Q9H9D4 · ZN408_HUMAN
- ProteinZinc finger protein 408
- GeneZNF408
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids720 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in transcriptional regulation.
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 | nucleus | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein 408
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H9D4
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Vitreoretinopathy, exudative 6 (EVR6)
- Note
- DescriptionA form of exudative vitreoretinopathy, a disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.
- See alsoMIM:616468
Natural variants in EVR6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_074612 | 126 | S>N | in EVR6; uncertain significance; does not affect localization to the nucleus; dbSNP:rs536561101 | |
VAR_074613 | 455 | H>Y | in EVR6; severely decreased localization to the nucleus; dbSNP:rs373273223 |
Retinitis pigmentosa 72 (RP72)
- Note
- DescriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
- See alsoMIM:616469
Natural variants in RP72
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_074615 | 541 | R>C | in RP72; decreased localization to the nucleus; dbSNP:rs781192528 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_074612 | 126 | in EVR6; uncertain significance; does not affect localization to the nucleus; dbSNP:rs536561101 | |||
Sequence: S → N | ||||||
Natural variant | VAR_052823 | 337 | in dbSNP:rs36017347 | |||
Sequence: R → P | ||||||
Natural variant | VAR_074613 | 455 | in EVR6; severely decreased localization to the nucleus; dbSNP:rs373273223 | |||
Sequence: H → Y | ||||||
Natural variant | VAR_074614 | 492 | in dbSNP:rs561740128 | |||
Sequence: G → R | ||||||
Natural variant | VAR_074615 | 541 | in RP72; decreased localization to the nucleus; dbSNP:rs781192528 | |||
Sequence: R → C | ||||||
Natural variant | VAR_074616 | 583 | ||||
Sequence: Q → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 908 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000047569 | 1-720 | UniProt | Zinc finger protein 408 | |||
Sequence: MEEAEELLLEGKKALQLAREPRLGLDLGWNPSGEGCTQGLKDVPPEPTRDILALKSLPRGLALGPSLAKEQRLGVWCVGDPLQPGLLWGPLEEESASKEKGEGVKPRQEENLSLGPWGDVCACEQSSGWTSLVQRGRLESEGNVAPVRISERLHLQVYQLVLPGSELLLWPQPSSEGPSLTQPGLDKEAAVAVVTEVESAVQQEVASPGEDAAEPCIDPGSQSPSGIQAENMVSPGLKFPTQDRISKDSQPLGPLLQDGDVDEECPAQAQMPPELQSNSATQQDPDGSGASFSSSARGTQPHGYLAKKLHSPSDQCPPRAKTPEPGAQQSGFPTLSRSPPGPAGSSPKQGRRYRCGECGKAFLQLCHLKKHAFVHTGHKPFLCTECGKSYSSEESFKAHMLGHRGVRPFPCPQCDKAYGTQRDLKEHQVVHSGARPFACDQCGKAFARRPSLRLHRKTHQVPAAPAPCPCPVCGRPLANQGSLRNHMRLHTGEKPFLCPHCGRAFRQRGNLRGHLRLHTGERPYRCPHCADAFPQLPELRRHLISHTGEAHLCPVCGKALRDPHTLRAHERLHSGERPFPCPQCGRAYTLATKLRRHLKSHLEDKPYRCPTCGMGYTLPQSLRRHQLSHRPEAPCSPPSVPSAASEPTVVLLQAEPQLLDTHREEEVSPARDVVEVTISESQEKCFVVPEEPDAAPSLVLIHKDMGLGAWAEVVEVEMGT | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 322 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest expression is observed in adult retina; abundantly expressed in the fetal eye (PubMed:23716654).
In the retina, it is detected in the outer nuclear layer, especially cone and rod photoreceptor cells, ganglion cell layer and both outer and inner plexiform layers (at protein level) (PubMed:25882705).
Expressed in retinal blood vessels (at protein level) (PubMed:25882705).
In the retina, it is detected in the outer nuclear layer, especially cone and rod photoreceptor cells, ganglion cell layer and both outer and inner plexiform layers (at protein level) (PubMed:25882705).
Expressed in retinal blood vessels (at protein level) (PubMed:25882705).
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 201-350 | Disordered | ||||
Sequence: VQQEVASPGEDAAEPCIDPGSQSPSGIQAENMVSPGLKFPTQDRISKDSQPLGPLLQDGDVDEECPAQAQMPPELQSNSATQQDPDGSGASFSSSARGTQPHGYLAKKLHSPSDQCPPRAKTPEPGAQQSGFPTLSRSPPGPAGSSPKQG | ||||||
Compositional bias | 271-300 | Polar residues | ||||
Sequence: MPPELQSNSATQQDPDGSGASFSSSARGTQ | ||||||
Compositional bias | 327-343 | Polar residues | ||||
Sequence: AQQSGFPTLSRSPPGPA | ||||||
Zinc finger | 353-375 | C2H2-type 1 | ||||
Sequence: YRCGECGKAFLQLCHLKKHAFVH | ||||||
Zinc finger | 381-403 | C2H2-type 2 | ||||
Sequence: FLCTECGKSYSSEESFKAHMLGH | ||||||
Zinc finger | 409-431 | C2H2-type 3 | ||||
Sequence: FPCPQCDKAYGTQRDLKEHQVVH | ||||||
Zinc finger | 437-459 | C2H2-type 4 | ||||
Sequence: FACDQCGKAFARRPSLRLHRKTH | ||||||
Zinc finger | 468-490 | C2H2-type 5 | ||||
Sequence: CPCPVCGRPLANQGSLRNHMRLH | ||||||
Zinc finger | 496-518 | C2H2-type 6 | ||||
Sequence: FLCPHCGRAFRQRGNLRGHLRLH | ||||||
Zinc finger | 524-546 | C2H2-type 7 | ||||
Sequence: YRCPHCADAFPQLPELRRHLISH | ||||||
Zinc finger | 551-573 | C2H2-type 8 | ||||
Sequence: HLCPVCGKALRDPHTLRAHERLH | ||||||
Zinc finger | 579-601 | C2H2-type 9 | ||||
Sequence: FPCPQCGRAYTLATKLRRHLKSH | ||||||
Zinc finger | 607-629 | C2H2-type 10 | ||||
Sequence: YRCPTCGMGYTLPQSLRRHQLSH |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length720
- Mass (Da)78,439
- Last updated2001-03-01 v1
- Checksum0D3CDA7572D17721
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 271-300 | Polar residues | ||||
Sequence: MPPELQSNSATQQDPDGSGASFSSSARGTQ | ||||||
Compositional bias | 327-343 | Polar residues | ||||
Sequence: AQQSGFPTLSRSPPGPA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF346626 EMBL· GenBank· DDBJ | AAK29075.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022889 EMBL· GenBank· DDBJ | BAB14295.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013355 EMBL· GenBank· DDBJ | AAH13355.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015708 EMBL· GenBank· DDBJ | AAH15708.1 EMBL· GenBank· DDBJ | mRNA |