Q9NTK5 · OLA1_HUMAN
- ProteinObg-like ATPase 1
- GeneOLA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | nucleolus | |
Cellular Component | platelet alpha granule lumen | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | cadherin binding | |
Molecular Function | GTP binding | |
Molecular Function | metal ion binding | |
Molecular Function | ribosomal large subunit binding | |
Biological Process | ATP metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameObg-like ATPase 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NTK5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 127 | Loss of ATP-binding. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_036613 | 168 | in a breast cancer sample; somatic mutation | |||
Sequence: E → Q | ||||||
Mutagenesis | 230 | Loss of ATP-binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 231-233 | Retention of ATP-binding specificity. | ||||
Sequence: LSE → KSD |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 342 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 chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122456 | 1-396 | Obg-like ATPase 1 | |||
Sequence: MPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYLEANMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKEEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTPQQPKKK | ||||||
Modified residue | 294 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested but its expression is more abundant in testis, liver, lung, and brain. Overexpressed in several malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.
Induction
Strongly down-regulated by DNA damage-inducing agents.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9NTK5 | gag PRO_0000038593 P04591 | 4 | EBI-766468, EBI-6179719 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-283 | OBG-type G | ||||
Sequence: LKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYL | ||||||
Motif | 267-274 | Nuclear export signal | ||||
Sequence: LELKLQEL | ||||||
Domain | 304-387 | TGS | ||||
Sequence: QLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKEEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKF |
Sequence similarities
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NTK5-1
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
- Length396
- Mass (Da)44,744
- Last updated2002-11-25 v2
- Checksum4C7629BFC27CBEB2
Q9NTK5-2
- Name2
- Differences from canonical
- 1-158: Missing
Q9NTK5-3
- Name3
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002049 | 1-158 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 33 | in Ref. 6; BAB55174 | ||||
Sequence: V → A | ||||||
Sequence conflict | 97 | in Ref. 4; AAD44500 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_002050 | 245-278 | in isoform 3 | |||
Sequence: IKIKEWVDKYDPGALVIPFSGALELKLQELSAEE → LESTDNKAEIILLKMEILSSSNLTHLNNRRRNKI | ||||||
Sequence conflict | 254 | in Ref. 3; CAB66481 | ||||
Sequence: Y → C | ||||||
Alternative sequence | VSP_002051 | 279-396 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 391 | in Ref. 5; AAF71123 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ250006 EMBL· GenBank· DDBJ | ABB72766.1 EMBL· GenBank· DDBJ | mRNA | ||
AF134478 EMBL· GenBank· DDBJ | AAP97255.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136546 EMBL· GenBank· DDBJ | CAB66481.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078859 EMBL· GenBank· DDBJ | AAD44491.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078868 EMBL· GenBank· DDBJ | AAD44500.1 EMBL· GenBank· DDBJ | mRNA | ||
AF116703 EMBL· GenBank· DDBJ | AAF71123.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027523 EMBL· GenBank· DDBJ | BAB55174.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074710 EMBL· GenBank· DDBJ | BAC11153.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471058 EMBL· GenBank· DDBJ | EAX11151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012842 EMBL· GenBank· DDBJ | AAH12842.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013925 EMBL· GenBank· DDBJ | AAH13925.1 EMBL· GenBank· DDBJ | mRNA | ||
BC029376 EMBL· GenBank· DDBJ | AAH29376.1 EMBL· GenBank· DDBJ | mRNA | ||
BC091522 EMBL· GenBank· DDBJ | AAH91522.1 EMBL· GenBank· DDBJ | mRNA |