Mitochondrial fission factor

<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

<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

• identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.17

    "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBUNIT.

GO - Biological processⁱ

• mitochondrial fission Source: UniProtKB
• mitochondrial fragmentation involved in apoptotic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.1

    "The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
    Gandre-Babbe S., van der Bliek A.M.
    Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• mitochondrial fusion Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.15

    "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
    Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
    J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION.
• mitochondrion morphogenesis Source: MGIInferred from mutant phenotypeⁱ
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• peroxisome fission Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
    Gandre-Babbe S., van der Bliek A.M.
    Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of mitochondrial fission Source: UniProtKBInferred from direct assayⁱ
  • "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
    Loson O.C., Song Z., Chen H., Chan D.C.
    Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
  • Ref.17

    "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBUNIT.
• positive regulation of protein targeting to membrane Source: UniProtKBInferred from direct assayⁱ
  • "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
    Loson O.C., Song Z., Chen H., Chan D.C.
    Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of release of cytochrome c from mitochondria Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• protein targeting to mitochondrion Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of mitochondrion organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
    Gandre-Babbe S., van der Bliek A.M.
    Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
  • "Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells."
    Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K.
    J Cell Biol 191:1141-1158(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of peroxisome organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
    Gandre-Babbe S., van der Bliek A.M.
    Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.
• release of cytochrome c from mitochondria Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells."
    Gandre-Babbe S., van der Bliek A.M.
    Mol. Biol. Cell 19:2402-2412(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY.

Enzyme and pathway databases

<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

Organism-specific databases

<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

• UniProt annotation
• GO - Cellular component

Topology

<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>Keywords - Cellular componentⁱ

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<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

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBUNIT.

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

<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

Coiled coil

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 5 described isoforms and 12 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSKGTSSDTS LGRVSRAAFP SPTAAEMAEI SRIQYEMEYT EGISQRMRVP 
        60         70         80         90        100
EKLKVAPPNA DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DVSFSRPADL 
       110        120        130        140        150
DLIQSTPFKP LALKTPPRVL TLSERPLDFL DLERPPTTPQ NEEIRAVGRL 
       160        170        180        190        200
KRERSMSENA VRQNGQLVRN DSLWHRSDSA PRNKISRFQA PISAPEYTVT 
       210        220        230        240        250
PSPQQARVCP PHMLPEDGAN LSSARGILSL IQSSTRRAYQ QILDVLDENR 
       260        270        280        290        300
RPVLRGGSAA ATSNPHHDNV RYGISNIDTT IEGTSDDLTV VDAASLRRQI 
       310        320        330        340 
IKLNRRLQLL EEENKERAKR EMVMYSITVA FWLLNSWLWF RR         

        10         20         30         40         50
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVPNASVI 
        60         70         80         90        100
MQVPERIVVA GNNEDVSFSR PADLDLIQST PFKPLALKTP PRVLTLSERP 
       110        120        130        140        150
LDFLDLERPP TTPQNEEIRA VGRLKRERSM SENAVRQNGQ LVRNDSLVTP 
       160        170        180        190        200
SPQQARVCPP HMLPEDGANL SSARGILSLI QSSTRRAYQQ ILDVLDENRR 
       210        220        230        240        250
PVLRGGSAAA TSNPHHDNVR YGISNIDTTI EGTSDDLTVV DAASLRRQII 
       260        270        280        290 
KLNRRLQLLE EENKERAKRE MVMYSITVAF WLLNSWLWFR R          

        10         20         30         40         50
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVPNASVI 
        60         70         80         90        100
MQVPERIVVA GNNEDVSFSR PADLDLIQST PFKPLALKTP PRVLTLSERP 
       110        120        130        140        150
LDFLDLERPP TTPQNEEIRA VGRLKRERSM SENAVRQNGQ LVRNDSLWHR 
       160        170        180        190        200
SDSAPRNKIS RFQAPISAPE YTYGISNIDT TIEGTSDDLT VVDAASLRRQ 
       210        220        230        240 
IIKLNRRLQL LEEENKERAK REMVMYSITV AFWLLNSWLW FRR        

        10         20         30         40         50
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVPNASVI 
        60         70         80         90        100
MQVPERIVVA GNNEDVSFSR PADLDLIQST PFKPLALKTP PRVLTLSERP 
       110        120        130        140        150
LDFLDLERPP TTPQNEEIRA VGRLKRERSM SENAVRQNGQ LVRNDSLYGI 
       160        170        180        190        200
SNIDTTIEGT SDDLTVVDAA SLRRQIIKLN RRLQLLEEEN KERAKREMVM 
       210 
YSITVAFWLL NSWLWFRR                                    

        10         20         30         40         50
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVPNASVI 
        60         70         80         90        100
MQVPERIVVA GNNEDVSFSR PADLDLIQST PFKPLALKTP PRVLTLSERP 
       110        120        130        140        150
LDFLDLERPP TTPQNEEIRA VGRLKRERSM SENAVRQNGQ LVRNDSLPVL 
       160        170        180        190        200
RGGSAAATSN PHHDNVRYGI SNIDTTIEGT SDDLTVVDAA SLRRQIIKLN 
       210        220        230 
RRLQLLEEEN KERAKREMVM YSITVAFWLL NSWLWFRR              

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

1. Human chromosome 2
   Human chromosome 2: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
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