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IID50054
UniprotQ63450
ProteinCalcium/calmodulin-dependent protein kinase type 1
GeneCamk1
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
374
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-329 Monomer :
 Evidence X-RAY 1a06 A Reference
       Region 1a06 A 1-9 disorder
       Region 1a06 A 10-53 order
       Region 1a06 A 54-63 disorder
       Region 1a06 A 64-163 order
       Region 1a06 A 164-181 disorder
       Region 1a06 A 182-316 order
       Region 1a06 A 317-329 disorder
Seq 294-318 Hetero dimer : IID50080Complex
 Evidence X-RAY 1mxe F Reference
       Region 1mxe F 294-318 order
 Evidence X-RAY 1mxe E Reference
       Region 1mxe E 294-318 order
Seq 299-320 Hetero dimer : IID00706Complex
 Evidence NMR 2l7l B Reference
       Region 2l7l B 299-320 order
SeqProS possible 294-318 The peptide (Ile294-Lys318), which is unstructured in solution (data not shown), is completely ordered within the complex.(PubMed=12475216) Hetero dimer : IID50080Complex
       Region 1mxe E 294-318 order
       Region 1mxe F 294-318 order
SeqProS possible 294-318 This region is ordered in the complex with another region of this protein. The C terminal region (323-329) of 1a06 was added by UniProt, but it seemd to be tag. :
       Region 1a06 A 182-316 order
Seqphosphorylation
    177-177 Phosphothreonine; by CaMKK1 and CaMKK2
 
Prediction
NeProc
Disorder 1-7,308-374
Order 8-307
ProS 1-7,308-319
AlphaFold
Disorder 1-9,29-30,59-63,65-66,164-181,299-315,319-374
Order 10-28,31-58,64-64,67-163,182-298,316-318
Pfam Hmmer
PF00069 20-276 6.2e-104
SEG 358-370
Function
Function in SwissProt
Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-516', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation (By similarity). Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-275' and 'Ser-294'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I.
Biological Process
Diagram with PDB data
Camk1/CALM1Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of calmodulin kinase I