O95140 (MFN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitofusin-2
EC=3.6.5.-

Alternative name(s):
Transmembrane GTPase MFN2

Gene names

Name:	MFN2
Synonyms:	CPRP1, KIAA0214

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.2 Ref.9 Ref.10
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 By similarity. Interacts with STOML2; may form heterooligomers. Ref.15
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein. Note: Colocalizes with BAX during apoptosis. Ref.9 Ref.10 Ref.11
Tissue specificity	Ubiquitous; expressed at low level. Highly expressed in heart and kidney. Ref.10 Ref.12
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 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.17 Ref.19 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.18
Sequence similarities	Belongs to the mitofusin family.
Sequence caution	The sequence BAA34389.2 differs from that shown. Reason: Erroneous initiation. The sequence CAB70866.2 differs from that shown. Reason: Frameshift at position 581.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blastocyst formation Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara mitochondrial fusion Non-traceable author statement Ref.9. 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_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB microtubule cytoskeleton Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 757	757	Mitofusin-2		PRO_0000127675
Regions
	Topological domain	1 – 604	604	Cytoplasmic Potential
	Transmembrane	605 – 625	21	Helical; Name=1; Potential
	Topological domain	626	1	Mitochondrial intermembrane Potential
	Transmembrane	627 – 647	21	Helical; Name=2; Potential
	Topological domain	648 – 757	110	Cytoplasmic Potential
	Nucleotide binding	103 – 110	8	GTP Probable
	Nucleotide binding	199 – 203	5	GTP Probable
	Nucleotide binding	258 – 261	4	GTP Probable
	Coiled coil	391 – 434	44	Potential
	Coiled coil	695 – 738	44	Potential
Natural variations
	Alternative sequence	1 – 302	302	Missing in isoform 2.		VSP_015159
	Alternative sequence	303 – 324	22	FVSAK…MPEGG → MHPHLSTLSLPRRRSMAFLS SW in isoform 2.		VSP_015160
	Alternative sequence	705 – 757	53	VTREN…LQPSR → GETLSERSMAKSTLMLLTLL FLCSFAGAQDVLTQ in isoform 2.		VSP_015161
	Natural variant	69	1	V → F in CMT2A2; in a Turkish family. Ref.13 Corresponds to variant rs28940296 [ dbSNP | Ensembl ].		VAR_018607
	Natural variant	76	1	L → P in CMT2A2; in a European family. Ref.13 Corresponds to variant rs28940293 [ dbSNP | Ensembl ].		VAR_018608
	Natural variant	94	1	R → Q in CMT2A2; in a Japanese and Russian kindred. Ref.13 Corresponds to variant rs28940291 [ dbSNP | Ensembl ].		VAR_018609
	Natural variant	94	1	R → W in CMT6. Ref.18		VAR_029876
	Natural variant	206	1	T → I in CMT6. Ref.18		VAR_029877
	Natural variant	233	1	L → V in CMT2A2. Ref.19		VAR_067088
	Natural variant	251	1	P → A in CMT2A2. Ref.13 Corresponds to variant rs28940295 [ dbSNP | Ensembl ].		VAR_018610
	Natural variant	276	1	Q → R in CMT6. Ref.18		VAR_029878
	Natural variant	280	1	R → H in CMT2A2. Ref.13 Corresponds to variant rs28940294 [ dbSNP | Ensembl ].		VAR_018611
	Natural variant	357	1	K → N in CMT2A2. Ref.17		VAR_022464
	Natural variant	361	1	H → Y in CMT6. Ref.18		VAR_029879
	Natural variant	364	1	R → W in CMT6 and CMT2A2. Ref.18 Ref.19		VAR_029880
	Natural variant	740	1	W → S in CMT2A2; in a European family. Ref.13 Corresponds to variant rs28940292 [ dbSNP | Ensembl ].		VAR_018612
	Natural variant	744	1	E → M in CMT2A2; requires 2 nucleotide substitutions. Ref.19		VAR_067089
Experimental info
	Mutagenesis	109	1	K → A or T: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.9 Ref.10
	Mutagenesis	110	1	S → N: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.10
	Mutagenesis	259	1	R → L: Does not affect its ability to cluster mitochondria; when overexpressed. Ref.10
	Mutagenesis	622 – 624	3	GGV → AAL: Does not affect the targeting to mitochondrial outer membrane. Ref.9
	Mutagenesis	622 – 624	3	GGV → RRE: Abolishes the targeting to mitochondrial outer membrane. Ref.9
	Mutagenesis	657 – 659	3	KER → TGV: Does not affect the targeting to mitochondrial outer membrane. Ref.9
	Sequence conflict	521	1	C → P in AAD02058. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 24, 2004. Version 3. Checksum: 6F859D740152DFAD	FASTA	757	86,402
	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
	Isoform 2 [UniParc]. Checksum: B3DA00C339C353C8	FASTA	436	50,041
	10 20 30 40 50 60 MHPHLSTLSL PRRRSMAFLS SWGALAEGFQ VRMFEFQNFE RRFEECISQS AVKTKFEQHT 70 80 90 100 110 120 VRAKQIAEAV RLIMDSLHMA AREQQVYCEE MREERQDRLK FIDKQLELLA QDYKLRIKQI 130 140 150 160 170 180 TEEVERQVST AMAEEIRRLS VLVDDYQMDF HPSPVVLKVY KNELHRHIEE GLGRNMSDRC 190 200 210 220 230 240 STAITNSLQT MQQDMIDGLK PLLPVSVRSQ IDMLVPRQCF SLNYDLNCDK LCADFQEDIE 250 260 270 280 290 300 FHFSLGWTML VNRFLGPKNS RRALMGYNDQ VQRPIPLTPA NPSMPPLPQG SLTQEEFMVS 310 320 330 340 350 360 MVTGLASLTS RTSMGILVVG GVVWKAVGWR LIALSFGLYG LLYVYERLTW TTKAKERAFK 370 380 390 400 410 420 RQFVEHASEK LQLVISYTGS NCSHQVQQEL SGTFAHLCQQ VDGETLSERS MAKSTLMLLT 430 LLFLCSFAGA QDVLTQ

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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. , 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]	"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.
[18]	"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.
[19]	"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.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

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.
IPI	IPI00642329. IPI00902732.
PIR	T46498.
RefSeq	NP_001121132.1. NM_001127660.1. NP_055689.1. NM_014874.3.
UniGene	Hs.376681.
3D structure databases
ProteinModelPortal	O95140.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42832N.
IntAct	O95140. 1 interaction.
MINT	MINT-3002608.
STRING	9606.ENSP00000235329.
Protein family/group databases
TCDB	9.B.25.2.1. mitochondrial inner/outer membrane fusion (MMF) family.
PTM databases
PhosphoSite	O95140.
Proteomic databases
PaxDb	O95140.
PRIDE	O95140.
Protocols and materials databases
DNASU	9927.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000235329; ENSP00000235329; ENSG00000116688. ENST00000444836; ENSP00000416338; ENSG00000116688.
GeneID	9927.
KEGG	hsa:9927.
UCSC	uc001atn.4. human.
Organism-specific databases
CTD	9927.
GeneCards	GC01P012040.
HGNC	HGNC:16877. MFN2.
HPA	HPA030554.
MIM	601152. phenotype. 608507. gene. 609260. phenotype.
neXtProt	NX_O95140.
Orphanet	99947. Autosomal dominant Charcot-Marie-Tooth disease type 2A2. 90118. Autosomal recessive Charcot-Marie-Tooth disease, Ouvrier type. 64751. Hereditary motor and sensory neuropathy type 5. 90120. Hereditary motor and sensory neuropathy type 6.
PharmGKB	PA134986046.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0699.
HOGENOM	HOG000231098.
HOVERGEN	HBG052465.
InParanoid	O95140.
KO	K06030.
OMA	RVQKAQG.
OrthoDB	EOG43JC43.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	O95140.
Bgee	O95140.
CleanEx	HS_MFN2.
Genevestigator	O95140.
GermOnline	ENSG00000116688. Homo sapiens.
Family and domain databases
InterPro	IPR001401. Dynamin_GTPase. IPR006884. Fzo/mitofusin_HR2. IPR027089. Mitofusin-2. IPR027094. Mitofusin_fam. [Graphical view]
PANTHER	PTHR10465. PTHR10465. 1 hit. PTHR10465:SF1. PTHR10465:SF1. 1 hit.
Pfam	PF00350. Dynamin_N. 1 hit. PF04799. Fzo_mitofusin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MFN2. human.
GenomeRNAi	9927.
NextBio	37454.
SOURCE	Search...

Entry information

Entry name

MFN2_HUMAN

Accession

Primary (citable) accession number: O95140
Secondary accession number(s): A8K1B3 , O95572, Q5JXC3, Q5JXC4, Q9H131, Q9NSX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.