O95831 · AIFM1_HUMAN
- ProteinApoptosis-inducing factor 1, mitochondrial
- GeneAIFM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids613 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed:20362274).
Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity).
The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:20362274).
Binds to DNA in a sequence-independent manner (PubMed:27178839).
Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969).
Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225).
In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228).
Isoform 4
Isoform 5
Catalytic activity
- A + H+ + NADH = AH2 + NAD+
Isoform 4
A + H+ + NADH = AH2 + NAD+
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.53 mM | NADH | |||||
26 μM | cytochrome c | 7.4 | 25 | |||
138 μM | dichlorophenolindophenol | 7.4 | 25 | |||
0.51 mM | NADH | 7.4 | 25 | |||
896 μM | NADPH |
kcat is 1.5 sec-1 for dichlorophenolindophenol reduction, 3.1 sec-1 for ferricyanide and 0.6 sec-1 for cytochrome c reduction (PubMed:24914854).
Isoform 4
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
102.6 μM | NADH | |||||
45.3 μM | NADPH |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 138-142 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GGGTA | ||||||
Binding site | 164-165 | FAD (UniProtKB | ChEBI) | ||||
Sequence: ED | ||||||
Binding site | 172 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 177 | FAD (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 196 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 233 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 285 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 308-311 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: GGFL | ||||||
Binding site | 336 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 342 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 399 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 438 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 453-454 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: EH | ||||||
Binding site | 454-455 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HH | ||||||
Binding site | 483 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 483 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 493 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 583 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameApoptosis-inducing factor 1, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95831
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity).
Translocation into the nucleus is promoted by interaction with (auto-poly-ADP-ribosylated) processed form of PARP1 (PubMed:33168626).
Colocalizes with EIF3G in the nucleus and perinuclear region (PubMed:17094969).
Isoform 3
Isoform 4
Isoform 5
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Combined oxidative phosphorylation deficiency 6 (COXPD6)
- Note
- DescriptionA mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy.
- See alsoMIM:300816
Natural variants in COXPD6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063827 | 201 | missing | in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death; dbSNP:rs387906500 | |
VAR_072791 | 243 | V>L | in COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding; dbSNP:rs1603225138 | |
VAR_067334 | 308 | G>E | in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE; dbSNP:rs1603224226 | |
VAR_083068 | 338 | G>E | in COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; dbSNP:rs1603223152 |
Charcot-Marie-Tooth disease, X-linked recessive, 4, with or without cerebellar ataxia (CMTX4)
- Note
- DescriptionA neuromuscular disorder characterized by progressive sensorimotor axonal neuropathy, distal sensory impairment, difficulty walking due to peripheral neuropathy and/or cerebellar ataxia, and deafness due to auditory neuropathy. Additional features include cognitive impairment, cerebellar atrophy, dysarthria, abnormal extraocular movements, tremor, dysmetria and spasticity. The age at onset ranges from infancy to young adulthood.
- See alsoMIM:310490
Natural variants in CMTX4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069468 | 493 | E>V | in CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4; dbSNP:rs281864468 |
Deafness, X-linked, 5, with peripheral neuropathy (DFNX5)
- Note
- DescriptionA form of hearing loss characterized by absent or severely abnormal auditory brainstem response, abnormal middle ear reflexes, abnormal speech discrimination, loss of outer hair cell function, and cochlear nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with childhood onset, associated with distal sensory impairment affecting the peripheral nervous system.
- See alsoMIM:300614
Natural variants in DFNX5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_076211 | 260 | T>A | in DFNX5; dbSNP:rs863225432 | |
VAR_076212 | 344 | L>F | in DFNX5; uncertain significance; dbSNP:rs184474885 | |
VAR_076213 | 360 | G>R | in DFNX5; uncertain significance; dbSNP:rs724160026 | |
VAR_076214 | 422 | R>Q | in DFNX5; dbSNP:rs724160021 | |
VAR_076215 | 422 | R>W | in DFNX5; dbSNP:rs724160020 | |
VAR_076216 | 430 | R>C | in DFNX5; uncertain significance; dbSNP:rs1223488720 | |
VAR_076217 | 451 | R>Q | in DFNX5; dbSNP:rs863225431 | |
VAR_076218 | 472 | A>V | in DFNX5; uncertain significance; dbSNP:rs2124648387 | |
VAR_076219 | 475 | P>L | in DFNX5; uncertain significance; dbSNP:rs724160022 | |
VAR_076220 | 498 | V>M | in DFNX5; uncertain significance; dbSNP:rs724160023 | |
VAR_076221 | 591 | I>M | in DFNX5; uncertain significance |
Spondyloepimetaphyseal dysplasia, X-linked, with hypomyelinating leukodystrophy (SEMDHL)
- Note
- DescriptionAn X-linked recessive developmental disorder characterized by slowly progressive skeletal and neurologic abnormalities, including short stature, large and deformed joints, significant motor impairment, visual defects, and sometimes cognitive deficits. Affected individuals typically have normal early development in the first year or so of life, followed by development regression and the development of symptoms. Brain imaging shows white matter abnormalities consistent with hypomyelinating leukodystrophy.
- See alsoMIM:300232
Natural variants in SEMDHL
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083739 | 235 | Q>H | in SEMDHL; severe decrease of protein expression; dbSNP:rs377527583 | |
VAR_083740 | 237 | D>G | in SEMDHL; dbSNP:rs1202786652 | |
VAR_083741 | 237 | D>V | in SEMDHL; dbSNP:rs1202786652 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 196 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: W → A | ||||||
Natural variant | VAR_063827 | 201 | in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death; dbSNP:rs387906500 | |||
Sequence: Missing | ||||||
Natural variant | VAR_083739 | 235 | in SEMDHL; severe decrease of protein expression; dbSNP:rs377527583 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_083740 | 237 | in SEMDHL; dbSNP:rs1202786652 | |||
Sequence: D → G | ||||||
Natural variant | VAR_083741 | 237 | in SEMDHL; dbSNP:rs1202786652 | |||
Sequence: D → V | ||||||
Natural variant | VAR_072791 | 243 | in COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding; dbSNP:rs1603225138 | |||
Sequence: V → L | ||||||
Natural variant | VAR_076211 | 260 | in DFNX5; dbSNP:rs863225432 | |||
Sequence: T → A | ||||||
Natural variant | VAR_083067 | 262 | found in patient with mitochondrial encephalomyopathy with moderate clinical severity and slow progressive course despite early onset as well as and cerebellar involvement; likely pathogenic; decreased protein level; strongly decreased redox potential; strongly decreased NADH oxidase activity; no effect on DNA-binding; dbSNP:rs1603224817 | |||
Sequence: G → S | ||||||
Natural variant | VAR_067334 | 308 | in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE; dbSNP:rs1603224226 | |||
Sequence: G → E | ||||||
Natural variant | VAR_083068 | 338 | in COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; dbSNP:rs1603223152 | |||
Sequence: G → E | ||||||
Natural variant | VAR_076212 | 344 | in DFNX5; uncertain significance; dbSNP:rs184474885 | |||
Sequence: L → F | ||||||
Natural variant | VAR_076213 | 360 | in DFNX5; uncertain significance; dbSNP:rs724160026 | |||
Sequence: G → R | ||||||
Mutagenesis | 413-430 | Disrupts dimerization. Lower efficiency in stabilizing charge-transfer complexes upon coenzyme reduction. | ||||
Sequence: EIDSDFGGFRVNAELQAR → AIDSDFGGFAVNAELQAA | ||||||
Natural variant | VAR_076214 | 422 | in DFNX5; dbSNP:rs724160021 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_076215 | 422 | in DFNX5; dbSNP:rs724160020 | |||
Sequence: R → W | ||||||
Natural variant | VAR_076216 | 430 | in DFNX5; uncertain significance; dbSNP:rs1223488720 | |||
Sequence: R → C | ||||||
Mutagenesis | 443-445 | Disrupts dimerization. Disrupts dimerization; when associated with A-477. | ||||
Sequence: YDI → ADA | ||||||
Natural variant | VAR_076217 | 451 | in DFNX5; dbSNP:rs863225431 | |||
Sequence: R → Q | ||||||
Mutagenesis | 454 | Allows dimerization in absence of NADH. | ||||
Sequence: H → A | ||||||
Natural variant | VAR_076218 | 472 | in DFNX5; uncertain significance; dbSNP:rs2124648387 | |||
Sequence: A → V | ||||||
Natural variant | VAR_076219 | 475 | in DFNX5; uncertain significance; dbSNP:rs724160022 | |||
Sequence: P → L | ||||||
Mutagenesis | 477 | Disrupts dimerization; when associated with A-443--445-A. | ||||
Sequence: W → A | ||||||
Mutagenesis | 480 | Allows dimerization in absence of NADH. | ||||
Sequence: S → A | ||||||
Mutagenesis | 485 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_069468 | 493 | in CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4; dbSNP:rs281864468 | |||
Sequence: E → V | ||||||
Natural variant | VAR_076220 | 498 | in DFNX5; uncertain significance; dbSNP:rs724160023 | |||
Sequence: V → M | ||||||
Mutagenesis | 529 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: R → A | ||||||
Mutagenesis | 531 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: E → A | ||||||
Mutagenesis | 533 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: E → A | ||||||
Mutagenesis | 535 | Increases protein dimerization at lower NADH levels. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_076221 | 591 | in DFNX5; uncertain significance | |||
Sequence: I → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 445 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, propeptide, modified residue (large scale data), chain, modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-54 | UniProt | Mitochondrion | ||||
Sequence: MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQM | |||||||
Propeptide | PRO_0000401935 | 55-101 | UniProt | Removed in mature form | |||
Sequence: ASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISG | |||||||
Modified residue (large scale data) | 100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000022030 | 102-613 | UniProt | Apoptosis-inducing factor 1, mitochondrial | |||
Sequence: LGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED | |||||||
Modified residue | 105 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 109 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue | 116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 255 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 268 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 268 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 292 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 371 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 388 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 521 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 524 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 530 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 593 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Detected in muscle and skin fibroblasts (at protein level) (PubMed:23217327).
Expressed in osteoblasts (at protein level) (PubMed:28842795).
Isoform 3
Isoform 4
Isoform 5
Induction
Isoform 5
Gene expression databases
Organism-specific databases
Interaction
Subunit
Also dimerizes with isoform 3 preventing its release from mitochondria (PubMed:20111043).
Interacts with XIAP/BIRC4 (PubMed:17967870).
Interacts (via N-terminus) with EIF3G (via C-terminus) (PubMed:17094969).
Interacts with PRELID1 (PubMed:21364629).
Interacts with CHCHD4; the interaction increases in presence of NADH (PubMed:26004228).
Interacts with processed form of PARP1 (Poly [ADP-ribose] polymerase 1, processed C-terminus); interaction is mediated with poly-ADP-ribose chains attached to PARP1, promoting translocation into the nucleus (PubMed:33168626).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95831 | EIF3G O75821 | 9 | EBI-356440, EBI-366632 | |
BINARY | O95831 | KANK2 Q63ZY3 | 3 | EBI-356440, EBI-2556193 | |
BINARY | O95831 | KANK2 Q63ZY3-2 | 4 | EBI-356440, EBI-6244894 | |
XENO | O95831 | PA Q5EP34 | 8 | EBI-356440, EBI-25772799 | |
BINARY | O95831 | TSC22D4 Q9Y3Q8 | 2 | EBI-356440, EBI-739485 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 1-31 | Mitochondrial localization signal | ||||
Sequence: MFRCGGLAAGALKQKLVPLVRTVCVRSPRQR | ||||||
Motif | 63-89 | Mitochondrial localization signal | ||||
Sequence: KIDNSVLVLIVGLSTVGAGAYAYKTMK | ||||||
Region | 100-127 | Disordered | ||||
Sequence: SGLGLTPEQKQKKAALSASEGEEVPQDK | ||||||
Region | 134-483 | FAD-dependent oxidoreductase | ||||
Sequence: FLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFW | ||||||
Motif | 446-451 | Nuclear localization signal | ||||
Sequence: KLGRRR | ||||||
Region | 513-554 | Disordered | ||||
Sequence: AQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAP | ||||||
Compositional bias | 514-546 | Polar residues | ||||
Sequence: QDNPKSATEQSGTGIRSESETESEASEITIPPS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 6 isoforms produced by Alternative splicing.
O95831-1
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
- SynonymsAIF
- Length613
- Mass (Da)66,901
- Last updated1999-05-01 v1
- ChecksumA156762BC64E6340
O95831-2
- Name2
- Differences from canonical
- 36-322: Missing
O95831-3
- Name3
- SynonymsAIF-exB, AIF2
- Differences from canonical
- 36-82: GNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGA → VVQSHHLGSPSRSLASTGASGKDGSNLVYFLIVGATVTGAGVY
O95831-4
- Name4
- SynonymsAIFsh2
O95831-5
- Name5
- SynonymsAIFsh
- Differences from canonical
- 1-352: Missing
O95831-6
- Name6
- SynonymsAIFsh3
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 17 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q8PFM5 | A0A6Q8PFM5_HUMAN | AIFM1 | 612 | ||
A0A6Q8PFE1 | A0A6Q8PFE1_HUMAN | AIFM1 | 622 | ||
A0A6Q8PFA7 | A0A6Q8PFA7_HUMAN | AIFM1 | 460 | ||
A0A7I2RLJ8 | A0A7I2RLJ8_HUMAN | AIFM1 | 441 | ||
A0A6Q8PFS4 | A0A6Q8PFS4_HUMAN | AIFM1 | 589 | ||
A0A6Q8PFW2 | A0A6Q8PFW2_HUMAN | AIFM1 | 293 | ||
A0A6Q8PFN1 | A0A6Q8PFN1_HUMAN | AIFM1 | 61 | ||
A0A6Q8PFQ8 | A0A6Q8PFQ8_HUMAN | AIFM1 | 565 | ||
A0A6Q8PG15 | A0A6Q8PG15_HUMAN | AIFM1 | 612 | ||
A0A6Q8PGB7 | A0A6Q8PGB7_HUMAN | AIFM1 | 98 | ||
A0A6Q8PF87 | A0A6Q8PF87_HUMAN | AIFM1 | 248 | ||
A0A6Q8PHJ4 | A0A6Q8PHJ4_HUMAN | AIFM1 | 229 | ||
A0A6Q8PHJ9 | A0A6Q8PHJ9_HUMAN | AIFM1 | 611 | ||
A0A6Q8PHC0 | A0A6Q8PHC0_HUMAN | AIFM1 | 609 | ||
E9PMA0 | E9PMA0_HUMAN | AIFM1 | 274 | ||
E9PMQ8 | E9PMQ8_HUMAN | AIFM1 | 89 | ||
A0A7I2PK44 | A0A7I2PK44_HUMAN | AIFM1 | 611 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046248 | 1-352 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022953 | 36-82 | in isoform 3 | |||
Sequence: GNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGA → VVQSHHLGSPSRSLASTGASGKDGSNLVYFLIVGATVTGAGVY | ||||||
Alternative sequence | VSP_004357 | 36-322 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060785 | 37-43 | in isoform 6 | |||
Sequence: NLFQRWH → LQDYERG | ||||||
Alternative sequence | VSP_060786 | 44-613 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043637 | 323-324 | in isoform 4 | |||
Sequence: AR → DI | ||||||
Alternative sequence | VSP_043638 | 325-613 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 514-546 | Polar residues | ||||
Sequence: QDNPKSATEQSGTGIRSESETESEASEITIPPS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF100928 EMBL· GenBank· DDBJ | AAD16436.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ016496 EMBL· GenBank· DDBJ | AAY84737.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ016498 EMBL· GenBank· DDBJ | AAY84739.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ016500 EMBL· GenBank· DDBJ | AAY84741.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AL049703 EMBL· GenBank· DDBJ | CAB41267.1 EMBL· GenBank· DDBJ | mRNA | ||
AL049704 EMBL· GenBank· DDBJ | CAB41268.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314446 EMBL· GenBank· DDBJ | BAG37055.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457379 EMBL· GenBank· DDBJ | CAG33660.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139234 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF459397 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF510638 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471107 EMBL· GenBank· DDBJ | EAX11811.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471107 EMBL· GenBank· DDBJ | EAX11812.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471107 EMBL· GenBank· DDBJ | EAX11810.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC111065 EMBL· GenBank· DDBJ | AAI11066.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139738 EMBL· GenBank· DDBJ | AAI39739.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131759 EMBL· GenBank· DDBJ | AAD20036.1 EMBL· GenBank· DDBJ | mRNA |