Ser16
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Home > Phosphorylation Site Page: > Ser16  -  PLB (rat)

Site Information
RSAIRRAstIEMPQQ   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448114

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 20 ) , mass spectrometry ( 4 ) , mutation of modification site ( 15 ) , phospho-antibody ( 1 , 2 , 3 , 5 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 ) , western blotting ( 1 , 2 , 3 , 5 , 7 , 8 , 9 , 10 , 16 , 18 , 19 )
Relevant cell line - cell type - tissue:
'heart, ventricle' ( 1 ) , heart ( 2 , 3 , 4 , 5 , 10 , 12 , 16 , 20 ) , intestine ( 4 ) , lung ( 4 ) , muscle ( 4 ) , myocardium ( 2 ) , myocyte ( 1 ) , myocyte-heart ( 5 , 7 , 8 , 9 , 11 , 14 , 15 , 17 , 18 , 19 ) , stomach ( 4 )

Upstream Regulation
Regulatory protein:
ADCY6 (mouse) ( 8 ) , Akt1 (human) ( 8 ) , PMCA4 iso2 (human) ( 7 ) , PRKD1 (mouse) ( 9 )
Putative in vivo kinases:
Akt1 (rat) ( 8 ) , PKACA (rat) ( 11 )
Kinases, in vitro:
Akt1 (human) ( 8 )
Putative upstream phosphatases:
PPP1CA (human) ( 5 )
Treatments:
8-Rp-cAMP ( 8 ) , acidosis ( 16 ) , Akt-I-1 ( 8 ) , Akt-I-1,2 ( 8 ) , aortic banding ( 2 ) , Bay 60-7550 ( 1 ) , bradykinin ( 13 ) , Ca(2+) ( 16 , 20 ) , ciclosporin ( 5 , 11 ) , colforsin ( 8 ) , CPA ( 8 ) , electrical_stimulation ( 12 , 18 ) , endothelin ( 9 ) , exercise ( 10 ) , FK506 ( 5 ) , Go_6976 ( 5 ) , H-89 ( 8 , 11 , 16 ) , hypertension ( 17 ) , ICI-118,551 ( 8 ) , inhibitor-1 ( 3 ) , ischemia ( 5 , 15 ) , ischemia/reperfusion ( 15 ) , isoproterenol ( 1 , 7 , 8 , 9 , 11 , 12 , 16 , 20 ) , liothyronine ( 19 ) , low_pH ( 20 ) , nifedipine ( 16 ) , norepinephrine ( 14 , 18 ) , okadaic_acid ( 11 , 16 ) , PKI ( 8 ) , prazosin ( 14 , 18 ) , propranolol ( 15 ) , serum ( 8 ) , SMLT ( 7 )

Downstream Regulation
Effects of modification on PLB:
activity, induced ( 5 ) , enzymatic activity, induced ( 1 , 2 )

Disease / Diagnostics Relevance
Relevant diseases:
hypertrophic cardiomyopathy ( 2 )

References 

1

Wang YW, et al. (2021) Bay 60-7550, a PDE2 inhibitor, exerts positive inotropic effect of rat heart by increasing PKA-mediated phosphorylation of phospholamban. Eur J Pharmacol 901, 174077
33798601   Curated Info

2

Mazeto IFS, et al. (2021) Calcium homeostasis behavior and cardiac function on left ventricular remodeling by pressure overload. Braz J Med Biol Res 54, e10138
33624728   Curated Info

3

Pritchard TJ, et al. (2013) Active inhibitor-1 maintains protein hyper-phosphorylation in aging hearts and halts remodeling in failing hearts. PLoS One 8, e80717
24312496   Curated Info

4

Lundby A, et al. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun 3, 876
22673903   Curated Info

5

Shintani-Ishida K, Yoshida K (2011) Ischemia induces phospholamban dephosphorylation via activation of calcineurin, PKC-α, and protein phosphatase 1, thereby inducing calcium overload in reperfusion. Biochim Biophys Acta 1812, 743-51
21447388   Curated Info

6

Yokoe S, et al. (2010) Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy. Glycobiology 20, 1217-26
20484118   Curated Info

7

Mohamed TM, et al. (2009) Specific role of neuronal nitric-oxide synthase when tethered to the plasma membrane calcium pump in regulating the beta-adrenergic signal in the myocardium. J Biol Chem 284, 12091-8
19278978   Curated Info

8

Gao MH, et al. (2008) Adenylyl cyclase type VI increases Akt activity and phospholamban phosphorylation in cardiac myocytes. J Biol Chem 283, 33527-35
18838385   Curated Info

9

Cuello F, et al. (2007) Protein kinase D selectively targets cardiac troponin I and regulates myofilament Ca2+ sensitivity in ventricular myocytes. Circ Res 100, 864-73
17322173   Curated Info

10

Kolwicz SC, et al. (2007) Effects of forskolin on inotropic performance and phospholamban phosphorylation in exercise-trained hypertensive myocardium. J Appl Physiol 102, 628-33
17082376   Curated Info

11

El-Armouche A, et al. (2006) Role of calcineurin and protein phosphatase-2A in the regulation of phosphatase inhibitor-1 in cardiac myocytes. Biochem Biophys Res Commun 346, 700-6
16774736   Curated Info

12

Valverde CA, et al. (2005) Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation. J Physiol 562, 801-13
15528241   Curated Info

13

Tschöpe C, et al. (2004) Improvement of defective sarcoplasmic reticulum Ca2+ transport in diabetic heart of transgenic rats expressing the human kallikrein-1 gene. FASEB J 18, 1967-9
15448111   Curated Info

14

Wang W, et al. (2004) Sustained beta1-adrenergic stimulation modulates cardiac contractility by Ca2+/calmodulin kinase signaling pathway. Circ Res 95, 798-806
15375008   Curated Info

15

Said M, et al. (2003) Role of dual-site phospholamban phosphorylation in the stunned heart: insights from phospholamban site-specific mutants. Am J Physiol Heart Circ Physiol 285, H1198-205
12763747   Curated Info

16

Said M, Mundiña-Weilenmann C, Vittone L, Mattiazzi A (2002) The relative relevance of phosphorylation of the Thr(17) residue of phospholamban is different at different levels of beta-adrenergic stimulation. Pflugers Arch 444, 801-9
12355181   Curated Info

17

Bokník P, et al. (2001) Enhanced protein phosphorylation in hypertensive hypertrophy. Cardiovasc Res 51, 717-28
11530105   Curated Info

18

Hagemann D, et al. (2000) Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes. J Biol Chem 275, 22532-6
10825152   Curated Info

19

Ojamaa K, Kenessey A, Klein I (2000) Thyroid hormone regulation of phospholamban phosphorylation in the rat heart. Endocrinology 141, 2139-44
10830301   Curated Info

20

Vittone L, Mundiña-Weilenmann C, Said M, Mattiazzi A (1998) Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart. J Biol Chem 273, 9804-11
9545319   Curated Info