Q0D2I5 · IFFO1_HUMAN
- ProteinNon-homologous end joining factor IFFO1
- GeneIFFO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Nuclear matrix protein involved in the immobilization of broken DNA ends and the suppression of chromosome translocation during DNA double-strand breaks (DSBs) (PubMed:31548606).
Interacts with the nuclear lamina component LMNA, resulting in the formation of a nucleoskeleton that relocalizes to the DSB sites in a XRCC4-dependent manner and promotes the immobilization of the broken ends, thereby preventing chromosome translocation (PubMed:31548606).
Acts as a scaffold that allows the DNA repair protein XRCC4 and LMNA to assemble into a complex at the DSB sites (PubMed:31548606).
Interacts with the nuclear lamina component LMNA, resulting in the formation of a nucleoskeleton that relocalizes to the DSB sites in a XRCC4-dependent manner and promotes the immobilization of the broken ends, thereby preventing chromosome translocation (PubMed:31548606).
Acts as a scaffold that allows the DNA repair protein XRCC4 and LMNA to assemble into a complex at the DSB sites (PubMed:31548606).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | intermediate filament | |
Cellular Component | nuclear inner membrane | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleoplasm | |
Cellular Component | site of double-strand break | |
Biological Process | DNA double-strand break attachment to nuclear envelope | |
Biological Process | double-strand break repair via nonhomologous end joining | |
Biological Process | protein localization to site of double-strand break |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-homologous end joining factor IFFO1
- Short namesNHEJ factor IFFO1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ0D2I5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 65 | Does not affect the interaction with LMNA. | ||||
Sequence: A → P or V | ||||||
Mutagenesis | 73 | Decreased interaction with LMNA. Loss of ability to immobilize broken ends; when associated with H-85. | ||||
Sequence: N → D | ||||||
Mutagenesis | 73 | Does not affect the interaction with LMNA. | ||||
Sequence: N → K | ||||||
Mutagenesis | 85 | Decreased interaction with LMNA. | ||||
Sequence: R → H | ||||||
Mutagenesis | 89 | Does not affect the interaction with LMNA. | ||||
Sequence: A → T or V | ||||||
Mutagenesis | 480 | Loss of interaction with XRCC4; when associated with R-487. | ||||
Sequence: I → R | ||||||
Mutagenesis | 487 | Loss of interaction with XRCC4; when associated with R-480. | ||||
Sequence: A → R | ||||||
Mutagenesis | 490 | Decreased interaction with XRCC4; when associated with A-516. Loss of interaction with XRCC4; when associated with A-509 and A-516. | ||||
Sequence: D → A | ||||||
Mutagenesis | 509 | Loss of interaction with XRCC4; when associated with A-490 and A-516. | ||||
Sequence: D → A | ||||||
Mutagenesis | 512 | Loss of interaction with XRCC4. | ||||
Sequence: M → R | ||||||
Mutagenesis | 515 | Loss of interaction with XRCC4, loss of localization at the sites of DNA damages and loss of ability to immobilize broken ends. | ||||
Sequence: C → R | ||||||
Mutagenesis | 516 | Decreased interaction with XRCC4; when associated with A-490. Loss of interaction with XRCC4; when associated with A-490 and A-509. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 741 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 (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000316794 | 1-559 | UniProt | Non-homologous end joining factor IFFO1 | |||
Sequence: MNPLFGPNLFLLQQEQQGLAGPLGDSLGGDHFAGGGDLPPAPLSPAGPAAYSPPGPGPAPPAAMALRNDLGSNINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLGRRDQAVQTGFVSPIRPLGLQLGARPAAVCSPSARVLGSPARSPAGPLAPSAASLSSSSTSTSTTYSSSARFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAELVVFKGLMSNNLSELDTKIQEKAMKVDMDICRRIDITAKLCDVAQQRNCEDMIQMFQVPSMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEESTALSINEEMQRMLNQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRKSPAFTAVPLSDPPPPPSEAEDSDRDVSSDSSMR | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 531 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 548 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Forms a heterotetramer with XRCC4 (PubMed:31548606).
The interaction with XRCC4 is direct, involves LIG4-free XRCC4 and leads to relocalization of IFFO1 at the double-strand break (DSB) sites (PubMed:31548606).
Interacts with LMNA; the interaction forms an interior nucleoskeleton and the recruitment to DNA double-strand breaks (PubMed:31548606).
The interaction with XRCC4 is direct, involves LIG4-free XRCC4 and leads to relocalization of IFFO1 at the double-strand break (DSB) sites (PubMed:31548606).
Interacts with LMNA; the interaction forms an interior nucleoskeleton and the recruitment to DNA double-strand breaks (PubMed:31548606).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q0D2I5 | LMNA P02545-2 | 2 | EBI-742894, EBI-351953 | |
BINARY | Q0D2I5 | XRCC4 Q13426 | 7 | EBI-742894, EBI-717592 | |
BINARY | Q0D2I5-5 | LMNA P02545 | 4 | EBI-21251044, EBI-351935 | |
BINARY | Q0D2I5-5 | XRCC4 Q13426 | 4 | EBI-21251044, EBI-717592 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 21-57 | Disordered | ||||
Sequence: GPLGDSLGGDHFAGGGDLPPAPLSPAGPAAYSPPGPG | ||||||
Compositional bias | 41-57 | Pro residues | ||||
Sequence: APLSPAGPAAYSPPGPG | ||||||
Region | 65-116 | LMNA binding | ||||
Sequence: ALRNDLGSNINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGR | ||||||
Domain | 73-526 | IF rod | ||||
Sequence: NINVLKTLNLRFRCFLAKVHELERRNRLLEKQLQQALEEGKQGRRGLGRRDQAVQTGFVSPIRPLGLQLGARPAAVCSPSARVLGSPARSPAGPLAPSAASLSSSSTSTSTTYSSSARFMPGTIWSFSHARRLGPGLEPTLVQGPGLSWVHPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAELVVFKGLMSNNLSELDTKIQEKAMKVDMDICRRIDITAKLCDVAQQRNCEDMIQMFQVPSMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEESTALSINEEMQRMLNQLREYDFEDDCDSLTWEETEETLLLWEDFSGYAMAAAEAQGEQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDRK | ||||||
Coiled coil | 85-117 | |||||
Sequence: RCFLAKVHELERRNRLLEKQLQQALEEGKQGRR | ||||||
Region | 158-187 | Disordered | ||||
Sequence: SPARSPAGPLAPSAASLSSSSTSTSTTYSS | ||||||
Compositional bias | 169-187 | Polar residues | ||||
Sequence: PSAASLSSSSTSTSTTYSS | ||||||
Coiled coil | 237-301 | |||||
Sequence: EIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQDRVNELQEEAQEADACQEELALKVEQLKAEL | ||||||
Region | 360-394 | Disordered | ||||
Sequence: SMGGRKRERKAAVEEDTSLSESEGPRQPDGDEEES | ||||||
Compositional bias | 362-392 | Basic and acidic residues | ||||
Sequence: GGRKRERKAAVEEDTSLSESEGPRQPDGDEE | ||||||
Region | 450-525 | XCCR4 binding. Required for localization to the double-strand breaks (DSBs) | ||||
Sequence: EQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQSGDR | ||||||
Coiled coil | 455-501 | |||||
Sequence: LEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEM | ||||||
Region | 520-559 | Disordered | ||||
Sequence: TQSGDRKSPAFTAVPLSDPPPPPSEAEDSDRDVSSDSSMR | ||||||
Compositional bias | 543-559 | Basic and acidic residues | ||||
Sequence: SEAEDSDRDVSSDSSMR |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q0D2I5-1
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
- Length559
- Mass (Da)61,979
- Last updated2009-09-22 v2
- Checksum050FCFFB4953CBD8
Q0D2I5-2
- Name2
- Differences from canonical
- 1-360: Missing
Q0D2I5-3
- Name3
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Q0D2I5-4
- Name4
- Differences from canonical
- 357-357: Q → QKKL
Q0D2I5-5
- Name5
Q0D2I5-6
- Name6
Q0D2I5-7
- Name7
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PPX7 | E9PPX7_HUMAN | IFFO1 | 255 | ||
A0A087WZ16 | A0A087WZ16_HUMAN | IFFO1 | 571 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_030781 | 1-360 | in isoform 2 and isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 41-57 | Pro residues | ||||
Sequence: APLSPAGPAAYSPPGPG | ||||||
Sequence conflict | 152-153 | in Ref. 3; AF124432 | ||||
Sequence: SA → LE | ||||||
Compositional bias | 169-187 | Polar residues | ||||
Sequence: PSAASLSSSSTSTSTTYSS | ||||||
Alternative sequence | VSP_030782 | 259-264 | in isoform 3 | |||
Sequence: WEEEYT → CFYRVK | ||||||
Alternative sequence | VSP_030783 | 265-559 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 285 | in Ref. 3; AF124432 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_030784 | 357 | in isoform 4 and isoform 5 | |||
Sequence: Q → QKKL | ||||||
Alternative sequence | VSP_039709 | 357 | in isoform 7 | |||
Sequence: Q → QKL | ||||||
Sequence conflict | 358 | in Ref. 2; AAI10388 | ||||
Sequence: V → F | ||||||
Compositional bias | 362-392 | Basic and acidic residues | ||||
Sequence: GGRKRERKAAVEEDTSLSESEGPRQPDGDEE | ||||||
Sequence conflict | 387 | in Ref. 3; AF124432 | ||||
Sequence: P → A | ||||||
Alternative sequence | VSP_038240 | 451 | in isoform 5, isoform 6 and isoform 7 | |||
Sequence: Q → QQ | ||||||
Sequence conflict | 471 | in Ref. 3; AF124432 | ||||
Sequence: K → M | ||||||
Sequence conflict | 474 | in Ref. 3; AF124432 | ||||
Sequence: Q → H | ||||||
Compositional bias | 543-559 | Basic and acidic residues | ||||
Sequence: SEAEDSDRDVSSDSSMR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH471116 EMBL· GenBank· DDBJ | EAW88781.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88783.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002857 EMBL· GenBank· DDBJ | AAH02857.2 EMBL· GenBank· DDBJ | mRNA | ||
BC004384 EMBL· GenBank· DDBJ | AAH04384.2 EMBL· GenBank· DDBJ | mRNA | ||
BC010431 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC071170 EMBL· GenBank· DDBJ | AAH71170.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103817 EMBL· GenBank· DDBJ | AAI03818.1 EMBL· GenBank· DDBJ | mRNA | ||
BC103818 EMBL· GenBank· DDBJ | AAI03819.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110387 EMBL· GenBank· DDBJ | AAI10388.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113848 EMBL· GenBank· DDBJ | AAI13849.1 EMBL· GenBank· DDBJ | mRNA | ||
BC114454 EMBL· GenBank· DDBJ | AAI14455.1 EMBL· GenBank· DDBJ | mRNA | ||
AF124432 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |