KKCC2_HUMAN - dbPTM
KKCC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KKCC2_HUMAN
UniProt AC Q96RR4
Protein Name Calcium/calmodulin-dependent protein kinase kinase 2
Gene Name CAMKK2
Organism Homo sapiens (Human).
Sequence Length 588
Subcellular Localization Nucleus. Cytoplasm . Cell projection . Predominantly nuclear in unstimulated cells (By similarity). 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. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. 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). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching..
Protein Sequence MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE
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		32.2322814378
32UbiquitinationSSSSESQKPCEALRG
CCCCCCHHHHHHHHH		62.00-
32 (in isoform 7)Ubiquitination-62.00-
56O-linked_GlycosylationMESFIVVTECEPGCA
CCEEEEEEECCCCCE		24.8323301498
85PhosphorylationGQEVPLDTSGSQARP
CCCCCCCCCCCCCCC		42.5429214152
86PhosphorylationQEVPLDTSGSQARPH
CCCCCCCCCCCCCCC		35.7928555341
88PhosphorylationVPLDTSGSQARPHLS
CCCCCCCCCCCCCCC		22.0429214152
95PhosphorylationSQARPHLSGRKLSLQ
CCCCCCCCCCCCCCH		33.2529214152
98UbiquitinationRPHLSGRKLSLQERS
CCCCCCCCCCCHHHH		46.05-
98 (in isoform 7)Ubiquitination-46.05-
100PhosphorylationHLSGRKLSLQERSQG
CCCCCCCCCHHHHCC		30.9223401153
114PhosphorylationGGLAAGGSLDMNGRC
CCCCCCCCCCCCCCE		21.9323186163
125PhosphorylationNGRCICPSLPYSPVS
CCCEECCCCCCCCCC		37.2523927012
128PhosphorylationCICPSLPYSPVSSPQ
EECCCCCCCCCCCCC		30.7923927012
129PhosphorylationICPSLPYSPVSSPQS
ECCCCCCCCCCCCCC		19.5230278072
132PhosphorylationSLPYSPVSSPQSSPR
CCCCCCCCCCCCCCC		39.4230278072
133PhosphorylationLPYSPVSSPQSSPRL
CCCCCCCCCCCCCCC		27.4830278072
136PhosphorylationSPVSSPQSSPRLPRR
CCCCCCCCCCCCCCC		45.7725159151
137PhosphorylationPVSSPQSSPRLPRRP
CCCCCCCCCCCCCCC		14.5923927012
145PhosphorylationPRLPRRPTVESHHVS
CCCCCCCCCCCCCEE		34.7827282143
148PhosphorylationPRRPTVESHHVSITG
CCCCCCCCCCEEEEC		17.9827251275
152PhosphorylationTVESHHVSITGMQDC
CCCCCCEEEECHHHH		15.2928348404
154PhosphorylationESHHVSITGMQDCVQ
CCCCEEEECHHHHHH		21.0628348404
173UbiquitinationTLKDEIGKGSYGVVK
EECCCCCCCCCEEEE		50.7921906983
173 (in isoform 1)Ubiquitination-50.7921906983
173 (in isoform 2)Ubiquitination-50.7921906983
173 (in isoform 3)Ubiquitination-50.7921906983
173 (in isoform 4)Ubiquitination-50.7921906983
173 (in isoform 5)Ubiquitination-50.7921906983
173 (in isoform 6)Ubiquitination-50.7921906983
173 (in isoform 7)Ubiquitination-50.7921906983
183PhosphorylationYGVVKLAYNENDNTY
CEEEEEEEECCCCCE		33.18-
189PhosphorylationAYNENDNTYYAMKVL
EEECCCCCEEEEHHH		22.2927642862
190PhosphorylationYNENDNTYYAMKVLS
EECCCCCEEEEHHHC		8.7617360941
191PhosphorylationNENDNTYYAMKVLSK
ECCCCCEEEEHHHCH		9.7427642862
194UbiquitinationDNTYYAMKVLSKKKL
CCCEEEEHHHCHHHH		31.67-
194 (in isoform 7)Ubiquitination-31.67-
234PhosphorylationRGPIEQVYQEIAILK
CCHHHHHHHHHHHHH		10.5027642862
241UbiquitinationYQEIAILKKLDHPNV
HHHHHHHHCCCCCCE		45.2221906983
241 (in isoform 1)Ubiquitination-45.2221906983
241 (in isoform 2)Ubiquitination-45.2221906983
241 (in isoform 3)Ubiquitination-45.2221906983
241 (in isoform 4)Ubiquitination-45.2221906983
241 (in isoform 5)Ubiquitination-45.2221906983
241 (in isoform 6)Ubiquitination-45.2221906983
241 (in isoform 7)Ubiquitination-45.2221906983
242UbiquitinationQEIAILKKLDHPNVV
HHHHHHHCCCCCCEE		56.56-
242 (in isoform 7)Ubiquitination-56.56-
307UbiquitinationIEYLHYQKIIHRDIK
HHHHHHEEEECCCCC		36.14-
307 (in isoform 7)Ubiquitination-36.14-
314UbiquitinationKIIHRDIKPSNLLVG
EEECCCCCHHHEEEC		46.8421906983
314 (in isoform 1)Ubiquitination-46.8421906983
314 (in isoform 2)Ubiquitination-46.8421906983
314 (in isoform 3)Ubiquitination-46.8421906983
314 (in isoform 4)Ubiquitination-46.8421906983
314 (in isoform 5)Ubiquitination-46.8421906983
314 (in isoform 6)Ubiquitination-46.8421906983
314 (in isoform 7)Ubiquitination-46.8421906983
327UbiquitinationVGEDGHIKIADFGVS
ECCCCCEEEEEECCC		26.60-
338UbiquitinationFGVSNEFKGSDALLS
ECCCCCCCCCCHHHC		51.86-
350PhosphorylationLLSNTVGTPAFMAPE
HHCCCCCCCCCCCCC		13.70-
401 (in isoform 7)Ubiquitination-43.32-
403UbiquitinationMCLHSKIKSQALEFP
HHHHHHHHHHHHCCC		40.012190698
403 (in isoform 1)Ubiquitination-40.0121906983
403 (in isoform 2)Ubiquitination-40.0121906983
403 (in isoform 3)Ubiquitination-40.0121906983
403 (in isoform 4)Ubiquitination-40.0121906983
403 (in isoform 5)Ubiquitination-40.0121906983
403 (in isoform 6)Ubiquitination-40.0121906983
403 (in isoform 7)Ubiquitination-40.0121906983
420UbiquitinationPDIAEDLKDLITRML
CCHHHHHHHHHHHHH		63.91-
429UbiquitinationLITRMLDKNPESRIV
HHHHHHCCCCHHCCE		71.13-
429 (in isoform 7)Ubiquitination-71.13-
441UbiquitinationRIVVPEIKLHPWVTR
CCEECCEECCCCCCC		38.80-
441 (in isoform 4)Ubiquitination-38.80-
441 (in isoform 5)Ubiquitination-38.80-
441 (in isoform 7)Ubiquitination-38.80-
445 (in isoform 5)Ubiquitination-8.05-
452 (in isoform 4)Phosphorylation-52.5425849741
452 (in isoform 5)Phosphorylation-52.5425849741
452 (in isoform 6)Phosphorylation-52.5425849741
468 (in isoform 5)Phosphorylation-58.2925849741
476 (in isoform 5)Ubiquitination-35.32-
479 (in isoform 5)Phosphorylation-24.0228355574
479 (in isoform 6)Phosphorylation-24.0222210691
486 (in isoform 5)Phosphorylation-2.5530257219
486 (in isoform 6)Phosphorylation-2.5522210691
488UbiquitinationLATVILVKTMIRKRS
HHHHHHHHHHHHHHC		29.00-
495PhosphorylationKTMIRKRSFGNPFEG
HHHHHHHCCCCCCCC		40.3119664994
503PhosphorylationFGNPFEGSRREERSL
CCCCCCCCCCHHHCC		22.4423403867
509PhosphorylationGSRREERSLSAPGNL
CCCCHHHCCCCCCCC		29.9225159151
511PhosphorylationRREERSLSAPGNLLT
CCHHHCCCCCCCCCC		33.3923401153
511 (in isoform 3)Phosphorylation-33.3925849741
518PhosphorylationSAPGNLLTKKPTREC
CCCCCCCCCCCCHHC		39.9423403867
519 (in isoform 3)Ubiquitination-57.64-
522PhosphorylationNLLTKKPTRECESLS
CCCCCCCCHHCCCHH		48.2419369195
522 (in isoform 2)Phosphorylation-48.2422210691
522 (in isoform 3)Phosphorylation-48.2428355574
529 (in isoform 2)Phosphorylation-50.6022210691
529 (in isoform 3)Phosphorylation-50.6030257219
559PhosphorylationGSALVRGSPCVESCW
CCCCCCCCCCCCCCE		12.4523532336
572PhosphorylationCWAPAPGSPARMHPL
CEECCCCCCCCCCCC		17.8328985074
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
85TPhosphorylationKinaseCAMKK2Q96RR4
PSP
511SPhosphorylationKinaseDAPK1P53355
PSP
511SPhosphorylationKinaseDAPK-FAMILY-GPS
511SPhosphorylationKinaseDAPK_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseFBXL12Q9NXK8
PMID:23707388
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KKCC2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OBSL1_HUMANOBSL1physical
20562859
FLNC_HUMANFLNCphysical
20562859
AAPK2_HUMANPRKAA2physical
20562859
GCN1_HUMANGCN1L1physical
20562859
XPOT_HUMANXPOTphysical
20562859
IQGA2_HUMANIQGAP2physical
20562859
PRKDC_HUMANPRKDCphysical
20562859
AAKG1_HUMANPRKAG1physical
20562859
FLNA_HUMANFLNAphysical
20562859
ATG4B_HUMANATG4Bphysical
20562859
ESYT2_HUMANESYT2physical
20562859
MK14_HUMANMAPK14physical
20562859
FANCI_HUMANFANCIphysical
20562859
SMC1A_HUMANSMC1Aphysical
20562859
SMC3_HUMANSMC3physical
20562859
M2OM_HUMANSLC25A11physical
20562859
IRAK1_HUMANIRAK1physical
20562859
A4_HUMANAPPphysical
21832049
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KKCC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-511,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 (ISOFORM 3),PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 (ISOFORM 5), ANDMASS SPECTROMETRY.

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