Overview
| Uniprot ID | Q95266 |
|---|
| Protein Name | Calcium/calmodulin-dependent protein kinase type II subunit delta |
|---|
| Gene Name | CAMK2D |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 147 |
ENLLLASKSKGAAVK |
Function
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. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity)
Protein Sequence
10
MASTTTCTRF
20
TDEYQLFEEL
30
GKGAFSVVRR
40
CMKIPTGQEY
50
AAKIINTKKL
60
SARDHQKLER
70
EARICRLLKH
80
PNIVRLHDSI
90
SEEGFHYLVF
100
DLVTGGELFE
110
DIVAREYYSE
120
ADASHCIQQI
130
LESVNHCHLN
140
GIVHRDLKPE
150
NLLLASKSKG
160
AAVKLADFGL
170
AIEVQGDQQA
180
WFGFAGTPGY
190
LSPEVLRKDP
200
YGKPVDMWAC
210
GVILYILLVG
220
YPPFWDEDQH
230
RLYQQIKAGA
240
YDFPSPEWDT
250
VTPEAKDLIN
260
KMLTINPAKR
270
ITASEALKHP
280
WICQRSTVAS
290
MMHRQETVDC
300
LKKFNARRKL
310
KGAILTTMLA
320
TRNFSAAKSL
330
LKKPDGVKES
340
TESSNTTIED
350
EDVKARKQEI
360
IKVTEQLIEA
370
INNGDFEAYT
380
KICDPGLTAF
390
EPEALGNLVE
400
GMDFHRFYFE
410
NALSKSNKPI
420
HTIILNPHVH
430
LVGDDAACIA
440
YIRLTQYMDG
450
SGMPKTMQSE
460
ETRVWHRRDG
470
KWQNVHFHRS
480
GSPTVPIKPS
490
CIPNGKENFS
GSTSLWQNI
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0043005 |
neuron projection |
| Cellular Component |
GO:0014069 |
postsynaptic density |
| Cellular Component |
GO:0042383 |
sarcolemma |
| Cellular Component |
GO:0033017 |
sarcoplasmic reticulum membrane |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0004683 |
calcium/calmodulin-dependent protein kinase activity |
| Molecular Function |
GO:0005516 |
calmodulin binding |
| Molecular Function |
GO:0106310 |
protein serine kinase activity |
| Biological Process |
GO:0010613 |
positive regulation of cardiac muscle hypertrophy |
| Biological Process |
GO:0006468 |
protein phosphorylation |
| Biological Process |
GO:0060341 |
regulation of cellular localization |
| Biological Process |
GO:0048168 |
regulation of neuronal synaptic plasticity |
| Biological Process |
GO:1903076 |
regulation of protein localization to plasma membrane |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.