Q8N568 · DCLK2_HUMAN
- ProteinSerine/threonine-protein kinase DCLK2
- GeneDCLK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids766 (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]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Molecular Function | ATP binding | |
Molecular Function | microtubule binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | hippocampus development | |
Biological Process | intracellular signal transduction | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | negative regulation of protein localization to nucleus | |
Biological Process | protein localization to nucleus | |
Biological Process | pyramidal neuron development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase DCLK2
- 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 accessionQ8N568
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_040441 | 119 | in dbSNP:rs56327537 | |||
Sequence: G → C | ||||||
Natural variant | VAR_073158 | 212 | found in a patient with hereditary motor and sensory neuropathy; uncertain significance; dbSNP:rs759398144 | |||
Sequence: V → M | ||||||
Natural variant | VAR_040442 | 372 | in dbSNP:rs34386880 | |||
Sequence: R → H | ||||||
Natural variant | VAR_040443 | 583 | in dbSNP:rs35745104 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 932 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000085922 | 1-766 | UniProt | Serine/threonine-protein kinase DCLK2 | |||
Sequence: MASTRSIELEHFEERDKRPRPGSRRGAPSSSGGSSSSGPKGNGLIPSPAHSAHCSFYRTRTLQALSSEKKAKKARFYRNGDRYFKGLVFAISSDRFRSFDALLIELTRSLSDNVNLPQGVRTIYTIDGSRKVTSLDELLEGESYVCASNEPFRKVDYTKNINPNWSVNIKGGTSRALAAASSVKSEVKESKDFIKPKLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKFRYAQDDFVLDHSECRVLKSSYSRSSAVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGPELDRCISPEGVNGNRCSESSTLLEKYKIGKVIGDGNFAVVKECIDRSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLVEEMETATELFLVMELVKGGDLFDAITSSTKYTERDGSAMVYNLANALRYLHGLSIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILAGKLEFPAPYWDNITDSAKELISQMLQVNVEARCTAGQILSHPWVSDDASQENNMQAEVTGKLKQHFNNALPKQNSTTTGVSVIMNTALDKEGQIFCSKHCQDSGRPGMEPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAPGGERAGTWRRHRD | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 61 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 320 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 362 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 647 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 666 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8N568 | KLHL15 Q96M94 | 3 | EBI-2930406, EBI-2510129 | |
BINARY | Q8N568 | YWHAE P62258 | 3 | EBI-2930406, EBI-356498 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-45 | Disordered | ||||
Sequence: MASTRSIELEHFEERDKRPRPGSRRGAPSSSGGSSSSGPKGNGLI | ||||||
Compositional bias | 7-23 | Basic and acidic residues | ||||
Sequence: IELEHFEERDKRPRPGS | ||||||
Compositional bias | 27-42 | Polar residues | ||||
Sequence: APSSSGGSSSSGPKGN | ||||||
Domain | 72-158 | Doublecortin 1 | ||||
Sequence: KKARFYRNGDRYFKGLVFAISSDRFRSFDALLIELTRSLSDNVNLPQGVRTIYTIDGSRKVTSLDELLEGESYVCASNEPFRKVDYT | ||||||
Domain | 197-280 | Doublecortin 2 | ||||
Sequence: KLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKFRYAQDD | ||||||
Compositional bias | 300-368 | Polar residues | ||||
Sequence: AVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGP | ||||||
Region | 300-378 | Disordered | ||||
Sequence: AVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGPELDRCISPEG | ||||||
Domain | 394-651 | Protein kinase | ||||
Sequence: YKIGKVIGDGNFAVVKECIDRSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLVEEMETATELFLVMELVKGGDLFDAITSSTKYTERDGSAMVYNLANALRYLHGLSIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILAGKLEFPAPYWDNITDSAKELISQMLQVNVEARCTAGQILSHPWV | ||||||
Region | 707-766 | Disordered | ||||
Sequence: CQDSGRPGMEPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAPGGERAGTWRRHRD | ||||||
Compositional bias | 716-753 | Pro residues | ||||
Sequence: EPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAP |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8N568-1
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
- Length766
- Mass (Da)83,606
- Last updated2010-05-18 v4
- Checksum024F3223874AE83C
Q8N568-2
Q8N568-3
- Name3
- Differences from canonical
- 321-321: V → VKRGGHYSSAYSTAKSPV
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RR70 | A0A0U1RR70_HUMAN | DCLK2 | 716 | ||
A0A0U1RRD0 | A0A0U1RRD0_HUMAN | DCLK2 | 78 | ||
G5E9L9 | G5E9L9_HUMAN | DCLK2 | 695 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 7-23 | Basic and acidic residues | ||||
Sequence: IELEHFEERDKRPRPGS | ||||||
Compositional bias | 27-42 | Polar residues | ||||
Sequence: APSSSGGSSSSGPKGN | ||||||
Compositional bias | 300-368 | Polar residues | ||||
Sequence: AVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGP | ||||||
Alternative sequence | VSP_012793 | 321 | in isoform 3 | |||
Sequence: V → VKRGGHYSSAYSTAKSPV | ||||||
Alternative sequence | VSP_012794 | 353 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 694 | in Ref. 3; CAD39156 | ||||
Sequence: A → V | ||||||
Compositional bias | 716-753 | Pro residues | ||||
Sequence: EPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAP | ||||||
Sequence conflict | 748 | in Ref. 1; BAD92418 and 3; CAD39156 | ||||
Sequence: P → C |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB209181 EMBL· GenBank· DDBJ | BAD92418.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC093748 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC105343 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108934 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC118064 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL834498 EMBL· GenBank· DDBJ | CAD39156.1 EMBL· GenBank· DDBJ | mRNA |