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Protein

Mitochondrial fission 1 protein

Gene

Fis1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. May be not essential for the assembly of functional fission complexes and the subsequent membrane scission event. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial fission 1 protein
Alternative name(s):
FIS1 homolog
Tetratricopeptide repeat protein 11
Short name:
TPR repeat protein 11
Gene namesi
Name:Fis1
Synonyms:Ttc11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1913687. Fis1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 122122CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Topological domaini144 – 1529Mitochondrial intermembraneSequence Analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Mitochondrial fission 1 proteinPRO_0000106394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei10 – 101PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated by MARCH5.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9CQ92.
PaxDbiQ9CQ92.
PRIDEiQ9CQ92.

PTM databases

PhosphoSiteiQ9CQ92.

Expressioni

Gene expression databases

BgeeiQ9CQ92.
ExpressionAtlasiQ9CQ92. baseline and differential.
GenevestigatoriQ9CQ92.

Interactioni

Subunit structurei

Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5 (By similarity). Interacts with MIEF1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211472. 1 interaction.
IntActiQ9CQ92. 1 interaction.
MINTiMINT-1859640.
STRINGi10090.ENSMUSP00000019198.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 65Combined sources
Helixi11 – 2717Combined sources
Helixi32 – 4413Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 6114Combined sources
Helixi68 – 8316Combined sources
Helixi87 – 10014Combined sources
Helixi105 – 12016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYGNMR-A1-120[»]
ProteinModelPortaliQ9CQ92.
SMRiQ9CQ92. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CQ92.

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.By similarity

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.
InParanoidiQ9CQ92.
KOiK17969.
OMAiTELPYAA.
PhylomeDBiQ9CQ92.
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.

Q9CQ92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNED
60 70 80 90 100
IRRGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT
110 120 130 140 150
EPQNNQAKEL ERLIDKAMKK DGLVGMAIVG GMALGVAGLA GLIGLAVSKS

KS
Length:152
Mass (Da):17,009
Last modified:June 1, 2001 - v1
Checksum:iB012DF491518A4B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004479 mRNA. Translation: BAB23324.1.
AK004917 mRNA. Translation: BAB23668.1.
AK008078 mRNA. Translation: BAB25445.1.
AK008323 mRNA. Translation: BAB25601.1.
AK008916 mRNA. Translation: BAB25966.1.
BC010783 mRNA. Translation: AAH10783.1.
CCDSiCCDS19757.1.
RefSeqiNP_001156715.1. NM_001163243.1.
NP_079838.1. NM_025562.3.
UniGeneiMm.25849.

Genome annotation databases

EnsembliENSMUST00000019198; ENSMUSP00000019198; ENSMUSG00000019054.
GeneIDi66437.
KEGGimmu:66437.
UCSCiuc009abf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004479 mRNA. Translation: BAB23324.1.
AK004917 mRNA. Translation: BAB23668.1.
AK008078 mRNA. Translation: BAB25445.1.
AK008323 mRNA. Translation: BAB25601.1.
AK008916 mRNA. Translation: BAB25966.1.
BC010783 mRNA. Translation: AAH10783.1.
CCDSiCCDS19757.1.
RefSeqiNP_001156715.1. NM_001163243.1.
NP_079838.1. NM_025562.3.
UniGeneiMm.25849.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYGNMR-A1-120[»]
ProteinModelPortaliQ9CQ92.
SMRiQ9CQ92. Positions 1-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211472. 1 interaction.
IntActiQ9CQ92. 1 interaction.
MINTiMINT-1859640.
STRINGi10090.ENSMUSP00000019198.

PTM databases

PhosphoSiteiQ9CQ92.

Proteomic databases

MaxQBiQ9CQ92.
PaxDbiQ9CQ92.
PRIDEiQ9CQ92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019198; ENSMUSP00000019198; ENSMUSG00000019054.
GeneIDi66437.
KEGGimmu:66437.
UCSCiuc009abf.2. mouse.

Organism-specific databases

CTDi51024.
MGIiMGI:1913687. Fis1.

Phylogenomic databases

eggNOGiNOG235677.
GeneTreeiENSGT00390000000592.
HOGENOMiHOG000165386.
HOVERGENiHBG081530.
InParanoidiQ9CQ92.
KOiK17969.
OMAiTELPYAA.
PhylomeDBiQ9CQ92.
TreeFamiTF315180.

Miscellaneous databases

EvolutionaryTraceiQ9CQ92.
NextBioi321685.
PROiQ9CQ92.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ92.
ExpressionAtlasiQ9CQ92. baseline and differential.
GenevestigatoriQ9CQ92.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Liver, Small intestine and Stomach.
  2. "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: Kidney.
  3. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-32; 54-64; 72-83 AND 96-108, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  4. "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.
  5. "Solution structure of RSGI RUH-001, a FIS1p-like and CGI-135 homologous domain from a mouse cDNA."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2002) to the PDB data bank
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFIS1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.