Q5XIS1
Gene name |
Ssh3 |
Protein name |
Protein phosphatase Slingshot homolog 3 |
Names |
SSH-like protein 3, SSH-3L |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:365396 |
EC number |
3.1.3.16: Phosphoric monoester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5XIS1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5XIS1-F1 | Predicted | AlphaFoldDB |
No variants for Q5XIS1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5XIS1 | |||||
No associated diseases with Q5XIS1
5 regional properties for Q5XIS1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dual specificity phosphatase, catalytic domain | 333 - 461 | IPR000340 |
| domain | Tyrosine-specific protein phosphatases domain | 390 - 445 | IPR000387 |
| domain | DEK, C-terminal | 266 - 321 | IPR014876 |
| active_site | Protein-tyrosine phosphatase, active site | 408 - 418 | IPR016130 |
| domain | Dual specificity protein phosphatase domain | 325 - 466 | IPR020422 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.3.16 | Phosphoric monoester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| myosin phosphatase activity | Catalysis of the reaction: phosphomyosin + H2O = myosin + phosphate. |
| phosphoprotein phosphatase activity | Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity. |
| protein tyrosine phosphatase activity | Catalysis of the reaction: protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
| protein tyrosine/serine/threonine phosphatase activity | Catalysis of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein threonine + phosphate; and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
| negative regulation of actin filament polymerization | Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization. |
| protein dephosphorylation | The process of removing one or more phosphoric residues from a protein. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALVTVSRSP | PASGHSTPVG | PTDRVIRRRG | RLQRRQSFAV | LRGAVLGLQD | GGEGNDAAEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DPEPMEKPSG | EEQPAEDQTD | NGQGSQSPWK | QVQKRHLHLM | VELLRPQDDI | RLAAQLEAAR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PPRLRYLLVV | STGEGLSEEE | TILLGVDFPD | SSSHSCTLGL | VLPLWSDTQV | YLDGDGGFSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TSGGQSRIFK | PVSIQTMWAT | LQVLHQACEV | ALGSGLVPGG | SALAWATHYQ | EKLNSDQGCL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NEWMAMSDLE | SFRPPNAEPG | QASEQEQMEQ | AILAELWQVL | DASDLDSVTS | KEIRQALELR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LGCPLQQYRD | FIDNQMLLLM | AQQDRASRIF | PHLYLGSEWN | AANLEELQRN | RVSHILNMAR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EIDNFFPERF | TYHNVRVWDE | ESAQLLPHWK | ETHRFIEDAR | AQGTRVLVHC | KMGVSRSAAT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VLAYAMKQYG | WGLEQALIHV | QELRPIVRPN | PGFLRQLQTY | QGILTASRQS | HVWEQKVGVV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SPEEPLAPEV | STPLPPLPPE | PGGSGEGMVM | GQKGSQETPK | EELGLRPRIN | LRGVMRSISL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LEPSSEPEST | TEAGDLPEVF | SSDEEPLHPF | SQLSRAKGGQ | RVCKGPWPAL | KSRQSVVALH |
| 610 | 620 | 630 | 640 | 650 | |
| SAALVASRAR | AFQGQGQGQG | QEQRETGTSS | TPRLRKVIRQ | ASVDDSREEG | KA |