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Q9Y3D6

- FIS1_HUMAN

UniProt

Q9Y3D6 - FIS1_HUMAN

Protein

Mitochondrial fission 1 protein

Gene

FIS1

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

    Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission.7 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor binding Source: UniProtKB

    GO - Biological processi

    1. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
    2. mitochondrial fission Source: UniProtKB
    3. mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
    4. mitochondrial fusion Source: UniProtKB
    5. mitochondrion degradation Source: UniProtKB
    6. mitochondrion morphogenesis Source: UniProtKB
    7. negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProtKB
    8. peroxisome fission Source: UniProtKB
    9. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    10. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    11. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    12. positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
    13. positive regulation of mitochondrial fission Source: UniProtKB
    14. positive regulation of protein targeting to membrane Source: UniProtKB
    15. protein homooligomerization Source: UniProtKB
    16. protein targeting to mitochondrion Source: UniProtKB
    17. regulation of mitochondrion organization Source: UniProtKB
    18. release of cytochrome c from mitochondria Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial fission 1 protein
    Alternative name(s):
    FIS1 homolog
    Short name:
    hFis1
    Tetratricopeptide repeat protein 11
    Short name:
    TPR repeat protein 11
    Gene namesi
    Name:FIS1
    Synonyms:TTC11
    ORF Names:CGI-135
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21689. FIS1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of mitochondrial outer membrane Source: UniProtKB
    2. integral component of peroxisomal membrane Source: UniProtKB
    3. membrane Source: UniProtKB
    4. mitochondrion Source: UniProtKB
    5. peroxisome Source: UniProtKB
    6. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141L → P: Approximately 40% of cells display fragmented mitochondria. 1 Publication
    Mutagenesisi42 – 421L → P: Less than 15% of cells display fragmented mitochondria. 1 Publication
    Mutagenesisi58 – 581L → P: Less than 15% of cells display fragmented mitochondria. 1 Publication
    Mutagenesisi77 – 771L → P: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L. 1 Publication
    Mutagenesisi91 – 911L → P: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L. 1 Publication
    Mutagenesisi110 – 1101L → P: Approximately 40% of cells display fragmented mitochondria. No change in binding to DNM1L. 1 Publication
    Mutagenesisi149 – 1491K → A: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-151. 1 Publication
    Mutagenesisi151 – 1511K → A: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-149. 1 Publication

    Organism-specific databases

    PharmGKBiPA134984211.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152152Mitochondrial fission 1 proteinPRO_0000106393Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Post-translational modificationi

    Ubiquitinated by MARCH5.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y3D6.
    PaxDbiQ9Y3D6.
    PeptideAtlasiQ9Y3D6.
    PRIDEiQ9Y3D6.

    2D gel databases

    UCD-2DPAGEQ9Y3D6.

    PTM databases

    PhosphoSiteiQ9Y3D6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y3D6.
    BgeeiQ9Y3D6.
    CleanExiHS_FIS1.
    GenevestigatoriQ9Y3D6.

    Organism-specific databases

    HPAiHPA017430.

    Interactioni

    Subunit structurei

    Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5. Interacts with MIEF1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAP31P515728EBI-3385283,EBI-77683
    MIEF1Q9NQG64EBI-3385283,EBI-740987

    Protein-protein interaction databases

    BioGridi119230. 23 interactions.
    IntActiQ9Y3D6. 9 interactions.
    MINTiMINT-2844167.
    STRINGi9606.ENSP00000223136.

    Structurei

    Secondary structure

    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 2727
    Helixi32 – 4211
    Beta strandi45 – 473
    Helixi48 – 6114
    Turni62 – 643
    Helixi67 – 8317
    Helixi87 – 10014
    Helixi105 – 12016
    Beta strandi129 – 1335
    Beta strandi142 – 1443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NZNX-ray2.00A1-123[»]
    1PC2NMR-A1-145[»]
    DisProtiDP00457.
    ProteinModelPortaliQ9Y3D6.
    SMRiQ9Y3D6. Positions 1-145.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3D6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 122122CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini144 – 1529Mitochondrial intermembraneSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei123 – 14321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati71 – 10434TPRAdd
    BLAST

    Domaini

    The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.

    Sequence similaritiesi

    Belongs to the FIS1 family.Curated
    Contains 1 TPR repeat.Curated

    Keywords - Domaini

    TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG235677.
    HOGENOMiHOG000165386.
    HOVERGENiHBG081530.
    InParanoidiQ9Y3D6.
    KOiK17969.
    OMAiEIFRTSP.
    PhylomeDBiQ9Y3D6.
    TreeFamiTF315180.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR016543. Fis1.
    IPR028061. Fis1_TPR_C.
    IPR028058. Fis1_TPR_N.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PANTHERiPTHR13247. PTHR13247. 1 hit.
    PfamiPF14853. Fis1_TPR_C. 1 hit.
    PF14852. Fis1_TPR_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF008835. TPR_repeat_11_Fis1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Y3D6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD    50
    IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT 100
    EPQNNQAKEL ERLIDKAMKK DGLVGMAIVG GMALGVAGLA GLIGLAVSKS 150
    KS 152
    Length:152
    Mass (Da):16,938
    Last modified:July 19, 2003 - v2
    Checksum:i6E76EC02B3731A9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 462SK → TR in AAD34130. (PubMed:10810093)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151893 mRNA. Translation: AAD34130.1.
    AC006329 Genomic DNA. Translation: AAP22366.1.
    BC003540 mRNA. Translation: AAH03540.1.
    BC009428 mRNA. Translation: AAH09428.1.
    CCDSiCCDS43626.1.
    RefSeqiNP_057152.2. NM_016068.2.
    UniGeneiHs.423968.

    Genome annotation databases

    EnsembliENST00000223136; ENSP00000223136; ENSG00000214253.
    GeneIDi51024.
    KEGGihsa:51024.
    UCSCiuc003uyj.4. human.

    Polymorphism databases

    DMDMi33112470.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151893 mRNA. Translation: AAD34130.1 .
    AC006329 Genomic DNA. Translation: AAP22366.1 .
    BC003540 mRNA. Translation: AAH03540.1 .
    BC009428 mRNA. Translation: AAH09428.1 .
    CCDSi CCDS43626.1.
    RefSeqi NP_057152.2. NM_016068.2.
    UniGenei Hs.423968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NZN X-ray 2.00 A 1-123 [» ]
    1PC2 NMR - A 1-145 [» ]
    DisProti DP00457.
    ProteinModelPortali Q9Y3D6.
    SMRi Q9Y3D6. Positions 1-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119230. 23 interactions.
    IntActi Q9Y3D6. 9 interactions.
    MINTi MINT-2844167.
    STRINGi 9606.ENSP00000223136.

    PTM databases

    PhosphoSitei Q9Y3D6.

    Polymorphism databases

    DMDMi 33112470.

    2D gel databases

    UCD-2DPAGE Q9Y3D6.

    Proteomic databases

    MaxQBi Q9Y3D6.
    PaxDbi Q9Y3D6.
    PeptideAtlasi Q9Y3D6.
    PRIDEi Q9Y3D6.

    Protocols and materials databases

    DNASUi 51024.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223136 ; ENSP00000223136 ; ENSG00000214253 .
    GeneIDi 51024.
    KEGGi hsa:51024.
    UCSCi uc003uyj.4. human.

    Organism-specific databases

    CTDi 51024.
    GeneCardsi GC07M100882.
    HGNCi HGNC:21689. FIS1.
    HPAi HPA017430.
    MIMi 609003. gene.
    neXtProti NX_Q9Y3D6.
    PharmGKBi PA134984211.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235677.
    HOGENOMi HOG000165386.
    HOVERGENi HBG081530.
    InParanoidi Q9Y3D6.
    KOi K17969.
    OMAi EIFRTSP.
    PhylomeDBi Q9Y3D6.
    TreeFami TF315180.

    Miscellaneous databases

    ChiTaRSi FIS1. human.
    EvolutionaryTracei Q9Y3D6.
    GeneWikii FIS1.
    GenomeRNAii 51024.
    NextBioi 53558.
    PROi Q9Y3D6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y3D6.
    Bgeei Q9Y3D6.
    CleanExi HS_FIS1.
    Genevestigatori Q9Y3D6.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR016543. Fis1.
    IPR028061. Fis1_TPR_C.
    IPR028058. Fis1_TPR_N.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    PANTHERi PTHR13247. PTHR13247. 1 hit.
    Pfami PF14853. Fis1_TPR_C. 1 hit.
    PF14852. Fis1_TPR_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF008835. TPR_repeat_11_Fis1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Pancreas.
    4. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-16, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    5. "hFis1, a novel component of the mammalian mitochondrial fission machinery."
      James D.I., Parone P.A., Mattenberger Y., Martinou J.-C.
      J. Biol. Chem. 278:36373-36379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1."
      Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A.
      Mol. Cell. Biol. 23:5409-5420(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNM1L.
    7. "Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology."
      Stojanovski D., Koutsopoulos O.S., Okamoto K., Ryan M.T.
      J. Cell Sci. 117:1201-1210(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF LYS-149 AND LYS-151.
    8. "Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1."
      Yu T., Fox R.J., Burwell L.S., Yoon Y.
      J. Cell Sci. 118:4141-4151(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNM1L, MUTAGENESIS OF LEU-14; LEU-42; LEU-58; LEU-77; LEU-91 AND LEU-110.
    9. "A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells."
      Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., Schrader M.
      Mol. Biol. Cell 16:5077-5086(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics."
      Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.
      EMBO J. 25:3618-3626(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
      Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
      EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIEF1.
    14. "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.
    15. "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]
      Cited for: FUNCTION.
    16. "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.
    17. "Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold."
      Dohm J.A., Lee S.J., Hardwick J.M., Hill R.B., Gittis A.G.
      Proteins 54:153-156(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-123.
    18. "The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle."
      Suzuki M., Jeong S.-Y., Karbowski M., Youle R.J., Tjandra N.
      J. Mol. Biol. 334:445-458(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiFIS1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3D6
    Secondary accession number(s): Q9BTP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: July 19, 2003
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3