CAMK1_ARATH - dbPTM
CAMK1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAMK1_ARATH
UniProt AC O80673
Protein Name CDPK-related kinase 1
Gene Name CRK1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 576
Subcellular Localization Membrane
Lipid-anchor
Cytoplasmic side.
Protein Description May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Serine/threonine kinase that phosphorylates histone H3. Confers thermotolerance; involved in the heat-shock-mediated calmodulin-dependent signal transduction leading to the activation of heat-shock transcription factors (HSFs); phosphorylates HSFA1A..
Protein Sequence MGICHGKPVEQQSKSLPVSGETNEAPTNSQPPAKSSGFPFYSPSPVPSLFKSSPSVSSSVSSTPLRIFKRPFPPPSPAKHIRAFLARRYGSVKPNEVSIPEGKECEIGLDKSFGFSKQFASHYEIDGEVGRGHFGYTCSAKGKKGSLKGQEVAVKVIPKSKMTTAIAIEDVSREVKMLRALTGHKNLVQFYDAFEDDENVYIVMELCKGGELLDKILQRGGKYSEDDAKKVMVQILSVVAYCHLQGVVHRDLKPENFLFSTKDETSPLKAIDFGLSDYVKPDERLNDIVGSAYYVAPEVLHRTYGTEADMWSIGVIAYILLCGSRPFWARTESGIFRAVLKAEPNFEEAPWPSLSPEAVDFVKRLLNKDYRKRLTAAQALCHPWLVGSHELKIPSDMIIYKLVKVYIMSTSLRKSALAALAKTLTVPQLAYLREQFTLLGPSKNGYISMQNYKTAILKSSTDAMKDSRVFDFVHMISCLQYKKLDFEEFCASALSVYQLEAMETWEQHARRAYELFEKDGNRPIMIEELASELGLGPSVPVHVVLQDWIRHSDGKLSFLGFVRLLHGVSSRTLQKA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGICHGKPV
------CCCCCCCCC
-
15PhosphorylationPVEQQSKSLPVSGET
CCCCCCCCCCCCCCC
25561503
19PhosphorylationQSKSLPVSGETNEAP
CCCCCCCCCCCCCCC
25561503
35PhosphorylationNSQPPAKSSGFPFYS
CCCCCCHHCCCCCCC
30407730
36PhosphorylationSQPPAKSSGFPFYSP
CCCCCHHCCCCCCCC
30407730
41PhosphorylationKSSGFPFYSPSPVPS
HHCCCCCCCCCCCCC
30407730
42PhosphorylationSSGFPFYSPSPVPSL
HCCCCCCCCCCCCCH
30407730
44PhosphorylationGFPFYSPSPVPSLFK
CCCCCCCCCCCCHHC
30407730
48PhosphorylationYSPSPVPSLFKSSPS
CCCCCCCCHHCCCCC
30407730
52PhosphorylationPVPSLFKSSPSVSSS
CCCCHHCCCCCCCCC
17317660
53PhosphorylationVPSLFKSSPSVSSSV
CCCHHCCCCCCCCCC
17317660
55PhosphorylationSLFKSSPSVSSSVSS
CHHCCCCCCCCCCCC
19376835
57PhosphorylationFKSSPSVSSSVSSTP
HCCCCCCCCCCCCCC
19376835
58PhosphorylationKSSPSVSSSVSSTPL
CCCCCCCCCCCCCCC
19376835
59PhosphorylationSSPSVSSSVSSTPLR
CCCCCCCCCCCCCCE
19376835
61PhosphorylationPSVSSSVSSTPLRIF
CCCCCCCCCCCCEEE
19376835
62PhosphorylationSVSSSVSSTPLRIFK
CCCCCCCCCCCEEEC
19376835
63PhosphorylationVSSSVSSTPLRIFKR
CCCCCCCCCCEEECC
19376835
76PhosphorylationKRPFPPPSPAKHIRA
CCCCCCCCHHHHHHH
23111157
163PhosphorylationVIPKSKMTTAIAIED
EECHHHCEEEEEHHH
27532006
164PhosphorylationIPKSKMTTAIAIEDV
ECHHHCEEEEEHHHH
27532006
291PhosphorylationRLNDIVGSAYYVAPE
HHHHHCCCHHHCCHH
-
331PhosphorylationSRPFWARTESGIFRA
CCCCEECCHHCHHHH
15308754
333PhosphorylationPFWARTESGIFRAVL
CCEECCHHCHHHHHH
30291188
557PhosphorylationRHSDGKLSFLGFVRL
HCCCCCEEHHHHHHH
-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
333SPhosphorylationKinaseCPK1Q06850
Uniprot
333SPhosphorylationKinaseCPK34Q3E9C0
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAMK1_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CAMK1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HFA1A_ARATHHSF1physical
18466301

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAMK1_ARATH

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Related Literatures of Post-Translational Modification

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