P04733 · MT1F_HUMAN
- ProteinMetallothionein-1F
- GeneMT1F
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 5 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 7 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 7 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 13 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 15 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 15 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 19 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 21 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 24 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 24 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 26 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 29 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 33 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 34 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 34 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 36 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 37 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 37 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 41 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 44 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 44 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 48 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 50 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 50 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 57 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 59 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 60 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 60 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to cadmium ion | |
Biological Process | cellular response to copper ion | |
Biological Process | cellular response to zinc ion | |
Biological Process | detoxification of copper ion | |
Biological Process | intracellular zinc ion homeostasis | |
Biological Process | negative regulation of growth |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetallothionein-1F
- Short namesMT-1F
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP04733
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 79 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000197237 | 1-61 | Metallothionein-1F | |||
Sequence: MDPNCSCAAGVSCTCAGSCKCKECKCTSCKKSCCSCCPVGCSKCAQGCVCKGASEKCSCCD | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P04733 | NOP2 P46087 | 3 | EBI-10209483, EBI-356811 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Beta | ||||
Sequence: MDPNCSCAAGVSCTCAGSCKCKECKCTSC | ||||||
Region | 30-61 | Alpha | ||||
Sequence: KKSCCSCCPVGCSKCAQGCVCKGASEKCSCCD |
Domain
Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines.
Sequence similarities
Belongs to the metallothionein superfamily. Type 1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length61
- Mass (Da)6,086
- Last updated1987-08-13 v1
- Checksum7C7A61E180D8D1C8
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BRY8 | H3BRY8_HUMAN | MT1F | 44 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M10943 EMBL· GenBank· DDBJ | AAA59588.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M13003 EMBL· GenBank· DDBJ | AAA36213.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF078844 EMBL· GenBank· DDBJ | AAF23355.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC029453 EMBL· GenBank· DDBJ | AAH29453.1 EMBL· GenBank· DDBJ | mRNA |