Q9H019 · MFR1L_HUMAN
- ProteinMitochondrial fission regulator 1-like
- GeneMTFR1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids292 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Biological Process | aerobic respiration | |
Biological Process | mitochondrial fission |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial fission regulator 1-like
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H019
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_044084 | 58 | in dbSNP:rs35448678 | |||
Sequence: P → S | ||||||
Mutagenesis | 103 | Loss of phosphorylation by AMPK. No effect on mitochondrial morphology; when associated with A-238. | ||||
Sequence: S → A | ||||||
Mutagenesis | 103 | Leads to fragmentation of mitochondrial network; when associated with D-238. | ||||
Sequence: S → D | ||||||
Mutagenesis | 238 | Loss of phosphorylation by AMPK. No effect on mitochondrial morphology; when associated with A-103. | ||||
Sequence: S → A | ||||||
Mutagenesis | 238 | Leads to fragmentation of mitochondrial network; when associated with D-103. | ||||
Sequence: S → D |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000341566 | 1-292 | UniProt | Mitochondrial fission regulator 1-like | |||
Sequence: MSGMEATVTIPIWQNKPHGAARSVVRRIGTNLPLKPCARASFETLPNISDLCLRDVPPVPTLADIAWIAADEEETYARVRSDTRPLRHTWKPSPLIVMQRNASVPNLRGSEERLLALKKPALPALSRTTELQDELSHLRSQIAKIVAADAASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLLCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN | |||||||
Modified residue | 30 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 103 | UniProt | Phosphoserine; by AMPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 224 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 225 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 238 | UniProt | Phosphoserine; by AMPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 261 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 273 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by AMPK. Upon stress, phosphorylation at Ser-103 and Ser-238 by AMPK is sufficient to induce mitochondrial fragmentation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H019 | AIRIM Q9NX04 | 3 | EBI-2824497, EBI-8643161 | |
BINARY | Q9H019 | ANKRD11 X5D778 | 3 | EBI-2824497, EBI-17183751 | |
BINARY | Q9H019 | ARMC1 Q9NVT9 | 7 | EBI-2824497, EBI-3506974 | |
BINARY | Q9H019 | CNOT2 Q9NZN8 | 3 | EBI-2824497, EBI-743033 | |
BINARY | Q9H019 | EFHC1 Q5JVL4 | 3 | EBI-2824497, EBI-743105 | |
BINARY | Q9H019 | MAGEA12 P43365 | 6 | EBI-2824497, EBI-749530 | |
BINARY | Q9H019 | ZNF76 P36508 | 3 | EBI-2824497, EBI-7254550 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length292
- Mass (Da)31,957
- Last updated2008-06-10 v2
- Checksum39B23825CA1638EF
Q9H019-2
- Name2
- Differences from canonical
- 151-292: ASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLLCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN → VTSPRRQRWRSLSFHQSPCFVLPALNVANQNTKLPAVRLKRMTASLCPRPAALQT
Q9H019-3
- Name3
- Differences from canonical
- 151-162: Missing
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JF50 | C9JF50_HUMAN | MTFR1L | 152 | ||
E9PRK5 | E9PRK5_HUMAN | MTFR1L | 182 | ||
E9PRW1 | E9PRW1_HUMAN | MTFR1L | 110 | ||
E9PSD6 | E9PSD6_HUMAN | MTFR1L | 115 | ||
E9PPF9 | E9PPF9_HUMAN | MTFR1L | 160 | ||
E9PPQ0 | E9PPQ0_HUMAN | MTFR1L | 53 | ||
E9PNJ0 | E9PNJ0_HUMAN | MTFR1L | 13 | ||
E9PLD2 | E9PLD2_HUMAN | MTFR1L | 195 | ||
E9PLU1 | E9PLU1_HUMAN | MTFR1L | 170 | ||
E9PJP7 | E9PJP7_HUMAN | MTFR1L | 73 | ||
E9PIF9 | E9PIF9_HUMAN | MTFR1L | 52 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 87 | in Ref. 4; CAC21683 | ||||
Sequence: R → W | ||||||
Sequence conflict | 136 | in Ref. 4; CAC21683 | ||||
Sequence: S → G | ||||||
Alternative sequence | VSP_034339 | 151-162 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_034338 | 151-292 | in isoform 2 | |||
Sequence: ASASLTPDFLSPGSSNVSSPLPCFGSSFHSTTSFVISDITEETEVEVPELPSVPLLCSASPECCKPEHKAACSSSEEDDCVSLSKASSFADMMGILKDFHRMKQSQDLNRSLLKEEDPAVLISEVLRRKFALKEEDISRKGN → VTSPRRQRWRSLSFHQSPCFVLPALNVANQNTKLPAVRLKRMTASLCPRPAALQT | ||||||
Sequence conflict | 273 | in Ref. 4; CAC21683 | ||||
Sequence: S → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |