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Q9GZY8

- MFF_HUMAN

UniProt

Q9GZY8 - MFF_HUMAN

Protein

Mitochondrial fission factor

Gene

MFF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. mitochondrial fission Source: UniProtKB
    2. mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
    3. mitochondrial fusion Source: UniProtKB
    4. mitochondrion morphogenesis Source: MGI
    5. peroxisome fission Source: UniProtKB
    6. positive regulation of mitochondrial fission Source: UniProtKB
    7. positive regulation of protein targeting to membrane Source: UniProtKB
    8. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    9. protein homooligomerization Source: UniProtKB
    10. protein targeting to mitochondrion Source: UniProtKB
    11. regulation of mitochondrion organization Source: UniProtKB
    12. regulation of peroxisome organization Source: UniProtKB
    13. release of cytochrome c from mitochondria Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial fission factor
    Gene namesi
    Name:MFF
    Synonyms:C2orf33
    ORF Names:AD030, AD033, GL004
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:24858. MFF.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. integral component of mitochondrial membrane Source: UniProtKB
    3. mitochondrial outer membrane Source: UniProtKB
    4. peroxisome Source: UniProtKB
    5. synaptic vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasmic vesicle, Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162395839.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Mitochondrial fission factorPRO_0000289184Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151Phosphothreonine1 Publication
    Modified residuei155 – 1551Phosphoserine3 Publications
    Modified residuei157 – 1571Phosphoserine3 Publications
    Modified residuei172 – 1721PhosphoserineBy similarity
    Modified residuei200 – 2001Phosphothreonine1 Publication
    Modified residuei202 – 2021Phosphoserine1 Publication
    Modified residuei229 – 2291Phosphoserine1 Publication
    Modified residuei233 – 2331Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9GZY8.
    PaxDbiQ9GZY8.
    PRIDEiQ9GZY8.

    PTM databases

    PhosphoSiteiQ9GZY8.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, kidney, liver, brain, muscle, and stomach.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZY8.
    BgeeiQ9GZY8.
    CleanExiHS_MFF.
    GenevestigatoriQ9GZY8.

    Organism-specific databases

    HPAiHPA010968.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DNM1L By similarity.By similarity

    Protein-protein interaction databases

    BioGridi121271. 6 interactions.
    STRINGi9606.ENSP00000302037.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GZY8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 322322CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini341 – 3422Mitochondrial intermembraneSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei323 – 34018Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili291 – 32232Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Tango11 family.Curated

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43415.
    HOGENOMiHOG000285976.
    HOVERGENiHBG105704.
    InParanoidiQ9GZY8.
    OMAiISAPEYT.
    PhylomeDBiQ9GZY8.
    TreeFamiTF325506.

    Family and domain databases

    InterProiIPR008518. FATE/Miff/Tango-11.
    [Graphical view]
    PANTHERiPTHR16501. PTHR16501. 1 hit.
    PfamiPF05644. Miff. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9GZY8-1) [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

    MSKGTSSDTS LGRVSRAAFP SPTAAEMAEI SRIQYEMEYT EGISQRMRVP    50
    EKLKVAPPNA DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DVSFSRPADL 100
    DLIQSTPFKP LALKTPPRVL TLSERPLDFL DLERPPTTPQ NEEIRAVGRL 150
    KRERSMSENA VRQNGQLVRN DSLWHRSDSA PRNKISRFQA PISAPEYTVT 200
    PSPQQARVCP PHMLPEDGAN LSSARGILSL IQSSTRRAYQ QILDVLDENR 250
    RPVLRGGSAA ATSNPHHDNV RYGISNIDTT IEGTSDDLTV VDAASLRRQI 300
    IKLNRRLQLL EEENKERAKR EMVMYSITVA FWLLNSWLWF RR 342
    Length:342
    Mass (Da):38,465
    Last modified:March 1, 2001 - v1
    Checksum:i1DBFBBE17DB122A0
    GO
    Isoform 2 (identifier: Q9GZY8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.
         174-198: Missing.

    Note: Contains a phosphothreonine at position 149. Contains a phosphoserine at position 151.

    Show »
    Length:291
    Mass (Da):32,973
    Checksum:i1CEA83C57D1E6FE6
    GO
    Isoform 3 (identifier: Q9GZY8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.
         199-271: Missing.

    Show »
    Length:243
    Mass (Da):27,964
    Checksum:i2D2B8A36FEA1C038
    GO
    Isoform 4 (identifier: Q9GZY8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.
         174-271: Missing.

    Show »
    Length:218
    Mass (Da):25,067
    Checksum:i07B22DF970A4995F
    GO
    Isoform 5 (identifier: Q9GZY8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.
         174-251: Missing.

    Note: Contains a phosphoserine at position 146.

    Show »
    Length:238
    Mass (Da):27,105
    Checksum:i3F647B952DAE2A05
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121H → Y in CAH56328. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71S → C.
    Corresponds to variant rs3211097 [ dbSNP | Ensembl ].
    VAR_053915
    Natural varianti7 – 71S → I.
    Corresponds to variant rs3211098 [ dbSNP | Ensembl ].
    VAR_053916
    Natural varianti29 – 291E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036028

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_025954Add
    BLAST
    Alternative sequencei174 – 27198Missing in isoform 4. 1 PublicationVSP_025955Add
    BLAST
    Alternative sequencei174 – 25178Missing in isoform 5. 1 PublicationVSP_025956Add
    BLAST
    Alternative sequencei174 – 19825Missing in isoform 2. 1 PublicationVSP_025957Add
    BLAST
    Alternative sequencei199 – 27173Missing in isoform 3. 1 PublicationVSP_025958Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK026137 mRNA. Translation: BAB15373.1.
    AF246239 mRNA. Translation: AAG44486.1.
    AF226049 mRNA. Translation: AAF86949.1.
    AF258660 mRNA. Translation: AAG44658.1.
    AC097662 Genomic DNA. Translation: AAY24252.1.
    BC000797 mRNA. Translation: AAH00797.1.
    BC093024 mRNA. Translation: AAH93024.1.
    AL833032 mRNA. Translation: CAH56328.1.
    CCDSiCCDS2465.1. [Q9GZY8-1]
    CCDS63139.1. [Q9GZY8-3]
    CCDS63140.1. [Q9GZY8-2]
    CCDS63141.1. [Q9GZY8-5]
    CCDS63142.1. [Q9GZY8-4]
    RefSeqiNP_001263990.1. NM_001277061.1. [Q9GZY8-1]
    NP_001263991.1. NM_001277062.1. [Q9GZY8-2]
    NP_001263992.1. NM_001277063.1. [Q9GZY8-3]
    NP_001263993.1. NM_001277064.1. [Q9GZY8-5]
    NP_001263994.1. NM_001277065.1. [Q9GZY8-4]
    NP_001263995.1. NM_001277066.1. [Q9GZY8-4]
    NP_001263996.1. NM_001277067.1.
    NP_001263997.1. NM_001277068.1.
    NP_064579.3. NM_020194.5. [Q9GZY8-1]
    XP_006712701.1. XM_006712638.1. [Q9GZY8-2]
    XP_006712702.1. XM_006712639.1. [Q9GZY8-5]
    UniGeneiHs.471528.

    Genome annotation databases

    EnsembliENST00000304593; ENSP00000304898; ENSG00000168958. [Q9GZY8-2]
    ENST00000337110; ENSP00000338412; ENSG00000168958. [Q9GZY8-3]
    ENST00000349901; ENSP00000304134; ENSG00000168958. [Q9GZY8-5]
    ENST00000353339; ENSP00000302037; ENSG00000168958. [Q9GZY8-1]
    ENST00000354503; ENSP00000346498; ENSG00000168958. [Q9GZY8-4]
    ENST00000392059; ENSP00000375912; ENSG00000168958. [Q9GZY8-1]
    ENST00000409565; ENSP00000386964; ENSG00000168958. [Q9GZY8-4]
    ENST00000409616; ENSP00000386641; ENSG00000168958. [Q9GZY8-5]
    GeneIDi56947.
    KEGGihsa:56947.
    UCSCiuc002vos.4. human. [Q9GZY8-1]
    uc002vot.4. human. [Q9GZY8-2]
    uc002vow.4. human. [Q9GZY8-3]
    uc002voz.4. human. [Q9GZY8-4]
    uc021vxu.2. human. [Q9GZY8-5]

    Polymorphism databases

    DMDMi74725008.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK026137 mRNA. Translation: BAB15373.1 .
    AF246239 mRNA. Translation: AAG44486.1 .
    AF226049 mRNA. Translation: AAF86949.1 .
    AF258660 mRNA. Translation: AAG44658.1 .
    AC097662 Genomic DNA. Translation: AAY24252.1 .
    BC000797 mRNA. Translation: AAH00797.1 .
    BC093024 mRNA. Translation: AAH93024.1 .
    AL833032 mRNA. Translation: CAH56328.1 .
    CCDSi CCDS2465.1. [Q9GZY8-1 ]
    CCDS63139.1. [Q9GZY8-3 ]
    CCDS63140.1. [Q9GZY8-2 ]
    CCDS63141.1. [Q9GZY8-5 ]
    CCDS63142.1. [Q9GZY8-4 ]
    RefSeqi NP_001263990.1. NM_001277061.1. [Q9GZY8-1 ]
    NP_001263991.1. NM_001277062.1. [Q9GZY8-2 ]
    NP_001263992.1. NM_001277063.1. [Q9GZY8-3 ]
    NP_001263993.1. NM_001277064.1. [Q9GZY8-5 ]
    NP_001263994.1. NM_001277065.1. [Q9GZY8-4 ]
    NP_001263995.1. NM_001277066.1. [Q9GZY8-4 ]
    NP_001263996.1. NM_001277067.1.
    NP_001263997.1. NM_001277068.1.
    NP_064579.3. NM_020194.5. [Q9GZY8-1 ]
    XP_006712701.1. XM_006712638.1. [Q9GZY8-2 ]
    XP_006712702.1. XM_006712639.1. [Q9GZY8-5 ]
    UniGenei Hs.471528.

    3D structure databases

    ProteinModelPortali Q9GZY8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121271. 6 interactions.
    STRINGi 9606.ENSP00000302037.

    PTM databases

    PhosphoSitei Q9GZY8.

    Polymorphism databases

    DMDMi 74725008.

    Proteomic databases

    MaxQBi Q9GZY8.
    PaxDbi Q9GZY8.
    PRIDEi Q9GZY8.

    Protocols and materials databases

    DNASUi 56947.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304593 ; ENSP00000304898 ; ENSG00000168958 . [Q9GZY8-2 ]
    ENST00000337110 ; ENSP00000338412 ; ENSG00000168958 . [Q9GZY8-3 ]
    ENST00000349901 ; ENSP00000304134 ; ENSG00000168958 . [Q9GZY8-5 ]
    ENST00000353339 ; ENSP00000302037 ; ENSG00000168958 . [Q9GZY8-1 ]
    ENST00000354503 ; ENSP00000346498 ; ENSG00000168958 . [Q9GZY8-4 ]
    ENST00000392059 ; ENSP00000375912 ; ENSG00000168958 . [Q9GZY8-1 ]
    ENST00000409565 ; ENSP00000386964 ; ENSG00000168958 . [Q9GZY8-4 ]
    ENST00000409616 ; ENSP00000386641 ; ENSG00000168958 . [Q9GZY8-5 ]
    GeneIDi 56947.
    KEGGi hsa:56947.
    UCSCi uc002vos.4. human. [Q9GZY8-1 ]
    uc002vot.4. human. [Q9GZY8-2 ]
    uc002vow.4. human. [Q9GZY8-3 ]
    uc002voz.4. human. [Q9GZY8-4 ]
    uc021vxu.2. human. [Q9GZY8-5 ]

    Organism-specific databases

    CTDi 56947.
    GeneCardsi GC02P228189.
    HGNCi HGNC:24858. MFF.
    HPAi HPA010968.
    MIMi 614785. gene.
    neXtProti NX_Q9GZY8.
    PharmGKBi PA162395839.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43415.
    HOGENOMi HOG000285976.
    HOVERGENi HBG105704.
    InParanoidi Q9GZY8.
    OMAi ISAPEYT.
    PhylomeDBi Q9GZY8.
    TreeFami TF325506.

    Miscellaneous databases

    ChiTaRSi MFF. human.
    GeneWikii Mitochondrial_fission_factor.
    GenomeRNAii 56947.
    NextBioi 62537.
    PROi Q9GZY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZY8.
    Bgeei Q9GZY8.
    CleanExi HS_MFF.
    Genevestigatori Q9GZY8.

    Family and domain databases

    InterProi IPR008518. FATE/Miff/Tango-11.
    [Graphical view ]
    PANTHERi PTHR16501. PTHR16501. 1 hit.
    Pfami PF05644. Miff. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "A novel gene expressed in human liver non-tumor tissues."
      Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Liver.
    4. Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 3 AND 5).
      Tissue: Placenta.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-342.
      Tissue: Stomach.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-155; SER-157; THR-200; SER-202; SER-229 AND SER-233, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    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.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-29.

    Entry informationi

    Entry nameiMFF_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZY8
    Secondary accession number(s): Q567U1
    , Q658R6, Q9BVZ1, Q9H690, Q9NRG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [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 2
      Human chromosome 2: 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

    External Data

    Dasty 3