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Protein

Mitofusin-1

Gene

MFN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12475957, PubMed:12759376, PubMed:27920125, PubMed:28114303). Membrane clustering requires GTPase activity (PubMed:27920125). It may involve a major rearrangement of the coiled coil domains (PubMed:27920125, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:12475957, PubMed:12759376). Overexpression induces the formation of mitochondrial networks (in vitro) (PubMed:12759376). Has low GTPase activity (PubMed:27920125, PubMed:28114303).4 Publications

Miscellaneous

A truncated MFN1 construct containing the GTPase domain and the associated helix bundle is a monomer in the absence of bound GTP and a homodimer in the GTP-bound form; GDP cannot replace GTP and induce dimerization.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei284GTPCombined sources2 Publications1
Binding sitei286GTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi85 – 90GTPCombined sources2 Publications6
Nucleotide bindingi237 – 240GTPCombined sources2 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • GTP metabolic process Source: UniProtKB
  • macroautophagy Source: Reactome
  • mitochondrial fusion Source: BHF-UCL
  • mitochondrial membrane fusion Source: UniProtKB
  • mitochondrion localization Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mitofusin-1 (EC:3.6.5.-2 Publications)
Alternative name(s):
Fzo homolog1 Publication
Transmembrane GTPase MFN1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MFN1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000171109.18

Human Gene Nomenclature Database

More...
HGNCi
HGNC:18262 MFN1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608506 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8IWA4

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 584CytoplasmicSequence analysisAdd BLAST584
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei585 – 605Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini606 – 608Mitochondrial intermembraneSequence analysis3
Transmembranei609 – 629Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini630 – 741CytoplasmicSequence analysisAdd BLAST112

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi15K → A: Decreases GTPase activity. Impairs mitochondrial fusion. 2 Publications1
Mutagenesisi74R → P: Mildly decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi88K → A: Abolishes GTPase activity. Abolishes dimerization. 1 Publication1
Mutagenesisi88K → T: Induces a strong decrease in mitochondrial clustering. 1 Publication1
Mutagenesisi99K → A: Mildly decreases GTPase activity. 1 Publication1
Mutagenesisi102P → L: Impairs protein folding. Decreases GTPase activity. 1 Publication1
Mutagenesisi107H → A: Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi109T → A: Acts as a dominant negative mutant; induces fragmentation of mitochondria. 1 Publication1
Mutagenesisi144H → A: Abolishes GTPase activity. Abolishes dimerization. 1 Publication1
Mutagenesisi173D → A: Decreases GTPase activity. 1 Publication1
Mutagenesisi189D → A: Causes mitochondrial clumping. 1 Publication1
Mutagenesisi209E → A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi238R → A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi239W → A: Abolishes GTP binding and GTPase activity. Loss of function in mitochondrial fusion. 1 Publication1
Mutagenesisi245E → A: Decreases GTPase activity. Abolishes dimerization. Impairs mitochondrial fusion. 1 Publication1
Mutagenesisi309G → P: Mildly decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi328I → A: Slightly decreases GTPase activity. 1 Publication1
Mutagenesisi336K → N: Loss of function in mitochondrial fusion. Abolishes dimerization. Decreases GTPase activity. 1 Publication1
Mutagenesisi336K → P: Decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi705L → P: Impairs protein folding. Decreases GTPase activity. 2 Publications1
Mutagenesisi733F → P: Impairs protein folding. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
55669

Open Targets

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OpenTargetsi
ENSG00000171109

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134945973

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
MFN1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
150421594

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001276721 – 741Mitofusin-1Add BLAST741

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated by non-degradative ubiquitin by PRKN (PubMed:23933751). Deubiquitination by USP30 inhibits mitochondrial fusion (By similarity). Ubiquitinated by MARCH5 (PubMed:20103533). When mitochondria are depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7 and PRKN (PubMed:23933751).By similarity2 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q8IWA4

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q8IWA4

MaxQB - The MaxQuant DataBase

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MaxQBi
Q8IWA4

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q8IWA4

PeptideAtlas

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PeptideAtlasi
Q8IWA4

PRoteomics IDEntifications database

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PRIDEi
Q8IWA4

ProteomicsDB human proteome resource

More...
ProteomicsDBi
70826
70827 [Q8IWA4-2]
70828 [Q8IWA4-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q8IWA4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8IWA4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in kidney and heart (at protein level) (PubMed:12759376). Ubiquitous (PubMed:11950885, PubMed:12759376). Expressed at slightly higher level in kidney and heart (PubMed:12759376). Isoform 2 may be overexpressed in some tumors, such as lung cancers (PubMed:11751411).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000171109 Expressed in 227 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

More...
CleanExi
HS_MFN1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q8IWA4 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8IWA4 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA059230

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer, also in the absence of bound GTP (PubMed:27920125, PubMed:28114303). Forms higher oligomers in the presence of a transition state GTP analog (PubMed:28114303). Forms homomultimers and heteromultimers with MFN2 (By similarity). Oligomerization is essential for mitochondrion fusion (PubMed:27920125, PubMed:28114303). Component of a high molecular weight multiprotein complex (PubMed:12759376). Interacts with VAT1 (By similarity).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MAVSQ7Z4342EBI-1048197,EBI-995373

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
120801, 16 interactors

Database of interacting proteins

More...
DIPi
DIP-50289N

Protein interaction database and analysis system

More...
IntActi
Q8IWA4, 6 interactors

Molecular INTeraction database

More...
MINTi
Q8IWA4

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000263969

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GNRX-ray2.65A1-364[»]
A696-741[»]
5GNSX-ray2.70A1-364[»]
A696-741[»]
5GNTX-ray2.67A1-364[»]
A696-741[»]
5GNUX-ray4.11A1-364[»]
A696-741[»]
5GO4X-ray2.20A1-365[»]
A696-741[»]
5GOEX-ray1.80A1-369[»]
A696-741[»]
5GOFX-ray1.60A1-362[»]
A696-741[»]
5GOMX-ray2.80A/B1-362[»]
A/B696-741[»]
5YEWX-ray3.20A/B/C1-364[»]
A/B/C694-741[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q8IWA4

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8IWA4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini72 – 321Dynamin-type GPROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 73Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST65
Regioni82 – 89G1 motifPROSITE-ProRule annotation8
Regioni108 – 109G2 motifPROSITE-ProRule annotation2
Regioni178 – 181G3 motifPROSITE-ProRule annotation4
Regioni237 – 240G4 motifPROSITE-ProRule annotation4
Regioni266G5 motifPROSITE-ProRule annotation1
Regioni338 – 364Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST27
Regioni703 – 734Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili371 – 408Sequence analysisAdd BLAST38
Coiled coili679 – 734Sequence analysisAdd BLAST56

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0448 Eukaryota
COG0699 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013727

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052465

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8IWA4

KEGG Orthology (KO)

More...
KOi
K21356

Identification of Orthologs from Complete Genome Data

More...
OMAi
AQNRIFF

Database of Orthologous Groups

More...
OrthoDBi
216494at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8IWA4

TreeFam database of animal gene trees

More...
TreeFami
TF314289

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022812 Dynamin_SF
IPR006884 Fzo/mitofusin_HR2
IPR030381 G_DYNAMIN_dom
IPR027088 Mitofusin-1
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR10465 PTHR10465, 1 hit
PTHR10465:SF2 PTHR10465:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00350 Dynamin_N, 1 hit
PF04799 Fzo_mitofusin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8IWA4-1) [UniParc]FASTAAdd to basket
Also known as: TG7411 Publication

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
MAEPVSPLKH FVLAKKAITA IFDQLLEFVT EGSHFVEATY KNPELDRIAT
60 70 80 90 100
EDDLVEMQGY KDKLSIIGEV LSRRHMKVAF FGRTSSGKSS VINAMLWDKV
110 120 130 140 150
LPSGIGHITN CFLSVEGTDG DKAYLMTEGS DEKKSVKTVN QLAHALHMDK
160 170 180 190 200
DLKAGCLVRV FWPKAKCALL RDDLVLVDSP GTDVTTELDS WIDKFCLDAD
210 220 230 240 250
VFVLVANSES TLMNTEKHFF HKVNERLSKP NIFILNNRWD ASASEPEYME
260 270 280 290 300
DVRRQHMERC LHFLVEELKV VNALEAQNRI FFVSAKEVLS ARKQKAQGMP
310 320 330 340 350
ESGVALAEGF HARLQEFQNF EQIFEECISQ SAVKTKFEQH TIRAKQILAT
360 370 380 390 400
VKNIMDSVNL AAEDKRHYSV EEREDQIDRL DFIRNQMNLL TLDVKKKIKE
410 420 430 440 450
VTEEVANKVS CAMTDEICRL SVLVDEFCSE FHPNPDVLKI YKSELNKHIE
460 470 480 490 500
DGMGRNLADR CTDEVNALVL QTQQEIIENL KPLLPAGIQD KLHTLIPCKK
510 520 530 540 550
FDLSYNLNYH KLCSDFQEDI VFRFSLGWSS LVHRFLGPRN AQRVLLGLSE
560 570 580 590 600
PIFQLPRSLA STPTAPTTPA TPDNASQEEL MITLVTGLAS VTSRTSMGII
610 620 630 640 650
IVGGVIWKTI GWKLLSVSLT MYGALYLYER LSWTTHAKER AFKQQFVNYA
660 670 680 690 700
TEKLRMIVSS TSANCSHQVK QQIATTFARL CQQVDITQKQ LEEEIARLPK
710 720 730 740
EIDQLEKIQN NSKLLRNKAV QLENELENFT KQFLPSSNEE S
Length:741
Mass (Da):84,160
Last modified:March 28, 2018 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB7BDC22437E30A58
GO
Isoform 2 (identifier: Q8IWA4-2) [UniParc]FASTAAdd to basket
Also known as: TG3701 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     367-370: HYSV → FHVQ
     371-741: Missing.

Show »
Length:370
Mass (Da):41,883
Checksum:i187B06EA1E971C6E
GO
Isoform 3 (identifier: Q8IWA4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     444-554: Missing.

Show »
Length:630
Mass (Da):71,401
Checksum:iD173A310365208BD
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C5H5H7C5H5_HUMAN
Mitofusin-1
MFN1
493Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JQT7C9JQT7_HUMAN
Mitofusin-1
MFN1
124Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JXQ1C9JXQ1_HUMAN
Mitofusin-1
MFN1
154Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti17A → G in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti21I → V in BAA91327 (PubMed:14702039).Curated1
Sequence conflicti162W → C in AAB64220 (PubMed:9230308).Curated1
Sequence conflicti226R → W in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti271V → A in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti406A → P in AAB64220 (PubMed:9230308).Curated1
Sequence conflicti688Q → H in AAB64220 (PubMed:9230308).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_036115415D → H in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_018606523R → P. Corresponds to variant dbSNP:rs7637065Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010362367 – 370HYSV → FHVQ in isoform 2. 1 Publication4
Alternative sequenceiVSP_010363371 – 741Missing in isoform 2. 1 PublicationAdd BLAST371
Alternative sequenceiVSP_010364444 – 554Missing in isoform 3. 1 PublicationAdd BLAST111

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF329637 mRNA Translation: AAK06840.1
AK000700 mRNA Translation: BAA91327.1
AK314306 mRNA Translation: BAG36958.1
AC007823 Genomic DNA No translation available.
AC007620 Genomic DNA No translation available.
KF457722 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78406.1
CH471052 Genomic DNA Translation: EAW78410.1
CH471052 Genomic DNA Translation: EAW78411.1
BC040557 mRNA Translation: AAH40557.1
U95822 mRNA Translation: AAB64220.1
AF054986 mRNA Translation: AAC09347.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3228.1 [Q8IWA4-1]

NCBI Reference Sequences

More...
RefSeqi
NP_284941.2, NM_033540.2 [Q8IWA4-1]
XP_005247653.2, XM_005247596.3 [Q8IWA4-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.478383

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000263969; ENSP00000263969; ENSG00000171109 [Q8IWA4-1]
ENST00000357390; ENSP00000349963; ENSG00000171109 [Q8IWA4-2]
ENST00000471841; ENSP00000420617; ENSG00000171109 [Q8IWA4-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
55669

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:55669

UCSC genome browser

More...
UCSCi
uc003fjs.4 human [Q8IWA4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329637 mRNA Translation: AAK06840.1
AK000700 mRNA Translation: BAA91327.1
AK314306 mRNA Translation: BAG36958.1
AC007823 Genomic DNA No translation available.
AC007620 Genomic DNA No translation available.
KF457722 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78406.1
CH471052 Genomic DNA Translation: EAW78410.1
CH471052 Genomic DNA Translation: EAW78411.1
BC040557 mRNA Translation: AAH40557.1
U95822 mRNA Translation: AAB64220.1
AF054986 mRNA Translation: AAC09347.1
CCDSiCCDS3228.1 [Q8IWA4-1]
RefSeqiNP_284941.2, NM_033540.2 [Q8IWA4-1]
XP_005247653.2, XM_005247596.3 [Q8IWA4-1]
UniGeneiHs.478383

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GNRX-ray2.65A1-364[»]
A696-741[»]
5GNSX-ray2.70A1-364[»]
A696-741[»]
5GNTX-ray2.67A1-364[»]
A696-741[»]
5GNUX-ray4.11A1-364[»]
A696-741[»]
5GO4X-ray2.20A1-365[»]
A696-741[»]
5GOEX-ray1.80A1-369[»]
A696-741[»]
5GOFX-ray1.60A1-362[»]
A696-741[»]
5GOMX-ray2.80A/B1-362[»]
A/B696-741[»]
5YEWX-ray3.20A/B/C1-364[»]
A/B/C694-741[»]
ProteinModelPortaliQ8IWA4
SMRiQ8IWA4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120801, 16 interactors
DIPiDIP-50289N
IntActiQ8IWA4, 6 interactors
MINTiQ8IWA4
STRINGi9606.ENSP00000263969

Protein family/group databases

TCDBi1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

PTM databases

iPTMnetiQ8IWA4
PhosphoSitePlusiQ8IWA4

Polymorphism and mutation databases

BioMutaiMFN1
DMDMi150421594

Proteomic databases

EPDiQ8IWA4
jPOSTiQ8IWA4
MaxQBiQ8IWA4
PaxDbiQ8IWA4
PeptideAtlasiQ8IWA4
PRIDEiQ8IWA4
ProteomicsDBi70826
70827 [Q8IWA4-2]
70828 [Q8IWA4-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
55669
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263969; ENSP00000263969; ENSG00000171109 [Q8IWA4-1]
ENST00000357390; ENSP00000349963; ENSG00000171109 [Q8IWA4-2]
ENST00000471841; ENSP00000420617; ENSG00000171109 [Q8IWA4-1]
GeneIDi55669
KEGGihsa:55669
UCSCiuc003fjs.4 human [Q8IWA4-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
55669
DisGeNETi55669
EuPathDBiHostDB:ENSG00000171109.18

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MFN1
HGNCiHGNC:18262 MFN1
HPAiHPA059230
MIMi608506 gene
neXtProtiNX_Q8IWA4
OpenTargetsiENSG00000171109
PharmGKBiPA134945973

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0448 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00390000013727
HOVERGENiHBG052465
InParanoidiQ8IWA4
KOiK21356
OMAiAQNRIFF
OrthoDBi216494at2759
PhylomeDBiQ8IWA4
TreeFamiTF314289

Enzyme and pathway databases

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

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MFN1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
55669

Protein Ontology

More...
PROi
PR:Q8IWA4

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000171109 Expressed in 227 organ(s), highest expression level in secondary oocyte
CleanExiHS_MFN1
ExpressionAtlasiQ8IWA4 baseline and differential
GenevisibleiQ8IWA4 HS

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR006884 Fzo/mitofusin_HR2
IPR030381 G_DYNAMIN_dom
IPR027088 Mitofusin-1
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PTHR10465:SF2 PTHR10465:SF2, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMFN1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IWA4
Secondary accession number(s): A0A0C4DFN1
, B2RAR1, D3DNR6, O15323, O60639, Q9BZB5, Q9NWQ2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 28, 2018
Last modified: January 16, 2019
This is version 149 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
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