P49903 · SPS1_HUMAN
- ProteinSelenide, water dikinase 1
- GeneSEPHS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids392 (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.
Activity regulation
Activated by phosphate ions and by potassium ions.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 31 | |||||
Sequence: C | ||||||
Binding site | 32 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Site | 32 | Important for catalytic activity | ||||
Sequence: K | ||||||
Binding site | 67-69 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: GMD | ||||||
Binding site | 69 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: D | ||||||
Binding site | 110 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: D | ||||||
Binding site | 110 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 161-164 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: GGQT | ||||||
Binding site | 265 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | selenide, water dikinase activity | |
Biological Process | protein modification process | |
Biological Process | selenocysteine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSelenide, water dikinase 1
- 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 accessionP49903
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Cell membrane ; Peripheral membrane protein
Nucleus membrane ; Peripheral membrane protein
Isoform 2
Isoform 3
Isoform 4
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 85 | Strongly reduced ADP hydrolysis. | ||||
Sequence: T → A | ||||||
Mutagenesis | 268 | No change in ATP-binding. | ||||
Sequence: G → C | ||||||
Mutagenesis | 270 | No change in ATP-binding. | ||||
Sequence: G → R | ||||||
Mutagenesis | 273 | Loss of ATP-binding. | ||||
Sequence: G → A, D, or V | ||||||
Mutagenesis | 274 | Reduced ATP-binding. | ||||
Sequence: H → N | ||||||
Mutagenesis | 274 | Increased ATP-binding. | ||||
Sequence: H → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 271 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, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000127648 | 2-392 | UniProt | Selenide, water dikinase 1 | |||
Sequence: STRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1
Gradually expressed during the cell cycle until G2/M phase and then decreases.
Isoform 2
Gradually expressed during the cell cycle until G2/M phase and then decreases.
Isoform 3
Gradually expressed during the cell cycle until S phase and then decreases.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Isoform 1
Isoform 2
Isoform 3
Isoform 4
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P49903 | PLAGL2 Q9UPG8 | 3 | EBI-714091, EBI-2876622 | |
BINARY | P49903 | QRICH1 Q2TAL8 | 9 | EBI-714091, EBI-2798044 | |
BINARY | P49903 | SEPHS1 P49903 | 6 | EBI-714091, EBI-714091 | |
BINARY | P49903 | SEPHS2 Q99611 | 2 | EBI-714091, EBI-3937791 | |
BINARY | P49903 | XAF1 Q6GPH4 | 3 | EBI-714091, EBI-2815120 | |
BINARY | P49903 | ZBTB25 P24278 | 7 | EBI-714091, EBI-739899 | |
BINARY | P49903 | ZNF202 O95125 | 5 | EBI-714091, EBI-751960 | |
BINARY | P49903 | ZNF276 Q8N554 | 3 | EBI-714091, EBI-750821 | |
BINARY | P49903 | ZNF474 Q6S9Z5 | 3 | EBI-714091, EBI-17269964 | |
BINARY | P49903 | ZNF526 Q8TF50 | 3 | EBI-714091, EBI-11035148 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
P49903-1
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
- SynonymsMajor type, MT
- Length392
- Mass (Da)42,911
- Last updated2002-12-13 v2
- ChecksumE9636E38146D926D
P49903-2
- Name2
- SynonymsDelta E8
- Differences from canonical
- 251-321: Missing
P49903-3
- Name3
- SynonymsDelta E2
- Differences from canonical
- 1-67: Missing
P49903-4
- Name4
- SynonymsE9, E9a
- Differences from canonical
- 322-392: GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS → DVQ
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046701 | 1-67 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046702 | 251-321 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 260 | in Ref. 1; AAA87567 | ||||
Sequence: A → T | ||||||
Alternative sequence | VSP_047451 | 322-392 | in isoform 4 | |||
Sequence: GGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS → DVQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U34044 EMBL· GenBank· DDBJ | AAA87567.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
GU954545 EMBL· GenBank· DDBJ | ADF78120.1 EMBL· GenBank· DDBJ | mRNA | ||
GU954546 EMBL· GenBank· DDBJ | ADF78121.1 EMBL· GenBank· DDBJ | mRNA | ||
GU954547 EMBL· GenBank· DDBJ | ADF78122.1 EMBL· GenBank· DDBJ | mRNA | ||
GU954548 EMBL· GenBank· DDBJ | ADF78123.1 EMBL· GenBank· DDBJ | mRNA | ||
GU954549 EMBL· GenBank· DDBJ | ADF78124.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301568 EMBL· GenBank· DDBJ | BAG63062.1 EMBL· GenBank· DDBJ | mRNA | ||
AL138764 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL355870 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471072 EMBL· GenBank· DDBJ | EAW86289.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471072 EMBL· GenBank· DDBJ | EAW86290.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471072 EMBL· GenBank· DDBJ | EAW86291.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471072 EMBL· GenBank· DDBJ | EAW86292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471072 EMBL· GenBank· DDBJ | EAW86293.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000941 EMBL· GenBank· DDBJ | AAH00941.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063816 EMBL· GenBank· DDBJ | AAH63816.1 EMBL· GenBank· DDBJ | mRNA |