UniProt ID | OLA1_MOUSE | |
---|---|---|
UniProt AC | Q9CZ30 | |
Protein Name | Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167} | |
Gene Name | Ola1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 396 | |
Subcellular Localization | Cytoplasm . Nucleus . Nucleus, nucleolus . Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm. | |
Protein Description | Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP.. | |
Protein Sequence | MPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPILDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYLEANMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKDEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTPQQPKKK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Malonylation | ---MPPKKGGDGIKP ---CCCCCCCCCCCC | 74.11 | 26320211 | |
11 | Ubiquitination | KKGGDGIKPPPIIGR CCCCCCCCCCCCCCC | 57.93 | 27667366 | |
55 | Glutathionylation | SAENFPFCTIDPNES HHCCCCCEEECCCCC | 3.12 | 24333276 | |
79 | Acetylation | DFLCQYHKPASKIPA CHHHHCCCCHHHCCH | 37.03 | 22826441 | |
83 | Ubiquitination | QYHKPASKIPAFLNV HCCCCHHHCCHHHCH | 55.61 | - | |
166 | Acetylation | MIGPILDKLEKVAVR HHHHHHHHHHHHHCC | 55.91 | 23954790 | |
166 | Ubiquitination | MIGPILDKLEKVAVR HHHHHHHHHHHHHCC | 55.91 | - | |
169 | Malonylation | PILDKLEKVAVRGGD HHHHHHHHHHCCCCC | 46.03 | 26320211 | |
187 | S-nitrosocysteine | KPEYDIMCKVKSWVI CCCCEEEEEEEEEEE | 4.72 | - | |
187 | S-nitrosylation | KPEYDIMCKVKSWVI CCCCEEEEEEEEEEE | 4.72 | 21278135 | |
187 | Glutathionylation | KPEYDIMCKVKSWVI CCCCEEEEEEEEEEE | 4.72 | 24333276 | |
190 | Ubiquitination | YDIMCKVKSWVIDQK CEEEEEEEEEEECCC | 24.89 | 27667366 | |
191 | Phosphorylation | DIMCKVKSWVIDQKK EEEEEEEEEEECCCC | 29.57 | - | |
209 | Acetylation | FYHDWNDKEIEVLNK EEECCCHHHHHHHHH | 58.33 | 23954790 | |
216 | Acetylation | KEIEVLNKHLFLTSK HHHHHHHHHEEECCC | 37.21 | 23236377 | |
234 | Acetylation | YLVNLSEKDYIRKKN EEEECCHHHHHHHCC | 53.08 | 23954790 | |
253 | Acetylation | KIKEWVDKYDPGALV EHHHHHHHCCCCCEE | 41.77 | 23954790 | |
281 | Ubiquitination | LSAEERQKYLEANMT CCHHHHHHHHHHHCC | 59.01 | - | |
282 | Phosphorylation | SAEERQKYLEANMTQ CHHHHHHHHHHHCCH | 11.05 | 28059163 | |
290 | Phosphorylation | LEANMTQSALPKIIK HHHHCCHHHHHHHHH | 23.70 | 28059163 | |
294 | Malonylation | MTQSALPKIIKAGFA CCHHHHHHHHHHHHH | 58.89 | 26320211 | |
294 | Acetylation | MTQSALPKIIKAGFA CCHHHHHHHHHHHHH | 58.89 | 22826441 | |
340 | Acetylation | KIHTDFEKGFIMAEV CCCCCHHHCCEEEEE | 60.14 | 22826441 | |
354 | Acetylation | VMKYEDFKDEGSENA EEEHHHHCCCCCHHH | 68.16 | 23954790 | |
394 | Malonylation | FNTPQQPKKK----- ECCCCCCCCC----- | 69.71 | 26320211 | |
394 | Ubiquitination | FNTPQQPKKK----- ECCCCCCCCC----- | 69.71 | 27667366 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of OLA1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OLA1_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of OLA1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of OLA1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...