064, ECO:0000269|PubMed:16835246, ECO:0000269|PubMed:18425620, ECO:0000269|PubMed:18946002, ECO:0000269|PubMed:19889647, ECO:0000269|PubMed:20008656, ECO:0000269|PubMed:20350294, ECO:0000269|PubMed:22206013}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuropathy, hereditary motor and sensory, 6A, with optic atrophy (HMSN6A) [MIM:601152]: An autosomal dominant neurologic disorder characterized by optic atrophy and peripheral sensorimotor neuropathy manifesting as axonal Charcot-Marie-Tooth disease. Charcot-Marie-Tooth disease is a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. It is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies and primary peripheral axonal neuropathies. Peripheral axonal neuropathies are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, and normal or slightly reduced nerve conduction velocities. {ECO:0000269|PubMed:16437557, ECO:0000269|PubMed:16835246, ECO:0000269|PubMed:19889647, ECO:0000269|PubMed:20008656, ECO:0000269|PubMed:20350294, ECO:0000269|PubMed:24604904, ECO:0000269|PubMed:26085578}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lipomatosis, multiple symmetric, with or without peripheral neuropathy (MSL) [MIM:151800]: An autosomal recessive disorder characterized by the growth of unencapsulated, lipomatous masses affecting the upper body, especially the cervical and thoracic regions. Lipomatosis can be disfiguring, and lipoma growth around the neck may cause difficulty swallowing or breathing. The age at onset ranges from childhood to young adulthood. Some patients develop distal muscle weakness and atrophy due to axonal peripheral neuropathy. {ECO:0000269|PubMed:18458227, ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:28414270}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity). {ECO:0000250|UniProtKB:Q80U63, ECO:0000250|UniProtKB:Q8R500, ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:19889647, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26085578, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:28114303, ECO:0000305}.
uniprot
proteins
mass_dalton
86402
uniprot
proteins
mutagenesis
MUTAGEN 109; /note="K->A,T: Does not affect its ability to cluster mitochondria; when overexpressed."; /evidence="ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885"; MUTAGEN 110; /note="S->N: Does not affect its ability to cluster mitochondria; when overexpressed."; /evidence="ECO:0000269|PubMed:11950885"; MUTAGEN 111; /note="T->A: Diminishes interaction with PRKN in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PRKN in presence of PINK1; when associated with Ala-442."; /evidence="ECO:0000269|PubMed:23620051"; MUTAGEN 111; /note="T->E: Interacts with PRKN in absence of PINK1; when associated with Glu-442."; /evidence="ECO:0000269|PubMed:23620051"; MUTAGEN 128; /note="H->A: Loss of function in promoting mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 230; /note="E->A: Loss of function in promoting mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 259; /note="R->A: Loss of function in promoting mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 259; /note="R->L: Does not affect its ability to cluster mitochondria; when overexpressed."; /evidence="ECO:0000269|PubMed:11950885"; MUTAGEN 260; /note="W->A: Loss of function in promoting mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 266; /note="E->A: Loss of function in promoting mitochondrial fusion."; /evidence="ECO:0000269|PubMed:28114303"; MUTAGEN 442; /note="S->A: Diminishes interaction with PRKN in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PRKN in presence of PINK1; when associated with Ala-111."; /evidence="ECO:0000269|PubMed:23620051"; MUTAGEN 442; /note="S->E: Interacts with PRKN in absence of PINK1; when associated with Glu-111."; /evidence="ECO:0000269|PubMed:23620051"; MUTAGEN 622..624; /note="GGV->AAL: Does not affect the targeting to mitochondrial outer membrane."; /evidence="ECO:0000269|PubMed:11181170"; MUTAGEN 622..624; /note="GGV->RRE: Abolishes the targeting to mitochondrial outer membrane."; /evidence="ECO:0000269|PubMed:11181170"; MUTAGEN 657..659; /note="KER->TGV: Does not affect the targeting to mitochondrial outer membrane."; /evidence="ECO:0000269|PubMed:11181170
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PINK1. {ECO:0000269|PubMed:23620051}.; PTM: Ubiquitinated by non-degradative ubiquitin by PRKN, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion (PubMed:23620051). Ubiquitinated by HUWE1 when dietary stearate (C18:0) levels are low; ubiquitination inhibits mitochondrial fusion (PubMed:26214738, PubMed:30217973). {ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26214738, ECO:0000269|PubMed:30217973}.
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
11950885
uniprot
proteins
pubmed
12499352
uniprot
proteins
pubmed
12598526
uniprot
proteins
pubmed
12759376
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15064763
uniprot
proteins
pubmed
15322553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15549395
uniprot
proteins
pubmed
16087932
uniprot
proteins
pubmed
16437557
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16762064
uniprot
proteins
pubmed
16835246
uniprot
proteins
pubmed
17121834
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18425620
uniprot
proteins
pubmed
18458227
uniprot
proteins
pubmed
18946002
uniprot
proteins
pubmed
19889647
uniprot
proteins
pubmed
20008656
uniprot
proteins
pubmed
20350294
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21715711
uniprot
proteins
pubmed
22206013
uniprot
proteins
pubmed
23620051
uniprot
proteins
pubmed
24604904
uniprot
proteins
pubmed
24627108
uniprot
proteins
pubmed
25008184
uniprot
proteins
pubmed
26085578
uniprot
proteins
pubmed
26214738
uniprot
proteins
pubmed
26316991
uniprot
proteins
pubmed
26955893
uniprot
proteins
pubmed
28114303
uniprot
proteins
pubmed
28414270
uniprot
proteins
pubmed
30217973
uniprot
proteins
pubmed
34193129
uniprot
proteins
pubmed
38843396
uniprot
proteins
pubmed
9039502
uniprot
proteins
sequence_length
757
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:26214738}; Multi-pass membrane protein {ECO:0000269|PubMed:11181170, ECO:0000269|PubMed:11950885, ECO:0000269|PubMed:12499352, ECO:0000269|PubMed:23620051}. Note=Colocalizes with BAX during apoptosis. {ECO:0000269|PubMed:12499352}.
uniprot
proteins
transmembrane_region
TRANSMEM 605..625; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 627..647; /note="Helical; Name=2"; /evidence="ECO:0000255
uniprot
proteins