KCC2D_MOUSE - dbPTM
KCC2D_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2D_MOUSE
UniProt AC Q6PHZ2
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit delta
Gene Name Camk2d
Organism Mus musculus (Mouse).
Sequence Length 499
Subcellular Localization Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side . Sarcoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side .
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..
Protein Sequence MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALSKSNKPIHTIILNPHVHLVGDDAACIAYIRLTQYMDGSGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTVPIKPPCIPNGKENFSGGTSLWQNI
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-
3Phosphorylation-----MASTTTCTRF
-----CCCCCCCCCC		25.6226643407
4Phosphorylation----MASTTTCTRFT
----CCCCCCCCCCC		19.3126643407
5Phosphorylation---MASTTTCTRFTD
---CCCCCCCCCCCC		19.8526643407
6Phosphorylation--MASTTTCTRFTDE
--CCCCCCCCCCCCH		16.3926643407
8PhosphorylationMASTTTCTRFTDEYQ
CCCCCCCCCCCCHHH		27.0726643407
11PhosphorylationTTTCTRFTDEYQLFE
CCCCCCCCCHHHHHH		25.3226239621
14PhosphorylationCTRFTDEYQLFEELG
CCCCCCHHHHHHHHC		17.2126239621
26PhosphorylationELGKGAFSVVRRCMK
HHCCCHHHHHHHHCC		21.1118056256
43UbiquitinationTGQEYAAKIINTKKL
CCHHHHHHHHHHHCC		35.63-
48AcetylationAAKIINTKKLSARDH
HHHHHHHHCCCHHHH		47.427768865
48UbiquitinationAAKIINTKKLSARDH
HHHHHHHHCCCHHHH		47.42-
49UbiquitinationAKIINTKKLSARDHQ
HHHHHHHCCCHHHHH		45.71-
69UbiquitinationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.70-
79PhosphorylationNIVRLHDSISEEGFH
CEEEECCCCCCCCCE		19.78-
138UbiquitinationGIVHRDLKPENLLLA
CCCCCCCCHHHEEEE		55.35-
138AcetylationGIVHRDLKPENLLLA
CCCCCCCCHHHEEEE		55.3523806337
146PhosphorylationPENLLLASKSKGAAV
HHHEEEEECCCCCCE		37.1120415495
148PhosphorylationNLLLASKSKGAAVKL
HEEEEECCCCCCEEH		33.5529514104
182PhosphorylationAGTPGYLSPEVLRKD
CCCCCCCCHHHHHCC		15.5523737553
227UbiquitinationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11-
231PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCC		19.7325521595
235PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCCCCCC		35.1325521595
240PhosphorylationFPSPEWDTVTPEAKD
CCCCCCCCCCHHHHH		27.6124925903
242PhosphorylationSPEWDTVTPEAKDLI
CCCCCCCCHHHHHHH		19.9420415495
246UbiquitinationDTVTPEAKDLINKML
CCCCHHHHHHHHHHH		51.94-
251UbiquitinationEAKDLINKMLTINPA
HHHHHHHHHHCCCHH		28.44-
254PhosphorylationDLINKMLTINPAKRI
HHHHHHHCCCHHHCC		18.4018779572
259UbiquitinationMLTINPAKRITASEA
HHCCCHHHCCCHHHH		45.66-
264PhosphorylationPAKRITASEALKHPW
HHHCCCHHHHHCCCC		18.1128464351
268UbiquitinationITASEALKHPWICQR
CCHHHHHCCCCHHCH		55.45-
268AcetylationITASEALKHPWICQR
CCHHHHHCCCCHHCH		55.4522826441
273GlutathionylationALKHPWICQRSTVAS
HHCCCCHHCHHHHHH		2.1324333276
276PhosphorylationHPWICQRSTVASMMH
CCCHHCHHHHHHHHH		11.0125521595
277PhosphorylationPWICQRSTVASMMHR
CCHHCHHHHHHHHHH		23.4521183079
280PhosphorylationCQRSTVASMMHRQET
HCHHHHHHHHHHHHH		16.5926239621
281SulfoxidationQRSTVASMMHRQETV
CHHHHHHHHHHHHHH		1.5718455987
282SulfoxidationRSTVASMMHRQETVD
HHHHHHHHHHHHHHH		1.8718455987
287PhosphorylationSMMHRQETVDCLKKF
HHHHHHHHHHHHHHH		17.2025521595
292UbiquitinationQETVDCLKKFNARRK
HHHHHHHHHHHHHHH		62.74-
293UbiquitinationETVDCLKKFNARRKL
HHHHHHHHHHHHHHH		30.79-
299MethylationKKFNARRKLKGAILT
HHHHHHHHHHHHHHH		49.34-
301UbiquitinationFNARRKLKGAILTTM
HHHHHHHHHHHHHHH		49.70-
301MethylationFNARRKLKGAILTTM
HHHHHHHHHHHHHHH		49.70-
306PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHHCC		12.2120415495
307PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCH		13.5226824392
307O-linked_GlycosylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCH		13.524047699
308SulfoxidationKGAILTTMLATRNFS
HHHHHHHHHHHCCHH		1.7032749237
311PhosphorylationILTTMLATRNFSAAK
HHHHHHHHCCHHHHH		23.3729899451
315 (in isoform 4)Phosphorylation-30.7629514104
315PhosphorylationMLATRNFSAAKSLLK
HHHHCCHHHHHHHHC		30.7627087446
315 (in isoform 5)Phosphorylation-30.7629514104
318AcetylationTRNFSAAKSLLKKPD
HCCHHHHHHHHCCCC		41.1623806337
319PhosphorylationRNFSAAKSLLKKPDG
CCHHHHHHHHCCCCC		33.9227087446
319 (in isoform 4)Phosphorylation-33.9229514104
319 (in isoform 5)Phosphorylation-33.9229514104
330PhosphorylationKPDGVKESTESSNTT
CCCCCCCCCCCCCCC		31.5825521595
331PhosphorylationPDGVKESTESSNTTI
CCCCCCCCCCCCCCC		40.7625521595
332 (in isoform 4)Phosphorylation-62.5423737553
333PhosphorylationGVKESTESSNTTIED
CCCCCCCCCCCCCCH		29.0425521595
333 (in isoform 4)Phosphorylation-29.0423737553
334PhosphorylationVKESTESSNTTIEDE
CCCCCCCCCCCCCHH		31.7825521595
336PhosphorylationESTESSNTTIEDEDV
CCCCCCCCCCCHHHH		30.9725521595
337 (in isoform 5)Phosphorylation-26.9829899451
337PhosphorylationSTESSNTTIEDEDVK
CCCCCCCCCCHHHHH		26.9825521595
338 (in isoform 5)Phosphorylation-6.2125521595
344 (in isoform 4)Phosphorylation-55.5923737553
345 (in isoform 5)Phosphorylation-24.6129899451
345 (in isoform 4)Phosphorylation-24.6129514104
347 (in isoform 4)Phosphorylation-58.0823737553
348 (in isoform 4)Phosphorylation-41.3823737553
350 (in isoform 4)Phosphorylation-3.2423737553
351 (in isoform 4)Phosphorylation-2.6323737553
352 (in isoform 5)Phosphorylation-49.0923737553
353 (in isoform 5)Phosphorylation-5.1225521595
364 (in isoform 5)Phosphorylation-36.1723737553
365 (in isoform 5)Phosphorylation-40.0930352176
367 (in isoform 5)Phosphorylation-45.5723737553
368 (in isoform 5)Phosphorylation-19.7923737553
370 (in isoform 5)Phosphorylation-22.4523737553
371 (in isoform 5)Phosphorylation-28.7623737553
404PhosphorylationFYFENALSKSNKPIH
HHHHHHHCCCCCCCE		31.46-
441PhosphorylationLTQYMDGSGMPKTMQ
HHHHCCCCCCCCCCC		27.88-
470 (in isoform 2)Phosphorylation-34.7423737553
470PhosphorylationQNVHFHRSGSPTVPI
EEEEEECCCCCCCCC		34.7426643407
472PhosphorylationVHFHRSGSPTVPIKP
EEEECCCCCCCCCCC		20.7426643407
472 (in isoform 2)Phosphorylation-20.7423737553
474 (in isoform 2)Phosphorylation-40.3823737553
474PhosphorylationFHRSGSPTVPIKPPC
EECCCCCCCCCCCCC		40.3826643407
481GlutathionylationTVPIKPPCIPNGKEN
CCCCCCCCCCCCCCC		12.5424333276
484 (in isoform 4)Phosphorylation-55.0123737553
486 (in isoform 4)Phosphorylation-57.0023737553
488 (in isoform 4)Phosphorylation-39.6123737553
490PhosphorylationPNGKENFSGGTSLWQ
CCCCCCCCCCCCCCC		48.1423737553
493PhosphorylationKENFSGGTSLWQNI-
CCCCCCCCCCCCCC-		24.9523737553
494PhosphorylationENFSGGTSLWQNI--
CCCCCCCCCCCCC--		30.7727087446
504 (in isoform 5)Phosphorylation-23737553
506 (in isoform 5)Phosphorylation-23737553
508 (in isoform 5)Phosphorylation-23737553
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
287TPhosphorylationKinaseRIPK3Q9QZL0
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KCC2D_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2D_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND THR-337, ANDMASS SPECTROMETRY.
"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 THR-337, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory