KCC2D_RAT - dbPTM
KCC2D_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2D_RAT
UniProt AC P15791
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit delta
Gene Name Camk2d
Organism Rattus norvegicus (Rat).
Sequence Length 533
Subcellular Localization Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side . Sarcoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side .
Isoform Delta 1: Nucleus.
Protein Description Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor (By similarity)..
Protein Sequence MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKINNKANVVTSPKENIPTPALEPQTTVIHNPDGNKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALPKINKPIHTIILNPHVHLVGDDAACIAYIRLTQYMDGNGMPKTMQSEETRVWHRRDGKWQNIHFHRSGSPTVPIKPPCIPNGKENFSGGTSLWQNI
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------MASTTTCTR
------CCCCCCCCC		18.65-
14PhosphorylationCTRFTDEYQLFEELG
CCCCCCHHHHHHHHC		17.21-
22AcetylationQLFEELGKGAFSVVR
HHHHHHCCCHHHHHH		60.7472610703
26PhosphorylationELGKGAFSVVRRCMK
HHCCCHHHHHHHHCC		21.1125403869
33UbiquitinationSVVRRCMKIPTGQEY
HHHHHHCCCCCCHHH		49.51-
40PhosphorylationKIPTGQEYAAKIINT
CCCCCHHHHHHHHHH		12.17-
43AcetylationTGQEYAAKIINTKKL
CCHHHHHHHHHHCCC		35.6322902405
43UbiquitinationTGQEYAAKIINTKKL
CCHHHHHHHHHHCCC		35.63-
48UbiquitinationAAKIINTKKLSARDH
HHHHHHHCCCCHHHH		47.42-
49UbiquitinationAKIINTKKLSARDHQ
HHHHHHCCCCHHHHH		45.71-
57AcetylationLSARDHQKLEREARI
CCHHHHHHHHHHHHH		49.2372607905
69AcetylationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.707768885
69UbiquitinationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.70-
107PhosphorylationEDIVAREYYSEADAS
HHHHHHHHCCHHCHH		13.51-
138UbiquitinationGIVHRDLKPENLLLA
CCCCCCCCHHHEEEE		55.35-
138AcetylationGIVHRDLKPENLLLA
CCCCCCCCHHHEEEE		55.357768897
146PhosphorylationPENLLLASKSKGAAV
HHHEEEEECCCCCCE		37.1127097102
147UbiquitinationENLLLASKSKGAAVK
HHEEEEECCCCCCEE		51.05-
154UbiquitinationKSKGAAVKLADFGLA
CCCCCCEEHHHCCEE		32.98-
182PhosphorylationAGTPGYLSPEVLRKD
CCCCCCCCHHHHHCC		15.5530181290
223PhosphorylationDEDQHRLYQQIKAGA
CHHHHHHHHHHHHCC		9.79-
227AcetylationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11134811
227UbiquitinationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11-
231PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCC		19.73-
235PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCCCCCC		35.1328551015
240PhosphorylationFPSPEWDTVTPEAKD
CCCCCCCCCCHHHHH		27.61-
242PhosphorylationSPEWDTVTPEAKDLI
CCCCCCCCHHHHHHH		19.94-
246UbiquitinationDTVTPEAKDLINKML
CCCCHHHHHHHHHHH		51.94-
251UbiquitinationEAKDLINKMLTINPA
HHHHHHHHHHCCCHH		28.44-
259UbiquitinationMLTINPAKRITASEA
HHCCCHHHCCCHHHH		45.66-
268UbiquitinationITASEALKHPWICQR
CCHHHHHCCCCHHCH		55.45-
276PhosphorylationHPWICQRSTVASMMH
CCCHHCHHHHHHHHH		11.0130411139
277PhosphorylationPWICQRSTVASMMHR
CCHHCHHHHHHHHHH		23.4527097102
280PhosphorylationCQRSTVASMMHRQET
HCHHHHHHHHHHHHH		16.5927097102
287PhosphorylationSMMHRQETVDCLKKF
HHHHHHHHHHHHHHH		17.2029779826
292UbiquitinationQETVDCLKKFNARRK
HHHHHHHHHHHHHHH		62.74-
293UbiquitinationETVDCLKKFNARRKL
HHHHHHHHHHHHHHH		30.79-
299UbiquitinationKKFNARRKLKGAILT
HHHHHHHHHHHHHHH		49.34-
301UbiquitinationFNARRKLKGAILTTM
HHHHHHHHHHHHHHH		49.70-
306PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHHCC		12.2128432305
307PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCH		13.5228432305
311PhosphorylationILTTMLATRNFSAAK
HHHHHHHHCCHHHHH		23.3727097102
315PhosphorylationMLATRNFSAAKSLLK
HHHHCCHHHHHHHHC		30.7629779826
318AcetylationTRNFSAAKSLLKKPD
HCCHHHHHHHHCCCC		41.1622902405
319PhosphorylationRNFSAAKSLLKKPDG
CCHHHHHHHHCCCCC		33.9227097102
322UbiquitinationSAAKSLLKKPDGVKI
HHHHHHHCCCCCCEE		68.50-
328UbiquitinationLKKPDGVKINNKANV
HCCCCCCEECCCCCE		45.29-
330 (in isoform 5)Phosphorylation-37.9321630457
330 (in isoform 2)Phosphorylation-37.9321630457
331 (in isoform 5)Phosphorylation-48.5721630457
331 (in isoform 2)Phosphorylation-48.5721630457
332UbiquitinationDGVKINNKANVVTSP
CCCEECCCCCEECCC		36.53-
333 (in isoform 2)Phosphorylation-19.0424972320
333 (in isoform 5)Phosphorylation-19.0424972320
334 (in isoform 2)Phosphorylation-30.3324972320
334 (in isoform 5)Phosphorylation-30.3324972320
336 (in isoform 5)Phosphorylation-4.3822668510
336 (in isoform 2)Phosphorylation-4.3822668510
337 (in isoform 4)Phosphorylation-34.7227115346
337PhosphorylationNNKANVVTSPKENIP
CCCCCEECCCCCCCC		34.7225403869
337 (in isoform 7)Phosphorylation-34.7227115346
338PhosphorylationNKANVVTSPKENIPT
CCCCEECCCCCCCCC		23.5130411139
338 (in isoform 4)Phosphorylation-23.5127115346
338 (in isoform 7)Phosphorylation-23.5127115346
352PhosphorylationTPALEPQTTVIHNPD
CCCCCCCEEEEECCC		33.4730240740
364PhosphorylationNPDGNKESTESSNTT
CCCCCCCCCCCCCCC		38.8030240740
365PhosphorylationPDGNKESTESSNTTI
CCCCCCCCCCCCCCC		40.7628551015
367PhosphorylationGNKESTESSNTTIED
CCCCCCCCCCCCCCH		29.0428551015
368PhosphorylationNKESTESSNTTIEDE
CCCCCCCCCCCCCHH		31.7828551015
370PhosphorylationESTESSNTTIEDEDV
CCCCCCCCCCCHHHH		30.9722108457
371PhosphorylationSTESSNTTIEDEDVK
CCCCCCCCCCHHHHH		26.9822108457
470 (in isoform 5)Phosphorylation-35.8222673903
472 (in isoform 5)Phosphorylation-3.7022673903
474 (in isoform 5)Phosphorylation-18.9622673903
479AcetylationMDGNGMPKTMQSEET
CCCCCCCCCCCCCCC		47.9722902405
490 (in isoform 7)Phosphorylation-16.4322673903
492 (in isoform 7)Phosphorylation-44.1122673903
494 (in isoform 7)Phosphorylation-31.1522673903
504 (in isoform 6)Phosphorylation-34.7422673903
504PhosphorylationQNIHFHRSGSPTVPI
EEEEEECCCCCCCCC		34.7430181290
506 (in isoform 6)Phosphorylation-20.7422673903
506PhosphorylationIHFHRSGSPTVPIKP
EEEECCCCCCCCCCC		20.7430181290
508 (in isoform 6)Phosphorylation-40.3822673903
508PhosphorylationFHRSGSPTVPIKPPC
EECCCCCCCCCCCCC		40.3830181290
524PhosphorylationPNGKENFSGGTSLWQ
CCCCCCCCCCCCCCC		48.1423984901
527PhosphorylationKENFSGGTSLWQNI-
CCCCCCCCCCCCCC-		24.9523984901
528PhosphorylationENFSGGTSLWQNI--
CCCCCCCCCCCCC--		30.7723984901
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
287TPhosphorylationKinaseCAMK2DP15791
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
287TPhosphorylation

-
287TPhosphorylation

-
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 KCC2D_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NMDE2_RATGrin2bphysical
12147342
NMDE1_RATGrin2aphysical
12147342
SRF_HUMANSRFphysical
10753652
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2D_RAT

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Related Literatures of Post-Translational Modification

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