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Q9Y3D6

- FIS1_HUMAN

UniProt

Q9Y3D6 - FIS1_HUMAN

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Protein

Mitochondrial fission 1 protein

Gene

FIS1

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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9Y3D6.
CleanExiHS_FIS1.
ExpressionAtlasiQ9Y3D6. baseline and differential.
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.
GeneTreeiENSGT00390000000592.
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_dom.
[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

        10         20         30         40         50
MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD
60 70 80 90 100
IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT
110 120 130 140 150
EPQNNQAKEL ERLIDKAMKK DGLVGMAIVG GMALGVAGLA GLIGLAVSKS

KS
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.
GeneTreei ENSGT00390000000592.
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

Bgeei Q9Y3D6.
CleanExi HS_FIS1.
ExpressionAtlasi Q9Y3D6. baseline and differential.
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_dom.
[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

« Hide 'large scale' publications
  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 29, 2014
This is version 129 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