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O95140 (MFN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitofusin-2

EC=3.6.5.-
Alternative name(s):
Transmembrane GTPase MFN2
Gene names
Name:MFN2
Synonyms:CPRP1, KIAA0214
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.9 Ref.10 Ref.17 Ref.18

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

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. Ref.15 Ref.18

Subcellular location

Mitochondrion outer membrane; Multi-pass membrane protein. Note: Colocalizes with BAX during apoptosis. Ref.9 Ref.10 Ref.11 Ref.18

Tissue specificity

Ubiquitous; expressed at low level. Highly expressed in heart and kidney. Ref.10 Ref.12

Post-translational modification

Phosphorylated by PINK1. Ref.18

Ubiquitinated by PARK2. Ref.18

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.13 Ref.19 Ref.21

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.13 Ref.20

Sequence similarities

Belongs to the mitofusin family.

Sequence caution

The sequence BAA34389.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB70866.2 differs from that shown. Reason: Frameshift at position 581.

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblastocyst formation

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial fusion

Inferred from mutant phenotype Ref.17. Source: UniProtKB

mitochondrial membrane organization

Inferred from direct assay Ref.9. Source: UniProtKB

mitochondrion localization

Inferred from direct assay Ref.9. Source: UniProtKB

negative regulation of Ras protein signal transduction

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to mitochondrion

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 16936636. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRK2Q5S0073EBI-3324756,EBI-5323863

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95140-1)

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.
Isoform 2 (identifier: O95140-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 757757Mitofusin-2
PRO_0000127675

Regions

Topological domain1 – 604604Cytoplasmic Potential
Transmembrane605 – 62521Helical; Name=1; Potential
Topological domain6261Mitochondrial intermembrane Potential
Transmembrane627 – 64721Helical; Name=2; Potential
Topological domain648 – 757110Cytoplasmic Potential
Nucleotide binding103 – 1108GTP Probable
Nucleotide binding199 – 2035GTP Probable
Nucleotide binding258 – 2614GTP Probable
Coiled coil391 – 43444 Potential
Coiled coil695 – 73844 Potential

Amino acid modifications

Modified residue1111Phosphothreonine; by PINK1 Probable
Modified residue4421Phosphoserine; by PINK1 Probable

Natural variations

Alternative sequence1 – 302302Missing in isoform 2.
VSP_015159
Alternative sequence303 – 32422FVSAK…MPEGG → MHPHLSTLSLPRRRSMAFLS SW in isoform 2.
VSP_015160
Alternative sequence705 – 75753VTREN…LQPSR → GETLSERSMAKSTLMLLTLL FLCSFAGAQDVLTQ in isoform 2.
VSP_015161
Natural variant691V → F in CMT2A2; in a Turkish family. Ref.13
Corresponds to variant rs28940296 [ dbSNP | Ensembl ].
VAR_018607
Natural variant761L → P in CMT2A2; in a European family. Ref.13
Corresponds to variant rs28940293 [ dbSNP | Ensembl ].
VAR_018608
Natural variant941R → Q in CMT2A2; in a Japanese and Russian kindred. Ref.13
Corresponds to variant rs28940291 [ dbSNP | Ensembl ].
VAR_018609
Natural variant941R → W in CMT6. Ref.20
VAR_029876
Natural variant2061T → I in CMT6. Ref.20
VAR_029877
Natural variant2331L → V in CMT2A2. Ref.21
VAR_067088
Natural variant2511P → A in CMT2A2. Ref.13
Corresponds to variant rs28940295 [ dbSNP | Ensembl ].
VAR_018610
Natural variant2761Q → R in CMT6. Ref.20
VAR_029878
Natural variant2801R → H in CMT2A2. Ref.13
Corresponds to variant rs28940294 [ dbSNP | Ensembl ].
VAR_018611
Natural variant3571K → N in CMT2A2. Ref.19
VAR_022464
Natural variant3611H → Y in CMT6. Ref.20
VAR_029879
Natural variant3641R → W in CMT6 and CMT2A2. Ref.20 Ref.21
VAR_029880
Natural variant7401W → S in CMT2A2; in a European family. Ref.13
Corresponds to variant rs28940292 [ dbSNP | Ensembl ].
VAR_018612
Natural variant7441E → M in CMT2A2; requires 2 nucleotide substitutions. Ref.21
VAR_067089

Experimental info

Mutagenesis1091K → A or T: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.9 Ref.10
Mutagenesis1101S → N: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.10
Mutagenesis1111T → 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. Ref.18
Mutagenesis1111T → E: Interacts with PARK2 in absence of PINK1; when associated with GLU-442. Ref.18
Mutagenesis2591R → L: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.10
Mutagenesis4421S → 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. Ref.18
Mutagenesis4421S → E: Interacts with PARK2 in absence of PINK1; when associated with GLU-111. Ref.18
Mutagenesis622 – 6243GGV → AAL: Does not affect the targeting to mitochondrial outer membrane. Ref.9
Mutagenesis622 – 6243GGV → RRE: Abolishes the targeting to mitochondrial outer membrane. Ref.9
Mutagenesis657 – 6593KER → TGV: Does not affect the targeting to mitochondrial outer membrane. Ref.9
Sequence conflict5211C → P in AAD02058. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 24, 2004. Version 3.
Checksum: 6F859D740152DFAD

FASTA75786,402
        10         20         30         40         50         60 
MSLLFSRCNS IVTVKKNKRH MAEVNASPLK HFVTAKKKIN GIFEQLGAYI QESATFLEDT 

        70         80         90        100        110        120 
YRNAELDPVT TEEQVLDVKG YLSKVRGISE VLARRHMKVA FFGRTSNGKS TVINAMLWDK 

       130        140        150        160        170        180 
VLPSGIGHTT NCFLRVEGTD GHEAFLLTEG SEEKRSAKTV NQLAHALHQD KQLHAGSLVS 

       190        200        210        220        230        240 
VMWPNSKCPL LKDDLVLMDS PGIDVTTELD SWIDKFCLDA DVFVLVANSE STLMQTEKHF 

       250        260        270        280        290        300 
FHKVSERLSR PNIFILNNRW DASASEPEYM EEVRRQHMER CTSFLVDELG VVDRSQAGDR 

       310        320        330        340        350        360 
IFFVSAKEVL NARIQKAQGM PEGGGALAEG FQVRMFEFQN FERRFEECIS QSAVKTKFEQ 

       370        380        390        400        410        420 
HTVRAKQIAE AVRLIMDSLH MAAREQQVYC EEMREERQDR LKFIDKQLEL LAQDYKLRIK 

       430        440        450        460        470        480 
QITEEVERQV STAMAEEIRR LSVLVDDYQM DFHPSPVVLK VYKNELHRHI EEGLGRNMSD 

       490        500        510        520        530        540 
RCSTAITNSL QTMQQDMIDG LKPLLPVSVR SQIDMLVPRQ CFSLNYDLNC DKLCADFQED 

       550        560        570        580        590        600 
IEFHFSLGWT MLVNRFLGPK NSRRALMGYN DQVQRPIPLT PANPSMPPLP QGSLTQEEFM 

       610        620        630        640        650        660 
VSMVTGLASL TSRTSMGILV VGGVVWKAVG WRLIALSFGL YGLLYVYERL TWTTKAKERA 

       670        680        690        700        710        720 
FKRQFVEHAS EKLQLVISYT GSNCSHQVQQ ELSGTFAHLC QQVDVTRENL EQEIAAMNKK 

       730        740        750 
IEVLDSLQSK AKLLRNKAGW LDSELNMFTH QYLQPSR 

« Hide

Isoform 2 [UniParc].

Checksum: B3DA00C339C353C8
Show »

FASTA43650,041

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A."
Zuechner S., Mersiyanova I.V., Muglia M., Bissar-Tadmouri N., Rochelle J., Dadali E.L., Zappia M., Nelis E., Patitucci A., Senderek J., Parman Y., Evgrafov O., Jonghe P.D., Takahashi Y., Tsuji S., Pericak-Vance M.A., Quattrone A., Battaloglu E. expand/collapse author list , Polyakov A.V., Timmerman V., Schroeder J.M., Vance J.M.
Nat. Genet. 36:449-451(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, VARIANTS CMT2A2 PHE-69; PRO-76; GLN-94; ALA-251; HIS-280 AND SER-740.
[14]Erratum
Zuechner S., Mersiyanova I.V., Muglia M., Bissar-Tadmouri N., Rochelle J., Dadali E.L., Zappia M., Nelis E., Patitucci A., Senderek J., Parman Y., Evgrafov O., Jonghe P.D., Takahashi Y., Tsuji S., Pericak-Vance M.A., Quattrone A., Battaloglu E. expand/collapse author list , Polyakov A.V., Timmerman V., Schroeder J.M., Vance J.M.
Nat. Genet. 36:660-660(2004)
[15]"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.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"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.
[19]"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.
[20]"Axonal neuropathy with optic atrophy is caused by mutations in mitofusin 2."
Zuechner S., De Jonghe P., Jordanova A., Claeys K.G., Guergueltcheva V., Cherninkova S., Hamilton S.R., Van Stavern G., Krajewski K.M., Stajich J., Tournev I., Verhoeven K., Langerhorst C.T., de Visser M., Baas F., Bird T., Timmerman V., Shy M., Vance J.M.
Ann. Neurol. 59:276-281(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMT6 TRP-94; ILE-206; ARG-276; TYR-361 AND TRP-364.
[21]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT46498.
RefSeqNP_001121132.1. NM_001127660.1.
NP_055689.1. NM_014874.3.
XP_005263600.1. XM_005263543.1.
XP_005263602.1. XM_005263545.1.
XP_005263604.1. XM_005263547.1.
XP_005263605.1. XM_005263548.1.
UniGeneHs.376681.

3D structure databases

ProteinModelPortalO95140.
SMRO95140. Positions 93-119, 695-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115255. 11 interactions.
DIPDIP-42832N.
IntActO95140. 5 interactions.
MINTMINT-3002608.
STRING9606.ENSP00000235329.

Protein family/group databases

TCDB9.B.25.2.1. the mitochondrial inner/outer membrane fusion (mmf) family.

PTM databases

PhosphoSiteO95140.

Proteomic databases

PaxDbO95140.
PRIDEO95140.

Protocols and materials databases

DNASU9927.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235329; ENSP00000235329; ENSG00000116688. [O95140-1]
ENST00000444836; ENSP00000416338; ENSG00000116688. [O95140-1]
GeneID9927.
KEGGhsa:9927.
UCSCuc001atn.4. human. [O95140-1]

Organism-specific databases

CTD9927.
GeneCardsGC01P012040.
HGNCHGNC:16877. MFN2.
HPAHPA030554.
MIM601152. phenotype.
608507. gene.
609260. phenotype.
neXtProtNX_O95140.
Orphanet99947. 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.
PharmGKBPA134986046.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000231098.
HOVERGENHBG052465.
InParanoidO95140.
KOK06030.
OMASTLMVTE.
OrthoDBEOG7HB58M.
PhylomeDBO95140.
TreeFamTF314289.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO95140.
BgeeO95140.
CleanExHS_MFN2.
GenevestigatorO95140.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR001401. Dynamin_GTPase.
IPR006884. Fzo/mitofusin_HR2.
IPR027089. Mitofusin-2.
IPR027094. Mitofusin_fam.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10465. PTHR10465. 1 hit.
PTHR10465:SF1. PTHR10465:SF1. 1 hit.
PfamPF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMFN2. human.
GeneWikiMFN2.
GenomeRNAi9927.
NextBio37454.
PROO95140.
SOURCESearch...

Entry information

Entry nameMFN2_HUMAN
AccessionPrimary (citable) accession number: O95140
Secondary accession number(s): A8K1B3 expand/collapse secondary AC list , O95572, Q5JXC3, Q5JXC4, Q9H131, Q9NSX8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM