P29620 · CDKD1_ORYSJ
- ProteinCyclin-dependent kinase D-1
- GeneCDKD-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids424 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
CDK-activating kinase that may control G1/S phase progression. May control the rate of cell differentiation to accomplish proper development of organs, or in response to a changing environment. Forms a complex with cyclin CYCH1-1 that phosphorylates CDKA-1 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II.
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 | |
Cellular Component | transcription factor TFIIK complex | |
Molecular Function | ATP binding | |
Molecular Function | cyclin-dependent protein serine/threonine kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | RNA polymerase II CTD heptapeptide repeat kinase activity | |
Biological Process | cell division | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclin-dependent kinase D-1
- EC number
- Short namesCDKD;1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionP29620
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086074 | 1-424 | UniProt | Cyclin-dependent kinase D-1 | |||
Sequence: MASGDGGDDAGVKRVADRYLKREVLGEGTYGVVFKAVDTKTGNTVAIKKIRLGKYKEGVNFTALREIKLLKELKDSNIIELIDAFPYKGNLHLVFEFMETDLEAVIRDRNIVLSPADTKSYIQMMLKGLAFCHKKWVLHRDMKPNNLLIGADGQLKLADFGLARIFGSPERNFTHQVFARWYRAPELLFGTKQYGSAVDIWAAGCIFAELLLRRPFLQGSSDIDQLGKIFAAFGTPKSSQWPDMVYLPDYVEYQFVSAPPLRSLFPMASDDALDLLSRMFTYDPKARITAQQALEHRYFLSVPAPTKPSQLPRPPPKGDSGNNKIPDLNLQDGPVVLSPPRKLRRVTAHEGMEVHMHRADRTEEHPSGARHMDDMSSQSSRIPMSVDVGAIFGTRPAPRPTLNSADKSRLKRKLDMDPEFGYTE | |||||||
Modified residue | 29 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 30 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 168 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 174 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 174 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 338 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Expressed in actively dividing cells of roots, leaves and shoots. Expressed in the intercalary meristem and the elongation zone of internodes.
Induction
By gibberellic acid (GA3) and submergence in the meristematic zone of internodes. Down-regulated by auxin.
Developmental stage
Expression reaches a peak in the G1/S phases and then decreases in the G2/M phases.
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-299 | Protein kinase | ||||
Sequence: YLKREVLGEGTYGVVFKAVDTKTGNTVAIKKIRLGKYKEGVNFTALREIKLLKELKDSNIIELIDAFPYKGNLHLVFEFMETDLEAVIRDRNIVLSPADTKSYIQMMLKGLAFCHKKWVLHRDMKPNNLLIGADGQLKLADFGLARIFGSPERNFTHQVFARWYRAPELLFGTKQYGSAVDIWAAGCIFAELLLRRPFLQGSSDIDQLGKIFAAFGTPKSSQWPDMVYLPDYVEYQFVSAPPLRSLFPMASDDALDLLSRMFTYDPKARITAQQALEHRYF | ||||||
Region | 303-337 | Disordered | ||||
Sequence: PAPTKPSQLPRPPPKGDSGNNKIPDLNLQDGPVVL | ||||||
Region | 359-424 | Disordered | ||||
Sequence: ADRTEEHPSGARHMDDMSSQSSRIPMSVDVGAIFGTRPAPRPTLNSADKSRLKRKLDMDPEFGYTE | ||||||
Compositional bias | 405-424 | Basic and acidic residues | ||||
Sequence: ADKSRLKRKLDMDPEFGYTE |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)47,613
- Last updated1993-04-01 v1
- Checksum28606BE7120BB048
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0WLZ1 | A0A0P0WLZ1_ORYSJ | Os05g0392300 | 147 | ||
B7F5K0 | B7F5K0_ORYSJ | Os05g0392300 | 279 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 405-424 | Basic and acidic residues | ||||
Sequence: ADKSRLKRKLDMDPEFGYTE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X58194 EMBL· GenBank· DDBJ | CAA41172.1 EMBL· GenBank· DDBJ | mRNA | ||
AC107085 EMBL· GenBank· DDBJ | AAV31263.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP008211 EMBL· GenBank· DDBJ | BAF17364.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014961 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |