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Protein

Mitofusin-2

Gene

MFN2

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

Functioni

Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, 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).By similarityCurated4 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei305GTPBy similarity1
Binding sitei307GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi106 – 111GTPBy similarity6
Nucleotide bindingi258 – 261GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • blastocyst formation Source: Ensembl
  • blood coagulation Source: Reactome
  • camera-type eye morphogenesis Source: Ensembl
  • macroautophagy Source: Reactome
  • mitochondrial fusion Source: UniProtKB
  • mitochondrial membrane organization Source: UniProtKB
  • mitochondrion localization Source: UniProtKB
  • negative regulation of Ras protein signal transduction Source: UniProtKB
  • negative regulation of smooth muscle cell proliferation Source: UniProtKB
  • parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • protein localization to pre-autophagosomal structure Source: MGI
  • protein targeting to mitochondrion Source: UniProtKB
  • response to unfolded protein Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase
Biological processApoptosis, Autophagy, Unfolded protein response
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5205685. Pink/Parkin Mediated Mitophagy.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiO95140.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16877. MFN2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 604CytoplasmicSequence analysisAdd BLAST604
Transmembranei605 – 625Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini626Mitochondrial intermembraneSequence analysis1
Transmembranei627 – 647Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini648 – 757CytoplasmicSequence analysisAdd BLAST110

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 2A2B (CMT2A2B)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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. CMT2A2B is a severe form with autosomal recessive inheritance.
See also OMIM:617087
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07689538Missing in CMT2A2B. 1 Publication1
Natural variantiVAR_01860994R → Q in CMT2A2A and CMT2A2B. 2 PublicationsCorresponds to variant dbSNP:rs28940291Ensembl.1
Natural variantiVAR_076896216F → S in CMT2A2B. 1 PublicationCorresponds to variant dbSNP:rs387906990Ensembl.1
Natural variantiVAR_076897362T → M in CMT2A2B. 1 PublicationCorresponds to variant dbSNP:rs387906991Ensembl.1
Charcot-Marie-Tooth disease 2A2A (CMT2A2A)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:609260
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01860769V → F in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940296Ensembl.1
Natural variantiVAR_01860876L → P in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940293Ensembl.1
Natural variantiVAR_01860994R → Q in CMT2A2A and CMT2A2B. 2 PublicationsCorresponds to variant dbSNP:rs28940291Ensembl.1
Natural variantiVAR_078437127G → V in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_067088233L → V in CMT2A2A. 1 Publication1
Natural variantiVAR_018610251P → A in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940295Ensembl.1
Natural variantiVAR_018611280R → H in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940294Ensembl.1
Natural variantiVAR_078438347E → V in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_022464357K → N in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs119103261Ensembl.1
Natural variantiVAR_029880364R → W in HMSN6A and CMT2A2A. 2 PublicationsCorresponds to variant dbSNP:rs119103265Ensembl.1
Natural variantiVAR_078439376M → I in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_078440468R → H in CMT2A2A; also found in patients with an unclassified form of Charcot-Marie-Tooth disease; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs138382758Ensembl.1
Natural variantiVAR_078443707R → W in CMT2A2A; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs119103267Ensembl.1
Natural variantiVAR_018612740W → S in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940292Ensembl.1
Natural variantiVAR_067089744E → M in CMT2A2A; requires 2 nucleotide substitutions. 1 Publication1
Neuropathy, hereditary motor and sensory, 6A (HMSN6A)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:601152
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02987694R → W in HMSN6A. 2 PublicationsCorresponds to variant dbSNP:rs119103263Ensembl.1
Natural variantiVAR_029877206T → I in HMSN6A. 1 PublicationCorresponds to variant dbSNP:rs119103266Ensembl.1
Natural variantiVAR_029878276Q → R in HMSN6A. 1 PublicationCorresponds to variant dbSNP:rs119103264Ensembl.1
Natural variantiVAR_029879361H → Y in HMSN6A. 1 Publication1
Natural variantiVAR_029880364R → W in HMSN6A and CMT2A2A. 2 PublicationsCorresponds to variant dbSNP:rs119103265Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi109K → A or T: Does not affect its ability to cluster mitochondria; when overexpressed. 2 Publications1
Mutagenesisi110S → N: Does not affect its ability to cluster mitochondria; when overexpressed. 1 Publication1
Mutagenesisi111T → 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. 1 Publication1
Mutagenesisi111T → E: Interacts with PRKN in absence of PINK1; when associated with GLU-442. 1 Publication1
Mutagenesisi128H → A: Loss of function in promoting mitochondrial fusion. 1 Publication1
Mutagenesisi230E → A: Loss of function in promoting mitochondrial fusion. 1 Publication1
Mutagenesisi259R → A: Loss of function in promoting mitochondrial fusion. 1 Publication1
Mutagenesisi259R → L: Does not affect its ability to cluster mitochondria; when overexpressed. 1 Publication1
Mutagenesisi260W → A: Loss of function in promoting mitochondrial fusion. 1 Publication1
Mutagenesisi266E → A: Loss of function in promoting mitochondrial fusion. 1 Publication1
Mutagenesisi442S → 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. 1 Publication1
Mutagenesisi442S → E: Interacts with PRKN in absence of PINK1; when associated with GLU-111. 1 Publication1
Mutagenesisi622 – 624GGV → AAL: Does not affect the targeting to mitochondrial outer membrane. 1 Publication3
Mutagenesisi622 – 624GGV → RRE: Abolishes the targeting to mitochondrial outer membrane. 1 Publication3
Mutagenesisi657 – 659KER → TGV: Does not affect the targeting to mitochondrial outer membrane. 1 Publication3

Keywords - Diseasei

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

Organism-specific databases

DisGeNETi9927.
GeneReviewsiMFN2.
MalaCardsiMFN2.
MIMi601152. phenotype.
609260. phenotype.
617087. phenotype.
OpenTargetsiENSG00000116688.
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.

Polymorphism and mutation databases

BioMutaiMFN2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276751 – 757Mitofusin-2Add BLAST757

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei111Phosphothreonine; by PINK11 Publication1
Modified residuei442Phosphoserine; by PINK11 Publication1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO95140.
MaxQBiO95140.
PaxDbiO95140.
PeptideAtlasiO95140.
PRIDEiO95140.

PTM databases

iPTMnetiO95140.
PhosphoSitePlusiO95140.
SwissPalmiO95140.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000116688.
CleanExiHS_MFN2.
ExpressionAtlasiO95140. baseline and differential.
GenevisibleiO95140. HS.

Organism-specific databases

HPAiHPA030554.

Interactioni

Subunit structurei

Forms homomultimers and heteromultimers with MFN1 (By similarity). Oligomerization is essential for mitochondrion fusion (Probable). Interacts with VAT1 (By similarity). Interacts with STOML2; may form heterooligomers (PubMed:17121834). Interacts (phosphorylated) with PRKN (PubMed:23620051). Interacts with EIF2AK3 (By similarity).By similarityCurated2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115255. 18 interactors.
DIPiDIP-42832N.
IntActiO95140. 8 interactors.
MINTiMINT-3002608.
STRINGi9606.ENSP00000235329.

Structurei

3D structure databases

ProteinModelPortaliO95140.
SMRiO95140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 342Dynamin-type GAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 94Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST65
Regioni359 – 385Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST27
Regioni722 – 753Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regionsBy similarityAdd BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili391 – 434Sequence analysisAdd BLAST44
Coiled coili695 – 738Sequence analysisAdd BLAST44

Domaini

A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion.By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0448. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00390000013727.
HOGENOMiHOG000231098.
HOVERGENiHBG052465.
InParanoidiO95140.
KOiK06030.
OMAiEQRVYCL.
OrthoDBiEOG091G02ES.
PhylomeDBiO95140.
TreeFamiTF314289.

Family and domain databases

InterProiView protein in InterPro
IPR022812. Dynamin_SF.
IPR006884. Fzo/mitofusin_HR2.
IPR030381. G_DYNAMIN_dom.
IPR027089. Mitofusin-2.
IPR027417. P-loop_NTPase.
PANTHERiPTHR10465:SF9. PTHR10465:SF9. 1 hit.
PfamiView protein in Pfam
PF00350. Dynamin_N. 1 hit.
PF04799. Fzo_mitofusin. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiView protein in PROSITE
PS51718. G_DYNAMIN_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95140-1) [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 BAA34389 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB70866 differs from that shown. Reason: Frameshift at position 581.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti521C → P in AAD02058 (PubMed:15322553).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07689538Missing in CMT2A2B. 1 Publication1
Natural variantiVAR_01860769V → F in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940296Ensembl.1
Natural variantiVAR_01860876L → P in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940293Ensembl.1
Natural variantiVAR_01860994R → Q in CMT2A2A and CMT2A2B. 2 PublicationsCorresponds to variant dbSNP:rs28940291Ensembl.1
Natural variantiVAR_02987694R → W in HMSN6A. 2 PublicationsCorresponds to variant dbSNP:rs119103263Ensembl.1
Natural variantiVAR_078437127G → V in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_029877206T → I in HMSN6A. 1 PublicationCorresponds to variant dbSNP:rs119103266Ensembl.1
Natural variantiVAR_076896216F → S in CMT2A2B. 1 PublicationCorresponds to variant dbSNP:rs387906990Ensembl.1
Natural variantiVAR_067088233L → V in CMT2A2A. 1 Publication1
Natural variantiVAR_018610251P → A in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940295Ensembl.1
Natural variantiVAR_073291259R → H Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs755065651Ensembl.1
Natural variantiVAR_029878276Q → R in HMSN6A. 1 PublicationCorresponds to variant dbSNP:rs119103264Ensembl.1
Natural variantiVAR_018611280R → H in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940294Ensembl.1
Natural variantiVAR_078438347E → V in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_022464357K → N in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs119103261Ensembl.1
Natural variantiVAR_029879361H → Y in HMSN6A. 1 Publication1
Natural variantiVAR_076897362T → M in CMT2A2B. 1 PublicationCorresponds to variant dbSNP:rs387906991Ensembl.1
Natural variantiVAR_029880364R → W in HMSN6A and CMT2A2A. 2 PublicationsCorresponds to variant dbSNP:rs119103265Ensembl.1
Natural variantiVAR_078439376M → I in CMT2A2A; unknown pathological significance. 1 Publication1
Natural variantiVAR_078440468R → H in CMT2A2A; also found in patients with an unclassified form of Charcot-Marie-Tooth disease; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs138382758Ensembl.1
Natural variantiVAR_078441570N → S Found in a patient with hereditary motor neuropathy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs376925978Ensembl.1
Natural variantiVAR_078442705V → I3 PublicationsCorresponds to variant dbSNP:rs142271930Ensembl.1
Natural variantiVAR_078443707R → W in CMT2A2A; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs119103267Ensembl.1
Natural variantiVAR_078444716A → T Found in a patient with intermediate Charcot-Marie-Tooth disease; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs144860227Ensembl.1
Natural variantiVAR_018612740W → S in CMT2A2A. 1 PublicationCorresponds to variant dbSNP:rs28940292Ensembl.1
Natural variantiVAR_067089744E → M in CMT2A2A; requires 2 nucleotide substitutions. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0151591 – 302Missing in isoform 2. CuratedAdd BLAST302
Alternative sequenceiVSP_015160303 – 324FVSAK…MPEGG → MHPHLSTLSLPRRRSMAFLS SW in isoform 2. CuratedAdd BLAST22
Alternative sequenceiVSP_015161705 – 757VTREN…LQPSR → GETLSERSMAKSTLMLLTLL FLCSFAGAQDVLTQ in isoform 2. CuratedAdd BLAST53

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005263543.3. [O95140-1]
XP_005263602.1. XM_005263545.3. [O95140-1]
XP_005263604.1. XM_005263547.3. [O95140-1]
XP_005263605.1. XM_005263548.3. [O95140-1]
UniGeneiHs.376681.

Genome annotation databases

EnsembliENST00000235329; ENSP00000235329; ENSG00000116688. [O95140-1]
ENST00000444836; ENSP00000416338; ENSG00000116688. [O95140-1]
GeneIDi9927.
KEGGihsa:9927.
UCSCiuc001atn.5. human. [O95140-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiMFN2_HUMAN
AccessioniPrimary (citable) accession number: O95140
Secondary accession number(s): A8K1B3
, O95572, Q5JXC3, Q5JXC4, Q9H131, Q9NSX8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: August 30, 2017
This is version 156 of the entry and version 3 of the sequence. See 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