Q99611 · SPS2_HUMAN
- ProteinSelenide, water dikinase 2
- GeneSEPHS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids448 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Synthesizes selenophosphate from selenide and ATP.
Catalytic activity
- ATP + H2O + hydrogenselenide = AMP + 2 H+ + phosphate + selenophosphate
Cofactor
Note: Binds 1 Mg2+ ion per monomer.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 60 | |||||
Sequence: U | ||||||
Binding site | 63 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Site | 63 | Important for catalytic activity | ||||
Sequence: K | ||||||
Binding site | 118-120 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: GMD | ||||||
Binding site | 120 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 138 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: D | ||||||
Binding site | 161 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: D | ||||||
Binding site | 161 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 212-215 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: GGQT | ||||||
Binding site | 316 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | selenide, water dikinase activity | |
Biological Process | selenium compound metabolic process | |
Biological Process | selenocysteine biosynthetic process | |
Biological Process | selenocysteine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSelenide, water dikinase 2
- 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 accessionQ99611
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052345 | 269 | in dbSNP:rs1804600 | |||
Sequence: P → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 470 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000127650 | 2-448 | UniProt | Selenide, water dikinase 2 | |||
Sequence: AEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGUGCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMDSCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVSQSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPDSAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNRTAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRFGLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKPRVIEVLPRGATAAVLAPDSSNASSEPSS | |||||||
Modified residue | 46 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Truncated SEPHS2 proteins produced by failed UGA/Sec decoding are ubiquitinated by the CRL2(KLHDC3) complex, which recognizes the glycine (Gly) at the C-terminus of truncated SEPHS2 proteins.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99611 | SEPHS1 P49903 | 2 | EBI-3937791, EBI-714091 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 84-107 | Disordered | ||||
Sequence: PLGRGLVGGQEEASQEAGLPAGAG |
Sequence similarities
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length448
- Mass (Da)47,305
- Last updated2008-02-26 v3
- Checksum309520C0CAE770F7
Features
Showing features for non-standard residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-standard residue | 60 | Selenocysteine | ||||
Sequence: U |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U43286 EMBL· GenBank· DDBJ | AAC50958.2 EMBL· GenBank· DDBJ | mRNA | ||
AC116348 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002381 EMBL· GenBank· DDBJ | AAH02381.3 EMBL· GenBank· DDBJ | mRNA | ||
BC016643 EMBL· GenBank· DDBJ | AAH16643.1 EMBL· GenBank· DDBJ | mRNA |