KKCC2_MOUSE - dbPTM
KKCC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KKCC2_MOUSE
UniProt AC Q8C078
Protein Name Calcium/calmodulin-dependent protein kinase kinase 2
Gene Name Camkk2
Organism Mus musculus (Mouse).
Sequence Length 588
Subcellular Localization Nucleus. Cytoplasm. Cell projection. Predominantly nuclear in unstimulated cells. Found in the cytoplasm and neurites after forskolin induction..
Protein Description Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching (By similarity). May be involved in hippocampal activation of CREB1..
Protein Sequence MSSCVSSQPTSDRVAPQDELGSGGGSREGQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLNLARDQPPEADGQELPLEASDPESRSPLSGRKMSLQEPSQGGPASSSNSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGARPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPGSPPRMPPLQPEEVMEPE
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
2Acetylation------MSSCVSSQP
------CCCCCCCCC
32.23-
85PhosphorylationQELPLEASDPESRSP
CCCCCCCCCCCCCCC
44.3021082442
89PhosphorylationLEASDPESRSPLSGR
CCCCCCCCCCCCCCC
43.3726824392
91PhosphorylationASDPESRSPLSGRKM
CCCCCCCCCCCCCCC
39.2025521595
94PhosphorylationPESRSPLSGRKMSLQ
CCCCCCCCCCCCCCC
39.6825619855
99PhosphorylationPLSGRKMSLQEPSQG
CCCCCCCCCCCCCCC
29.9025521595
104PhosphorylationKMSLQEPSQGGPASS
CCCCCCCCCCCCCCC
40.4825619855
110PhosphorylationPSQGGPASSSNSLDM
CCCCCCCCCCCCCCC
37.1225619855
111PhosphorylationSQGGPASSSNSLDMN
CCCCCCCCCCCCCCC
35.3325619855
112PhosphorylationQGGPASSSNSLDMNG
CCCCCCCCCCCCCCC
28.1325619855
114PhosphorylationGPASSSNSLDMNGRC
CCCCCCCCCCCCCEE
27.9125619855
125PhosphorylationNGRCICPSLSYSPAS
CCEEECCCCCCCCCC
26.0726643407
127PhosphorylationRCICPSLSYSPASSP
EEECCCCCCCCCCCC
28.0926745281
128PhosphorylationCICPSLSYSPASSPQ
EECCCCCCCCCCCCC
24.7826745281
129PhosphorylationICPSLSYSPASSPQS
ECCCCCCCCCCCCCC
15.6021082442
132PhosphorylationSLSYSPASSPQSSPR
CCCCCCCCCCCCCCC
46.0321082442
133PhosphorylationLSYSPASSPQSSPRM
CCCCCCCCCCCCCCC
29.1225521595
136PhosphorylationSPASSPQSSPRMPRR
CCCCCCCCCCCCCCC
45.7725168779
137PhosphorylationPASSPQSSPRMPRRP
CCCCCCCCCCCCCCC
15.9821082442
154PhosphorylationESHHVSITGLQDCVQ
CCCCCEEECHHHHHH
25.0829899451
176PhosphorylationDEIGKGSYGVVKLAY
CCCCCCCCEEEEEEE
23.70-
190PhosphorylationYNENDNTYYAMKVLS
EECCCCCEEEEHHHC
8.76-
191PhosphorylationNENDNTYYAMKVLSK
ECCCCCEEEEHHHCH
9.74-
223GlutathionylationARPAPGGCIQPRGPI
CCCCCCCCCCCCCHH
3.0224333276
456PhosphorylationHGAEPLPSEDENCTL
CCCCCCCCCCCCCEE
66.42-
462PhosphorylationPSEDENCTLVEVTEE
CCCCCCCEEEECCHH
45.4829899451
474PhosphorylationTEEEVENSVKHIPSL
CHHHHHHHHCCCCHH
21.02-
483PhosphorylationKHIPSLATVILVKTM
CCCCHHHHHHHHHHH
17.2421183079
489PhosphorylationATVILVKTMIRKRSF
HHHHHHHHHHHHHCC
15.45-
495PhosphorylationKTMIRKRSFGNPFEG
HHHHHHHCCCCCCCC
40.3125521595
503PhosphorylationFGNPFEGSRREERSL
CCCCCCCCCCHHHCC
22.4428833060
509PhosphorylationGSRREERSLSAPGNL
CCCCHHHCCCCCCCC
29.9222324799
511PhosphorylationRREERSLSAPGNLLT
CCHHHCCCCCCCCCC
33.3922942356
511 (in isoform 2)Phosphorylation-33.3927566939
518PhosphorylationSAPGNLLTKKPTREW
CCCCCCCCCCCCCCC
39.9428833060
522PhosphorylationNLLTKKPTREWEPLS
CCCCCCCCCCCCCCC
50.5324719451
522 (in isoform 2)Phosphorylation-50.5325266776
525 (in isoform 2)Phosphorylation-14.8230635358
564PhosphorylationKGGPCVESWGAPAPG
ECCCCCCCCCCCCCC
15.4825619855
572PhosphorylationWGAPAPGSPPRMPPL
CCCCCCCCCCCCCCC
30.5825521595

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

Oops, there are no upstream regulatory protein records of KKCC2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KKCC2_MOUSE !!

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 KKCC2_MOUSE !!

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

Oops, there are no PPI records of KKCC2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KKCC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-133, ANDMASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASSSPECTROMETRY.

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