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Protein

Mitofusin-2

Gene

Mfn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.4 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Keywords - Biological processi

Apoptosis, Autophagy, Unfolded protein response

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin-2 (EC:3.6.5.-)
Alternative name(s):
Hypertension-related protein 1
Mitochondrial assembly regulatory factor
Short name:
HSG protein
Transmembrane GTPase MFN2
Gene namesi
Name:Mfn2
Synonyms:Kiaa0214, Marf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2442230. Mfn2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 604604CytoplasmicSequence analysisAdd
BLAST
Transmembranei605 – 62521Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini626 – 6261Mitochondrial intermembraneSequence analysis
Transmembranei627 – 64721Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini648 – 757110CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intrinsic component of mitochondrial outer membrane Source: UniProtKB
  • microtubule cytoskeleton Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

Dilated heart with increasing age, insensitive to beta-adrenergic stimulation and with impaired contractile performance. In cardiomyocytes, mitochondrial enlargement with respiratory impairment.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 757757Mitofusin-2PRO_0000127676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphothreonine; by PINK1By similarity
Modified residuei442 – 4421PhosphoserineCombined sources
Modified residuei442 – 4421Phosphoserine; by PINK1By similarity

Post-translational modificationi

Phosphorylated by PINK1.1 Publication
Ubiquitinated by non-degradative ubiquitin by PARK2, promoting mitochondrial fusion; deubiquitination by USP30 inhibits mitochondrial fusion.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80U63.
MaxQBiQ80U63.
PaxDbiQ80U63.
PRIDEiQ80U63.

PTM databases

iPTMnetiQ80U63.
PhosphoSiteiQ80U63.

Expressioni

Tissue specificityi

Ubiquitous. Expression is markedly reduced in ApoE-knockout mouse atherosclerotic arteries.2 Publications

Gene expression databases

BgeeiQ80U63.
CleanExiMM_MFN2.
ExpressionAtlasiQ80U63. baseline and differential.
GenevisibleiQ80U63. MM.

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 PARK2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif2ak3Q9Z2B52EBI-8437663,EBI-1226344

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228398. 4 interactions.
DIPiDIP-60970N.
IntActiQ80U63. 3 interactions.
MINTiMINT-8057620.
STRINGi10090.ENSMUSP00000030884.

Structurei

3D structure databases

ProteinModelPortaliQ80U63.
SMRiQ80U63. Positions 98-125, 695-754.
ModBaseiSearch...
MobiDBiSearch...

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 coili406 – 43429Sequence analysisAdd
BLAST
Coiled coili696 – 73843Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0448. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00390000013727.
HOVERGENiHBG052465.
InParanoidiQ80U63.
KOiK06030.
OMAiMNVESAQ.
OrthoDBiEOG7HB58M.
PhylomeDBiQ80U63.
TreeFamiTF314289.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR006884. Fzo/mitofusin_HR2.
IPR030381. G_DYNAMIN_dom.
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. AlignAdd to basket

Isoform 1 (identifier: Q80U63-1) [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 IVTVKKDKRH MAEVNASPLK HFVTAKKKIN GIFEQLGAYI
60 70 80 90 100
QESASFLEDT HRNTELDPVT TEEQVLDVKG YLSKVRGISE VLARRHMKVA
110 120 130 140 150
FFGRTSNGKS TVINAMLWDK VLPSGIGHTT NCFLRVGGTD GHEAFLLTEG
160 170 180 190 200
SEEKKSVKTV NQLAHALHQD EQLHAGSMVS VMWPNSKCPL LKDDLVLMDS
210 220 230 240 250
PGIDVTTELD SWIDKFCLDA DVFVLVANSE STLMQTEKQF FHKVSERLSR
260 270 280 290 300
PNIFILNNRW DASASEPEYM EEVRRQHMER CTSFLVDELG VVDRAQAGDR
310 320 330 340 350
IFFVSAKEVL SARVQKAQGM PEGGGALAEG FQVRMFEFQN FERQFEECIS
360 370 380 390 400
QSAVKTKFEQ HTVRAKQIAE AVRLIMDSLH IAAQEQRVYC LEMREERQDR
410 420 430 440 450
LRFIDKQLEL LAQDYKLRIK QITEEVERQV STAMAEEIRR LSVLVDEYQM
460 470 480 490 500
DFHPSPVVLK VYKNELHRHI EEGLGRNLSD RCSTAIASSL QTMQQDMIDG
510 520 530 540 550
LKPLLPVSMR NQIDMLVPRQ CFSLSYDLNC DKLCADFQED IEFHFSLGWT
560 570 580 590 600
MLVNRFLGPK NSRRALLGYS DQVQRPLPLT PANPSMPPLP QSSLTQEELM
610 620 630 640 650
VSMVTGLASL TSRTSMGILV VGGVVWKAVG WRLIALSFGL YGLLYVYERL
660 670 680 690 700
TWTTKAKERA FKRQFVEYAS EKLQLIISYT GSNCSHQVQQ ELSGTFAHLC
710 720 730 740 750
QQVDITRDNL EQEIAAMNKK VEALDSLQSR AKLLRNKAGW LDSELNMFTH

QYLQPSR
Length:757
Mass (Da):86,188
Last modified:May 24, 2004 - v3
Checksum:i25B0EAE8301F4D1A
GO
Isoform 2 (identifier: Q80U63-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     573-605: VQRPLPLTPANPSMPPLPQSSLTQEELMVSMVT → ARSSFPWCIMGDHPDTRYGSQSTTAGVLRAEAI
     606-757: Missing.

Note: No experimental confirmation available.
Show »
Length:605
Mass (Da):68,938
Checksum:iEDCB31AC12D60912
GO

Sequence cautioni

The sequence BAC65502.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231P → L in AAH46503 (PubMed:15489334).Curated
Sequence conflicti167 – 1671L → I in BAC33826 (PubMed:16141072).Curated
Sequence conflicti332 – 3321Q → K in AAK27416 (PubMed:12598526).Curated
Sequence conflicti344 – 3441Q → R in BAB39351 (Ref. 3) Curated
Sequence conflicti344 – 3441Q → R in AAK66559 (PubMed:15322553).Curated
Sequence conflicti437 – 4371E → G in BAB39351 (Ref. 3) Curated
Sequence conflicti570 – 5701S → N in AAK27416 (PubMed:12598526).Curated
Sequence conflicti592 – 5921S → G in AAK27416 (PubMed:12598526).Curated
Sequence conflicti601 – 6011V → G in AAK27416 (PubMed:12598526).Curated
Sequence conflicti633 – 6353LIA → IIP in AAK27416 (PubMed:12598526).Curated
Sequence conflicti656 – 6561A → T in AAK27416 (PubMed:12598526).Curated
Sequence conflicti659 – 6591R → K in AAK27416 (PubMed:12598526).Curated
Sequence conflicti666 – 6661V → A in AAK66559 (PubMed:15322553).Curated
Sequence conflicti667 – 6671E → D in BAB39351 (Ref. 3) Curated
Sequence conflicti676 – 6761I → T in BAB39351 (Ref. 3) Curated
Sequence conflicti697 – 6971A → G in AAK27416 (PubMed:12598526).Curated
Sequence conflicti730 – 7301R → K in AAK27416 (PubMed:12598526).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei573 – 60533VQRPL…VSMVT → ARSSFPWCIMGDHPDTRYGS QSTTAGVLRAEAI in isoform 2. 1 PublicationVSP_010365Add
BLAST
Alternative sequencei606 – 757152Missing in isoform 2. 1 PublicationVSP_010366Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY123975 mRNA. Translation: AAM88577.1.
AY028170 mRNA. Translation: AAK27416.1.
AB048831 mRNA. Translation: BAB39351.1.
AF384100 mRNA. Translation: AAK66559.1.
AK042080 mRNA. Translation: BAE20620.1.
AK049583 mRNA. Translation: BAC33826.1.
AK052689 mRNA. Translation: BAC35096.1.
AK122220 Transcribed RNA. Translation: BAC65502.2. Different initiation.
AL607066 Genomic DNA. Translation: CAM23513.1.
AL607066 Genomic DNA. Translation: CAP19097.1.
BC046503 mRNA. Translation: AAH46503.1.
CCDSiCCDS38965.1. [Q80U63-1]
RefSeqiNP_001272849.1. NM_001285920.1. [Q80U63-1]
NP_001272850.1. NM_001285921.1. [Q80U63-1]
NP_001272851.1. NM_001285922.1. [Q80U63-1]
NP_001272852.1. NM_001285923.1. [Q80U63-1]
NP_573464.2. NM_133201.3. [Q80U63-1]
XP_006538672.1. XM_006538609.2. [Q80U63-1]
XP_006538673.1. XM_006538610.1. [Q80U63-1]
XP_006538674.1. XM_006538611.2. [Q80U63-1]
UniGeneiMm.154312.
Mm.437499.

Genome annotation databases

EnsembliENSMUST00000030884; ENSMUSP00000030884; ENSMUSG00000029020. [Q80U63-1]
ENSMUST00000105714; ENSMUSP00000101339; ENSMUSG00000029020. [Q80U63-2]
ENSMUST00000105715; ENSMUSP00000101340; ENSMUSG00000029020. [Q80U63-1]
ENSMUST00000105716; ENSMUSP00000101341; ENSMUSG00000029020. [Q80U63-1]
GeneIDi170731.
KEGGimmu:170731.
UCSCiuc008vtg.2. mouse. [Q80U63-1]
uc008vtj.2. mouse. [Q80U63-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY123975 mRNA. Translation: AAM88577.1.
AY028170 mRNA. Translation: AAK27416.1.
AB048831 mRNA. Translation: BAB39351.1.
AF384100 mRNA. Translation: AAK66559.1.
AK042080 mRNA. Translation: BAE20620.1.
AK049583 mRNA. Translation: BAC33826.1.
AK052689 mRNA. Translation: BAC35096.1.
AK122220 Transcribed RNA. Translation: BAC65502.2. Different initiation.
AL607066 Genomic DNA. Translation: CAM23513.1.
AL607066 Genomic DNA. Translation: CAP19097.1.
BC046503 mRNA. Translation: AAH46503.1.
CCDSiCCDS38965.1. [Q80U63-1]
RefSeqiNP_001272849.1. NM_001285920.1. [Q80U63-1]
NP_001272850.1. NM_001285921.1. [Q80U63-1]
NP_001272851.1. NM_001285922.1. [Q80U63-1]
NP_001272852.1. NM_001285923.1. [Q80U63-1]
NP_573464.2. NM_133201.3. [Q80U63-1]
XP_006538672.1. XM_006538609.2. [Q80U63-1]
XP_006538673.1. XM_006538610.1. [Q80U63-1]
XP_006538674.1. XM_006538611.2. [Q80U63-1]
UniGeneiMm.154312.
Mm.437499.

3D structure databases

ProteinModelPortaliQ80U63.
SMRiQ80U63. Positions 98-125, 695-754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228398. 4 interactions.
DIPiDIP-60970N.
IntActiQ80U63. 3 interactions.
MINTiMINT-8057620.
STRINGi10090.ENSMUSP00000030884.

PTM databases

iPTMnetiQ80U63.
PhosphoSiteiQ80U63.

Proteomic databases

EPDiQ80U63.
MaxQBiQ80U63.
PaxDbiQ80U63.
PRIDEiQ80U63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030884; ENSMUSP00000030884; ENSMUSG00000029020. [Q80U63-1]
ENSMUST00000105714; ENSMUSP00000101339; ENSMUSG00000029020. [Q80U63-2]
ENSMUST00000105715; ENSMUSP00000101340; ENSMUSG00000029020. [Q80U63-1]
ENSMUST00000105716; ENSMUSP00000101341; ENSMUSG00000029020. [Q80U63-1]
GeneIDi170731.
KEGGimmu:170731.
UCSCiuc008vtg.2. mouse. [Q80U63-1]
uc008vtj.2. mouse. [Q80U63-2]

Organism-specific databases

CTDi9927.
MGIiMGI:2442230. Mfn2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0448. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00390000013727.
HOVERGENiHBG052465.
InParanoidiQ80U63.
KOiK06030.
OMAiMNVESAQ.
OrthoDBiEOG7HB58M.
PhylomeDBiQ80U63.
TreeFamiTF314289.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ80U63.
SOURCEiSearch...

Gene expression databases

BgeeiQ80U63.
CleanExiMM_MFN2.
ExpressionAtlasiQ80U63. baseline and differential.
GenevisibleiQ80U63. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022812. Dynamin_SF.
IPR006884. Fzo/mitofusin_HR2.
IPR030381. G_DYNAMIN_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development."
    Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., Chan D.C.
    J. Cell Biol. 160:189-200(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MULTIMERIZATION.
    Strain: FVB/NJ.
  2. "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).
  3. "Characterization of mouse fzo."
    Honda S., Hirose S.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Thymus.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  9. "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).
    Strain: FVB/N.
    Tissue: Salivary gland.
  10. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 421-428, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  11. "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: TISSUE SPECIFICITY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  13. Cited for: FUNCTION IN UPR, INTERACTION WITH EIF2AK3.
  14. "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, UBIQUITINATION BY PARK2, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  15. "A small natural molecule promotes mitochondrial fusion through inhibition of the deubiquitinase USP30."
    Yue W., Chen Z., Liu H., Yan C., Chen M., Feng D., Yan C., Wu H., Du L., Wang Y., Liu J., Huang X., Xia L., Liu L., Wang X., Jin H., Wang J., Song Z., Hao X., Chen Q.
    Cell Res. 24:482-496(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION.

Entry informationi

Entry nameiMFN2_MOUSE
AccessioniPrimary (citable) accession number: Q80U63
Secondary accession number(s): A2A7Y7
, A8Y5E4, Q3V3B8, Q80WP4, Q80XK3, Q8BHF0, Q8BKV5, Q8R535, Q923X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 8, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

MFN2 deficient mice die early during embryonic development, due to altered mitochondria morphology, which are fragmented, showing that mitochondrial fusion is essential for embryonic development.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.