Q00537 · CDK17_HUMAN
- ProteinCyclin-dependent kinase 17
- GeneCDK17
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids523 (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 | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | cyclin-dependent protein serine/threonine kinase activity | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclin-dependent kinase 17
- 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 accessionQ00537
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_064743 | 214 | found in a renal cell carcinoma sample; somatic mutation; dbSNP:rs764448325 | |||
Sequence: T → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 406 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_0000086487 | 1-523 | UniProt | Cyclin-dependent kinase 17 | |||
Sequence: MKKFKRRLSLTLRGSQTIDESLSELAEQMTIEENSSKDNEPIVKNGRPPTSHSMHSFLHQYTGSFKKPPLRRPHSVIGGSLGSFMAMPRNGSRLDIVHENLKMGSDGESDQASGTSSDEVQSPTGVCLRNRIHRRISMEDLNKRLSLPADIRIPDGYLEKLQINSPPFDQPMSRRSRRASLSEIGFGKMETYIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPSQETWPGISSNEEFKNYNFPKYKPQPLINHAPRLDSEGIELITKFLQYESKKRVSAEEAMKHVYFRSLGPRIHALPESVSIFSLKEIQLQKDPGFRNSSYPETGHGKNRRQSMLF | |||||||
Modified residue | 9 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 80 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 83 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 92 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 137 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 146 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 165 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 180 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 180 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q00537 | BICDL2 A1A5D9 | 3 | EBI-624648, EBI-10171799 | |
BINARY | Q00537 | CDK16 Q00536 | 5 | EBI-624648, EBI-726261 | |
BINARY | Q00537 | CDKN2B P42772 | 3 | EBI-624648, EBI-711280 | |
BINARY | Q00537 | DPY30 Q9C005 | 3 | EBI-624648, EBI-744973 | |
BINARY | Q00537 | YWHAE P62258 | 4 | EBI-624648, EBI-356498 | |
BINARY | Q00537 | YWHAZ P63104 | 6 | EBI-624648, EBI-347088 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 30-55 | Disordered | ||||
Sequence: TIEENSSKDNEPIVKNGRPPTSHSMH | ||||||
Region | 103-123 | Disordered | ||||
Sequence: MGSDGESDQASGTSSDEVQSP | ||||||
Compositional bias | 106-123 | Polar residues | ||||
Sequence: DGESDQASGTSSDEVQSP | ||||||
Domain | 192-473 | Protein kinase | ||||
Sequence: YIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPSQETWPGISSNEEFKNYNFPKYKPQPLINHAPRLDSEGIELITKFLQYESKKRVSAEEAMKHVYF | ||||||
Region | 501-523 | Disordered | ||||
Sequence: PGFRNSSYPETGHGKNRRQSMLF |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q00537-1
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
- Length523
- Mass (Da)59,582
- Last updated2005-02-15 v2
- Checksum429ABD1DCBB5A082
Q00537-2
- Name2
- Differences from canonical
- 513-523: HGKNRRQSMLF → VFVINHFTCRS
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 106-123 | Polar residues | ||||
Sequence: DGESDQASGTSSDEVQSP | ||||||
Sequence conflict | 367 | in Ref. 1; CAA47004 | ||||
Sequence: S → L | ||||||
Sequence conflict | 433 | in Ref. 1; CAA47004 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 451 | in Ref. 1; CAA47004 | ||||
Sequence: T → R | ||||||
Alternative sequence | VSP_043295 | 513-523 | in isoform 2 | |||
Sequence: HGKNRRQSMLF → VFVINHFTCRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X66360 EMBL· GenBank· DDBJ | CAA47004.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290011 EMBL· GenBank· DDBJ | BAF82700.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315214 EMBL· GenBank· DDBJ | BAG37649.1 EMBL· GenBank· DDBJ | mRNA | ||
AC125612 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471054 EMBL· GenBank· DDBJ | EAW97566.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW97567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC033005 EMBL· GenBank· DDBJ | AAH33005.1 EMBL· GenBank· DDBJ | mRNA |