P49761 · CLK3_HUMAN
- ProteinDual specificity protein kinase CLK3
- GeneCLK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids490 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | acrosomal vesicle | |
Cellular Component | intermediate filament cytoskeleton | |
Cellular Component | membrane | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein serine/threonine/tyrosine kinase activity | |
Molecular Function | protein tyrosine kinase activity | |
Molecular Function | RNA binding | |
Biological Process | protein phosphorylation | |
Biological Process | regulation of RNA splicing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual specificity protein kinase CLK3
- 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 accessionP49761
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_040413 | 338 | in dbSNP:rs975796055 | |||
Sequence: R → C | ||||||
Natural variant | VAR_045579 | 459 | in dbSNP:rs910378995 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_045580 | 480 | in dbSNP:rs920443187 | |||
Sequence: R → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 514 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000085870 | 1-490 | UniProt | Dual specificity protein kinase CLK3 | |||
Sequence: MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR | |||||||
Modified residue | 7 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 67 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 67 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 76 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 78 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 135 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 135 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-78 | Basic and acidic residues | ||||
Sequence: MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPS | ||||||
Region | 1-138 | Disordered | ||||
Sequence: MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVED | ||||||
Compositional bias | 89-118 | Basic residues | ||||
Sequence: SRHRRRSRERGPYRTRKHAHHCHKRRTRSC | ||||||
Domain | 156-472 | Protein kinase | ||||
Sequence: YEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFF |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P49761-1
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
- SynonymsLong
- Length490
- Mass (Da)58,588
- Last updated2024-07-24 v4
- Checksum86A342ABB8AB24CA
P49761-2
- Name2
- SynonymsShort
- NoteLacks the kinase domain. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
P49761-3
- Name3
- Differences from canonical
- 158-180: Missing
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BV35 | H3BV35_HUMAN | CLK3 | 145 | ||
H3BUL5 | H3BUL5_HUMAN | CLK3 | 224 | ||
H3BVF8 | H3BVF8_HUMAN | CLK3 | 239 | ||
H3BTW9 | H3BTW9_HUMAN | CLK3 | 19 | ||
H3BRK0 | H3BRK0_HUMAN | CLK3 | 173 | ||
H3BRE4 | H3BRE4_HUMAN | CLK3 | 190 | ||
H3BRT8 | H3BRT8_HUMAN | CLK3 | 117 | ||
H3BRW2 | H3BRW2_HUMAN | CLK3 | 70 | ||
H3BQG1 | H3BQG1_HUMAN | CLK3 | 286 | ||
H3BQR7 | H3BQR7_HUMAN | CLK3 | 145 | ||
H3BNC8 | H3BNC8_HUMAN | CLK3 | 59 | ||
H3BNQ5 | H3BNQ5_HUMAN | CLK3 | 193 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-78 | Basic and acidic residues | ||||
Sequence: MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPS | ||||||
Compositional bias | 89-118 | Basic residues | ||||
Sequence: SRHRRRSRERGPYRTRKHAHHCHKRRTRSC | ||||||
Alternative sequence | VSP_062381 | 124-152 | in isoform 2 | |||
Sequence: RSQQSSKRSSRSVEDDKEGHLVCRIGDWL → MRLWGTWVKAPLARWWSAWTMPEGSLRLP | ||||||
Sequence conflict | 132-133 | in Ref. 1; AAA61484 | ||||
Sequence: SS → TG | ||||||
Alternative sequence | VSP_062382 | 153-490 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_062383 | 158-180 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L29220 EMBL· GenBank· DDBJ | AAA61483.1 EMBL· GenBank· DDBJ | mRNA | ||
L29217 EMBL· GenBank· DDBJ | AAA61484.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006993 EMBL· GenBank· DDBJ | AAP35639.1 EMBL· GenBank· DDBJ | mRNA | ||
AC100835 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471136 EMBL· GenBank· DDBJ | EAW99321.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471136 EMBL· GenBank· DDBJ | EAW99322.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002555 EMBL· GenBank· DDBJ | AAH02555.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006103 EMBL· GenBank· DDBJ | AAH06103.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019881 EMBL· GenBank· DDBJ | AAH19881.1 EMBL· GenBank· DDBJ | mRNA |