P49761
Gene name |
CLK3 |
Protein name |
Dual specificity protein kinase CLK3 |
Names |
CDC-like kinase 3 |
Species |
Homo sapiens (Human) |
KEGG Pathway |
hsa:1198 |
EC number |
2.7.12.1: Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) |
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
467-487 (Activation loop from InterPro)
Target domain |
304-620 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
20 structures for P49761
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2EU9 | X-ray | 153 A | A | 284-638 | PDB |
| 2EXE | X-ray | 235 A | A | 275-631 | PDB |
| 2WU6 | X-ray | 192 A | A | 275-632 | PDB |
| 2WU7 | X-ray | 225 A | A | 275-632 | PDB |
| 3RAW | X-ray | 209 A | A/B | 275-632 | PDB |
| 6FT7 | X-ray | 202 A | A/B | 275-632 | PDB |
| 6FYP | X-ray | 229 A | A | 275-632 | PDB |
| 6FYR | X-ray | 142 A | A | 275-632 | PDB |
| 6KHF | X-ray | 260 A | A | 149-638 | PDB |
| 6RCT | X-ray | 232 A | A/B | 275-632 | PDB |
| 6YTW | X-ray | 200 A | A/B | 275-632 | PDB |
| 6YTY | X-ray | 176 A | A | 275-632 | PDB |
| 6YU1 | X-ray | 190 A | a/c | 275-632 | PDB |
| 6Z2V | X-ray | 260 A | A | 275-632 | PDB |
| 6Z51 | X-ray | 192 A | A | 275-632 | PDB |
| 6Z52 | X-ray | 212 A | A/B | 275-632 | PDB |
| 6Z53 | X-ray | 165 A | A | 275-632 | PDB |
| 6Z54 | X-ray | 173 A | A | 275-632 | PDB |
| 6Z55 | X-ray | 170 A | A/B | 275-632 | PDB |
| AF-P49761-F1 | Predicted | AlphaFoldDB |
3 variants for P49761
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
|
VAR_040413 rs975796055 |
486 | R>C | No |
UniProt dbSNP |
|
|
VAR_045579 rs910378995 |
607 | Q>R | No |
UniProt dbSNP |
|
|
rs920443187 VAR_045580 |
628 | R>W | No |
UniProt dbSNP |
No associated diseases with P49761
1 regional properties for P49761
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GPCR, rhodopsin-like, 7TM | 22 - 605 | IPR017452 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.12.1 | Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| acrosomal vesicle | A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome. |
| intermediate filament cytoskeleton | Cytoskeletal structure made from intermediate filaments, typically organized in the cytosol as an extended system that stretches from the nuclear envelope to the plasma membrane. Some intermediate filaments run parallel to the cell surface, while others traverse the cytosol; together they form an internal framework that helps support the shape and resilience of the cell. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| 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. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
| protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
| protein tyrosine kinase activity | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| peptidyl-tyrosine phosphorylation | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. |
| protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| regulation of RNA splicing | Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPVLSARRRE | LADHAGSGRR | SGPSPTARSG | PHLSALRAQP | ARAAHLSGRG | TYVRRDTAGG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPGQARPLGP | PGTSLLGRGA | RRSGEGWCPG | AFESGARAAR | PPSRVEPRLA | TAASREGAGL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PRAEVAAGSG | RGARSGEWGL | AAAGAWETMH | HCKRYRSPEP | DPYLSYRWKR | RRSYSREHEG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLRYPSRREP | PPRRSRSRSH | DRLPYQRRYR | ERRDSDTYRC | EERSPSFGED | YYGPSRSRHR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RRSRERGPYR | TRKHAHHCHK | RRTRSCSSAS | SRSQQSSKRS | SRSVEDDKEG | HLVCRIGDWL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QERYEIVGNL | GEGTFGKVVE | CLDHARGKSQ | VALKIIRNVG | KYREAARLEI | NVLKKIKEKD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KENKFLCVLM | SDWFNFHGHM | CIAFELLGKN | TFEFLKENNF | QPYPLPHVRH | MAYQLCHALR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FLHENQLTHT | DLKPENILFV | NSEFETLYNE | HKSCEEKSVK | NTSIRVADFG | SATFDHEHHT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TIVATRHYRP | PEVILELGWA | QPCDVWSIGC | ILFEYYRGFT | LFQTHENREH | LVMMEKILGP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IPSHMIHRTR | KQKYFYKGGL | VWDENSSDGR | YVKENCKPLK | SYMLQDSLEH | VQLFDLMRRM |
| 610 | 620 | 630 | |||
| LEFDPAQRIT | LAEALLHPFF | AGLTPEERSF | HTSRNPSR |