Q9H019 · MFR1L_HUMAN

  • Protein
    Mitochondrial fission regulator 1-like
  • Gene
    MTFR1L
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Mitochondrial protein required for adaptation of miochondrial dynamics to metabolic changes. Regulates mitochondrial morphology at steady state and mediates AMPK-dependent stress-induced mitochondrial fragmentation via the control of OPA1 levels.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial outer membrane
Cellular Componentmitochondrion
Biological Processaerobic respiration
Biological Processmitochondrial fission

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitochondrial fission regulator 1-like

Gene names

    • Name
      MTFR1L
    • Synonyms
      FAM54B
    • ORF names
      HYST1888, MSTP116

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9H019
  • Secondary accessions
    • A6NCB4
    • B7WNV5
    • D3DPJ4
    • Q63HP1
    • Q7Z2S7
    • Q9NUI7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_04408458in dbSNP:rs35448678
Mutagenesis103Loss of phosphorylation by AMPK. No effect on mitochondrial morphology; when associated with A-238.
Mutagenesis103Leads to fragmentation of mitochondrial network; when associated with D-238.
Mutagenesis238Loss of phosphorylation by AMPK. No effect on mitochondrial morphology; when associated with A-103.
Mutagenesis238Leads to fragmentation of mitochondrial network; when associated with D-103.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 299 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00003415661-292UniProtMitochondrial fission regulator 1-like
Modified residue30UniProtPhosphothreonine
Modified residue41UniProtPhosphoserine
Modified residue (large scale data)41PRIDEPhosphoserine
Modified residue (large scale data)44PRIDEPhosphothreonine
Modified residue103UniProtPhosphoserine; by AMPK
Modified residue (large scale data)103PRIDEPhosphoserine
Modified residue110UniProtPhosphoserine
Modified residue (large scale data)110PRIDEPhosphoserine
Modified residue (large scale data)223PRIDEPhosphoserine
Modified residue224UniProtPhosphoserine
Modified residue (large scale data)224PRIDEPhosphoserine
Modified residue225UniProtPhosphoserine
Modified residue (large scale data)225PRIDEPhosphoserine
Modified residue (large scale data)232PRIDEPhosphoserine
Modified residue (large scale data)234PRIDEPhosphoserine
Modified residue (large scale data)237PRIDEPhosphoserine
Modified residue238UniProtPhosphoserine; by AMPK
Modified residue (large scale data)238PRIDEPhosphoserine
Modified residue261UniProtPhosphoserine
Modified residue (large scale data)261PRIDEPhosphoserine
Modified residue273UniProtPhosphoserine

Post-translational modification

Phosphorylated by AMPK. Upon stress, phosphorylation at Ser-103 and Ser-238 by AMPK is sufficient to induce mitochondrial fragmentation.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Family & Domains

Sequence similarities

Belongs to the MTFR1 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q9H019-1

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.

  • Length
    292
  • Mass (Da)
    31,957
  • Last updated
    2008-06-10 v2
  • Checksum
    39B23825CA1638EF
MSGMEATVTIPIWQNKPHGAARSVVRRIGTNLPLKPCARASFETLPNISDLCLRDVPPVPTLADIAWIAADEEETYARVRSDTRPLRHTWKPSPLIVMQRNASVPNLRGSEERLLALKKPALPALSRTTELQDELSHLRSQIAKIVAADAASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLLCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN

Q9H019-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 151-292: ASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLLCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN → VTSPRRQRWRSLSFHQSPCFVLPALNVANQNTKLPAVRLKRMTASLCPRPAALQT

Q9H019-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JF50C9JF50_HUMANMTFR1L152
E9PRK5E9PRK5_HUMANMTFR1L182
E9PRW1E9PRW1_HUMANMTFR1L110
E9PSD6E9PSD6_HUMANMTFR1L115
E9PPF9E9PPF9_HUMANMTFR1L160
E9PPQ0E9PPQ0_HUMANMTFR1L53
E9PNJ0E9PNJ0_HUMANMTFR1L13
E9PLD2E9PLD2_HUMANMTFR1L195
E9PLU1E9PLU1_HUMANMTFR1L170
E9PJP7E9PJP7_HUMANMTFR1L73
E9PIF9E9PIF9_HUMANMTFR1L52

Sequence caution

The sequence AAQ13638.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict87in Ref. 4; CAC21683
Sequence conflict136in Ref. 4; CAC21683
Alternative sequenceVSP_034339151-162in isoform 3
Alternative sequenceVSP_034338151-292in isoform 2
Sequence conflict273in Ref. 4; CAC21683

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF173891
EMBL· GenBank· DDBJ
AAQ13638.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AB075880
EMBL· GenBank· DDBJ
BAD38662.1
EMBL· GenBank· DDBJ
mRNA
AK290744
EMBL· GenBank· DDBJ
BAF83433.1
EMBL· GenBank· DDBJ
mRNA
AL512766
EMBL· GenBank· DDBJ
CAC21683.1
EMBL· GenBank· DDBJ
mRNA
BX647921
EMBL· GenBank· DDBJ
CAH56194.1
EMBL· GenBank· DDBJ
mRNA
AL020996
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471059
EMBL· GenBank· DDBJ
EAX07865.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471059
EMBL· GenBank· DDBJ
EAX07866.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471059
EMBL· GenBank· DDBJ
EAX07868.1
EMBL· GenBank· DDBJ
Genomic DNA
BC017175
EMBL· GenBank· DDBJ
AAH17175.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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