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O95140

- MFN2_HUMAN

UniProt

O95140 - MFN2_HUMAN

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Protein

Mitofusin-2

Gene

MFN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN2 acts independently of the cytoskeleton. It therefore plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Overexpression induces the formation of mitochondrial networks. Plays an important role in the regulation of vascular smooth muscle cell proliferation. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PARK2 recruitment to dysfunctional mitochondria. Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress. Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions.5 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi103 – 1108GTPCurated
Nucleotide bindingi199 – 2035GTPCurated
Nucleotide bindingi258 – 2614GTPCurated

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. autophagy Source: UniProtKB-KW
  3. blastocyst formation Source: Ensembl
  4. blood coagulation Source: Reactome
  5. camera-type eye morphogenesis Source: Ensembl
  6. mitochondrial fusion Source: UniProtKB
  7. mitochondrial membrane organization Source: UniProtKB
  8. mitochondrion localization Source: UniProtKB
  9. negative regulation of Ras protein signal transduction Source: UniProtKB
  10. negative regulation of smooth muscle cell proliferation Source: UniProtKB
  11. protein localization to pre-autophagosomal structure Source: MGI
  12. protein targeting to mitochondrion Source: UniProtKB
  13. response to unfolded protein Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Autophagy, Unfolded protein response

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Protein family/group databases

TCDBi9.B.25.2.1. the mitochondrial inner/outer membrane fusion (mmf) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin-2 (EC:3.6.5.-)
Alternative name(s):
Transmembrane GTPase MFN2
Gene namesi
Name:MFN2
Synonyms:CPRP1, KIAA0214
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16877. MFN2.

Subcellular locationi

Mitochondrion outer membrane 4 Publications; Multi-pass membrane protein 4 Publications
Note: Colocalizes with BAX during apoptosis.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. intrinsic component of mitochondrial outer membrane Source: UniProtKB
  4. microtubule cytoskeleton Source: Ensembl
  5. mitochondrial outer membrane Source: Reactome
  6. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 2A2 (CMT2A2) [MIM:609260]: 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. Nerve conduction velocities are normal or slightly reduced.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691V → F in CMT2A2; in a Turkish family. 1 Publication
Corresponds to variant rs28940296 [ dbSNP | Ensembl ].
VAR_018607
Natural varianti76 – 761L → P in CMT2A2; in a European family. 1 Publication
Corresponds to variant rs28940293 [ dbSNP | Ensembl ].
VAR_018608
Natural varianti94 – 941R → Q in CMT2A2; in a Japanese and Russian kindred. 1 Publication
Corresponds to variant rs28940291 [ dbSNP | Ensembl ].
VAR_018609
Natural varianti233 – 2331L → V in CMT2A2. 1 Publication
VAR_067088
Natural varianti251 – 2511P → A in CMT2A2. 1 Publication
Corresponds to variant rs28940295 [ dbSNP | Ensembl ].
VAR_018610
Natural varianti280 – 2801R → H in CMT2A2. 1 Publication
Corresponds to variant rs28940294 [ dbSNP | Ensembl ].
VAR_018611
Natural varianti357 – 3571K → N in CMT2A2. 1 Publication
VAR_022464
Natural varianti364 – 3641R → W in CMT6 and CMT2A2. 2 Publications
VAR_029880
Natural varianti740 – 7401W → S in CMT2A2; in a European family. 1 Publication
Corresponds to variant rs28940292 [ dbSNP | Ensembl ].
VAR_018612
Natural varianti744 – 7441E → M in CMT2A2; requires 2 nucleotide substitutions. 1 Publication
VAR_067089
Charcot-Marie-Tooth disease 6 (CMT6) [MIM:601152]: A form of Charcot-Marie-Tooth disease characterized by the association of axonal peripheral neuropathy with optic atrophy. 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, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941R → W in CMT6. 1 Publication
VAR_029876
Natural varianti206 – 2061T → I in CMT6. 1 Publication
VAR_029877
Natural varianti276 – 2761Q → R in CMT6. 1 Publication
VAR_029878
Natural varianti361 – 3611H → Y in CMT6. 1 Publication
VAR_029879
Natural varianti364 – 3641R → W in CMT6 and CMT2A2. 2 Publications
VAR_029880

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091K → A or T: Does not affect its ability to cluster mitochondria; when overexpressed. 2 Publications
Mutagenesisi110 – 1101S → N: Does not affect its ability to cluster mitochondria; when overexpressed. 1 Publication
Mutagenesisi111 – 1111T → A: Diminishes interaction with PARK2 in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PARK2 in presence of PINK1; when associated with ALA-442. 1 Publication
Mutagenesisi111 – 1111T → E: Interacts with PARK2 in absence of PINK1; when associated with GLU-442. 1 Publication
Mutagenesisi259 – 2591R → L: Does not affect its ability to cluster mitochondria; when overexpressed. 1 Publication
Mutagenesisi442 – 4421S → A: Diminishes interaction with PARK2 in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PARK2 in presence of PINK1; when associated with ALA-111. 1 Publication
Mutagenesisi442 – 4421S → E: Interacts with PARK2 in absence of PINK1; when associated with GLU-111. 1 Publication
Mutagenesisi622 – 6243GGV → AAL: Does not affect the targeting to mitochondrial outer membrane. 1 Publication
Mutagenesisi622 – 6243GGV → RRE: Abolishes the targeting to mitochondrial outer membrane. 1 Publication
Mutagenesisi657 – 6593KER → TGV: Does not affect the targeting to mitochondrial outer membrane. 1 Publication

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi601152. phenotype.
609260. phenotype.
Orphaneti99947. Autosomal dominant Charcot-Marie-Tooth disease type 2A2.
1215. Autosomal dominant optic atrophy plus syndrome.
64751. Hereditary motor and sensory neuropathy type 5.
90120. Hereditary motor and sensory neuropathy type 6.
90118. Severe early-onset axonal neuropathy due to MFN2 deficiency.
PharmGKBiPA134986046.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 757757Mitofusin-2PRO_0000127675Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphothreonine; by PINK11 Publication
Modified residuei442 – 4421Phosphoserine; by PINK11 Publication

Post-translational modificationi

Phosphorylated by PINK1.1 Publication
Ubiquitinated by non-degradative ubiquitin by PARK2, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95140.
PaxDbiO95140.
PRIDEiO95140.

PTM databases

PhosphoSiteiO95140.

Expressioni

Tissue specificityi

Ubiquitous; expressed at low level. Highly expressed in heart and kidney.2 Publications

Gene expression databases

BgeeiO95140.
CleanExiHS_MFN2.
ExpressionAtlasiO95140. baseline and differential.
GenevestigatoriO95140.

Organism-specific databases

HPAiHPA030554.

Interactioni

Subunit structurei

Forms homomultimers and heteromultimers with MFN1. Oligomerization, which is mediated by the second coiled coil region, may play an essential role in mitochondrion fusion. Interacts with VAT1. Interacts with STOML2; may form heterooligomers. Interacts (phosphorylated) with PARK2. Interacts with EIF2AK3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-3324756,EBI-5323863

Protein-protein interaction databases

BioGridi115255. 10 interactions.
DIPiDIP-42832N.
IntActiO95140. 6 interactions.
MINTiMINT-3002608.
STRINGi9606.ENSP00000235329.

Structurei

3D structure databases

ProteinModelPortaliO95140.
SMRiO95140. Positions 695-754.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 604604CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini626 – 6261Mitochondrial intermembraneSequence Analysis
Topological domaini648 – 757110CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei605 – 62521Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei627 – 64721Helical; Name=2Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 342250Dynamin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili391 – 43444Sequence AnalysisAdd
BLAST
Coiled coili695 – 73844Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00390000013727.
HOGENOMiHOG000231098.
HOVERGENiHBG052465.
InParanoidiO95140.
KOiK06030.
OMAiSTLMVTE.
OrthoDBiEOG7HB58M.
PhylomeDBiO95140.
TreeFamiTF314289.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR001401. Dynamin_GTPase.
IPR006884. Fzo/mitofusin_HR2.
IPR027089. Mitofusin-2.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF1. PTHR10465:SF1. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95140) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLLFSRCNS IVTVKKNKRH MAEVNASPLK HFVTAKKKIN GIFEQLGAYI
60 70 80 90 100
QESATFLEDT YRNAELDPVT TEEQVLDVKG YLSKVRGISE VLARRHMKVA
110 120 130 140 150
FFGRTSNGKS TVINAMLWDK VLPSGIGHTT NCFLRVEGTD GHEAFLLTEG
160 170 180 190 200
SEEKRSAKTV NQLAHALHQD KQLHAGSLVS VMWPNSKCPL LKDDLVLMDS
210 220 230 240 250
PGIDVTTELD SWIDKFCLDA DVFVLVANSE STLMQTEKHF FHKVSERLSR
260 270 280 290 300
PNIFILNNRW DASASEPEYM EEVRRQHMER CTSFLVDELG VVDRSQAGDR
310 320 330 340 350
IFFVSAKEVL NARIQKAQGM PEGGGALAEG FQVRMFEFQN FERRFEECIS
360 370 380 390 400
QSAVKTKFEQ HTVRAKQIAE AVRLIMDSLH MAAREQQVYC EEMREERQDR
410 420 430 440 450
LKFIDKQLEL LAQDYKLRIK QITEEVERQV STAMAEEIRR LSVLVDDYQM
460 470 480 490 500
DFHPSPVVLK VYKNELHRHI EEGLGRNMSD RCSTAITNSL QTMQQDMIDG
510 520 530 540 550
LKPLLPVSVR SQIDMLVPRQ CFSLNYDLNC DKLCADFQED IEFHFSLGWT
560 570 580 590 600
MLVNRFLGPK NSRRALMGYN DQVQRPIPLT PANPSMPPLP QGSLTQEEFM
610 620 630 640 650
VSMVTGLASL TSRTSMGILV VGGVVWKAVG WRLIALSFGL YGLLYVYERL
660 670 680 690 700
TWTTKAKERA FKRQFVEHAS EKLQLVISYT GSNCSHQVQQ ELSGTFAHLC
710 720 730 740 750
QQVDVTRENL EQEIAAMNKK IEVLDSLQSK AKLLRNKAGW LDSELNMFTH

QYLQPSR
Length:757
Mass (Da):86,402
Last modified:May 24, 2004 - v3
Checksum:i6F859D740152DFAD
GO
Isoform 2 (identifier: O95140-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.
     303-324: FVSAKEVLNARIQKAQGMPEGG → MHPHLSTLSLPRRRSMAFLSSW
     705-757: VTRENLEQEI...FTHQYLQPSR → GETLSERSMAKSTLMLLTLLFLCSFAGAQDVLTQ

Note: No experimental confirmation available.

Show »
Length:436
Mass (Da):50,041
Checksum:iB3DA00C339C353C8
GO

Sequence cautioni

The sequence CAB70866.2 differs from that shown. Reason: Frameshift at position 581.
The sequence BAA34389.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti521 – 5211C → P in AAD02058. (PubMed:15322553)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691V → F in CMT2A2; in a Turkish family. 1 Publication
Corresponds to variant rs28940296 [ dbSNP | Ensembl ].
VAR_018607
Natural varianti76 – 761L → P in CMT2A2; in a European family. 1 Publication
Corresponds to variant rs28940293 [ dbSNP | Ensembl ].
VAR_018608
Natural varianti94 – 941R → Q in CMT2A2; in a Japanese and Russian kindred. 1 Publication
Corresponds to variant rs28940291 [ dbSNP | Ensembl ].
VAR_018609
Natural varianti94 – 941R → W in CMT6. 1 Publication
VAR_029876
Natural varianti206 – 2061T → I in CMT6. 1 Publication
VAR_029877
Natural varianti233 – 2331L → V in CMT2A2. 1 Publication
VAR_067088
Natural varianti251 – 2511P → A in CMT2A2. 1 Publication
Corresponds to variant rs28940295 [ dbSNP | Ensembl ].
VAR_018610
Natural varianti276 – 2761Q → R in CMT6. 1 Publication
VAR_029878
Natural varianti280 – 2801R → H in CMT2A2. 1 Publication
Corresponds to variant rs28940294 [ dbSNP | Ensembl ].
VAR_018611
Natural varianti357 – 3571K → N in CMT2A2. 1 Publication
VAR_022464
Natural varianti361 – 3611H → Y in CMT6. 1 Publication
VAR_029879
Natural varianti364 – 3641R → W in CMT6 and CMT2A2. 2 Publications
VAR_029880
Natural varianti740 – 7401W → S in CMT2A2; in a European family. 1 Publication
Corresponds to variant rs28940292 [ dbSNP | Ensembl ].
VAR_018612
Natural varianti744 – 7441E → M in CMT2A2; requires 2 nucleotide substitutions. 1 Publication
VAR_067089

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 302302Missing in isoform 2. CuratedVSP_015159Add
BLAST
Alternative sequencei303 – 32422FVSAK…MPEGG → MHPHLSTLSLPRRRSMAFLS SW in isoform 2. CuratedVSP_015160Add
BLAST
Alternative sequencei705 – 75753VTREN…LQPSR → GETLSERSMAKSTLMLLTLL FLCSFAGAQDVLTQ in isoform 2. CuratedVSP_015161Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028429 mRNA. Translation: AAK18728.1.
AF036536 mRNA. Translation: AAD02058.2.
D86987 mRNA. Translation: BAA34389.2. Different initiation.
AK289828 mRNA. Translation: BAF82517.1.
AL096840 Genomic DNA. Translation: CAI19087.2.
AL096840 Genomic DNA. Translation: CAI19088.2.
CH471130 Genomic DNA. Translation: EAW71726.1.
BC017061 mRNA. Translation: AAH17061.1.
AL137666 mRNA. Translation: CAB70866.2. Frameshift.
CCDSiCCDS30587.1. [O95140-1]
PIRiT46498.
RefSeqiNP_001121132.1. NM_001127660.1. [O95140-1]
NP_055689.1. NM_014874.3. [O95140-1]
XP_005263600.1. XM_005263543.1. [O95140-1]
XP_005263602.1. XM_005263545.1. [O95140-1]
XP_005263604.1. XM_005263547.1. [O95140-1]
XP_005263605.1. XM_005263548.1. [O95140-1]
UniGeneiHs.376681.

Genome annotation databases

EnsembliENST00000235329; ENSP00000235329; ENSG00000116688. [O95140-1]
ENST00000444836; ENSP00000416338; ENSG00000116688. [O95140-1]
GeneIDi9927.
KEGGihsa:9927.
UCSCiuc001atn.4. human. [O95140-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028429 mRNA. Translation: AAK18728.1 .
AF036536 mRNA. Translation: AAD02058.2 .
D86987 mRNA. Translation: BAA34389.2 . Different initiation.
AK289828 mRNA. Translation: BAF82517.1 .
AL096840 Genomic DNA. Translation: CAI19087.2 .
AL096840 Genomic DNA. Translation: CAI19088.2 .
CH471130 Genomic DNA. Translation: EAW71726.1 .
BC017061 mRNA. Translation: AAH17061.1 .
AL137666 mRNA. Translation: CAB70866.2 . Frameshift.
CCDSi CCDS30587.1. [O95140-1 ]
PIRi T46498.
RefSeqi NP_001121132.1. NM_001127660.1. [O95140-1 ]
NP_055689.1. NM_014874.3. [O95140-1 ]
XP_005263600.1. XM_005263543.1. [O95140-1 ]
XP_005263602.1. XM_005263545.1. [O95140-1 ]
XP_005263604.1. XM_005263547.1. [O95140-1 ]
XP_005263605.1. XM_005263548.1. [O95140-1 ]
UniGenei Hs.376681.

3D structure databases

ProteinModelPortali O95140.
SMRi O95140. Positions 695-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115255. 10 interactions.
DIPi DIP-42832N.
IntActi O95140. 6 interactions.
MINTi MINT-3002608.
STRINGi 9606.ENSP00000235329.

Protein family/group databases

TCDBi 9.B.25.2.1. the mitochondrial inner/outer membrane fusion (mmf) family.

PTM databases

PhosphoSitei O95140.

Proteomic databases

MaxQBi O95140.
PaxDbi O95140.
PRIDEi O95140.

Protocols and materials databases

DNASUi 9927.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000235329 ; ENSP00000235329 ; ENSG00000116688 . [O95140-1 ]
ENST00000444836 ; ENSP00000416338 ; ENSG00000116688 . [O95140-1 ]
GeneIDi 9927.
KEGGi hsa:9927.
UCSCi uc001atn.4. human. [O95140-1 ]

Organism-specific databases

CTDi 9927.
GeneCardsi GC01P012040.
GeneReviewsi MFN2.
HGNCi HGNC:16877. MFN2.
HPAi HPA030554.
MIMi 601152. phenotype.
608507. gene.
609260. phenotype.
neXtProti NX_O95140.
Orphaneti 99947. Autosomal dominant Charcot-Marie-Tooth disease type 2A2.
1215. Autosomal dominant optic atrophy plus syndrome.
64751. Hereditary motor and sensory neuropathy type 5.
90120. Hereditary motor and sensory neuropathy type 6.
90118. Severe early-onset axonal neuropathy due to MFN2 deficiency.
PharmGKBi PA134986046.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0699.
GeneTreei ENSGT00390000013727.
HOGENOMi HOG000231098.
HOVERGENi HBG052465.
InParanoidi O95140.
KOi K06030.
OMAi STLMVTE.
OrthoDBi EOG7HB58M.
PhylomeDBi O95140.
TreeFami TF314289.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi MFN2. human.
GeneWikii MFN2.
GenomeRNAii 9927.
NextBioi 37454.
PROi O95140.
SOURCEi Search...

Gene expression databases

Bgeei O95140.
CleanExi HS_MFN2.
ExpressionAtlasi O95140. baseline and differential.
Genevestigatori O95140.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR001401. Dynamin_GTPase.
IPR006884. Fzo/mitofusin_HR2.
IPR027089. Mitofusin-2.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10465. PTHR10465. 1 hit.
PTHR10465:SF1. PTHR10465:SF1. 1 hit.
Pfami PF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity."
    Bach D., Pich S., Soriano F.X., Vega N., Baumgartner B., Oriola J., Daugaard J.R., Lloberas J., Camps M., Zierath J.R., Rabasa-Lhoret R., Wallberg-Henriksson H., Laville M., Palacin M., Vidal H., Rivera F., Brand M., Zorzano A.
    J. Biol. Chem. 278:17190-17197(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Dysregulation of HSG triggers vascular proliferative disorders."
    Chen K.-H., Guo X., Ma D., Guo Y., Li Q., Yang D., Li P., Qiu X., Wen S., Xiao R.-P., Tang J.
    Nat. Cell Biol. 6:872-883(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISEASE.
  3. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-757 (ISOFORM 1).
    Tissue: Testis.
  9. "Control of mitochondrial morphology by a human mitofusin."
    Santel A., Fuller M.T.
    J. Cell Sci. 114:867-874(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-109; 622-GLY--VAL-624 AND 657-LYS--ARG-659.
  10. "Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo."
    Rojo M., Legros F., Chateau D., Lombes A.
    J. Cell Sci. 115:1663-1674(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-109; SER-110 AND ARG-259.
  11. "Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis."
    Karbowski M., Lee Y.-J., Gaume B., Jeong S.-Y., Frank S., Nechushtan A., Santel A., Fuller M., Smith C.L., Youle R.J.
    J. Cell Biol. 159:931-938(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells."
    Santel A., Frank S., Gaume B., Herrler M., Youle R.J., Fuller M.T.
    J. Cell Sci. 116:2763-2774(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. Cited for: DISEASE, VARIANTS CMT2A2 PHE-69; PRO-76; GLN-94; ALA-251; HIS-280 AND SER-740.
  14. "Identification of a novel mitochondrial complex containing mitofusin 2 and stomatin-like protein 2."
    Hajek P., Chomyn A., Attardi G.
    J. Biol. Chem. 282:5670-5681(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STOML2.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
    Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
    J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."
    Chen Y., Dorn G.W. II
    Science 340:471-475(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MITOPHAGY, INTERACTION WITH PARK2, PHOSPHORYLATION AT THR-111 AND SER-442 BY PINK1, UBIQUITINATION BY PARK2, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-111 AND SER-442.
  18. "Mitochondrial GTPase mitofusin 2 mutation in Charcot-Marie-Tooth neuropathy type 2A."
    Kijima K., Numakura C., Izumino H., Umetsu K., Nezu A., Shiiki T., Ogawa M., Ishizaki Y., Kitamura T., Shozawa Y., Hayasaka K.
    Hum. Genet. 116:23-27(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2A2 ASN-357.
  19. Cited for: VARIANTS CMT6 TRP-94; ILE-206; ARG-276; TYR-361 AND TRP-364.
  20. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
    Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
    PLoS ONE 6:E29393-E29393(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMT2A2 VAL-233; TRP-364 AND MET-744.

Entry informationi

Entry nameiMFN2_HUMAN
AccessioniPrimary (citable) accession number: O95140
Secondary accession number(s): A8K1B3
, O95572, Q5JXC3, Q5JXC4, Q9H131, Q9NSX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: October 29, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3