PPLA_HUMAN - dbPTM
PPLA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPLA_HUMAN
UniProt AC P26678
Protein Name Cardiac phospholamban
Gene Name PLN
Organism Homo sapiens (Human).
Sequence Length 52
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Sarcoplasmic reticulum membrane
Single-pass membrane protein . Mitochondrion membrane
Single-pass membrane protein . Membrane
Single-pass membrane protein . Colocalizes with HAX1 a
Protein Description Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation..
Protein Sequence MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL
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
1Acetylation-------MEKVQYLT
-------CHHHHHHH
11.53-
8PhosphorylationMEKVQYLTRSAIRRA
CHHHHHHHHHHHHHH
20.0426437602
10PhosphorylationKVQYLTRSAIRRAST
HHHHHHHHHHHHHHH
23.8622210691
16PhosphorylationRSAIRRASTIEMPQQ
HHHHHHHHHCCCCHH
28.273759968
17PhosphorylationSAIRRASTIEMPQQA
HHHHHHHHCCCCHHH
21.703759968
36S-palmitoylationQNLFINFCLILICLL
HHHHHHHHHHHHHHH
1.68-

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
16SPhosphorylationKinaseDMPKQ09013
Uniprot
16SPhosphorylationKinasePRKACAP17612
GPS
16SPhosphorylationKinaseCAMK2DQ13557
GPS
16SPhosphorylationKinasePKA-FAMILY-GPS
16SPhosphorylationKinasePKA-Uniprot
16SPhosphorylationKinasePKA_GROUP-PhosphoELM
17TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
17TPhosphorylationKinaseCAMK2BQ13554
GPS
17TPhosphorylationKinaseCAMK2DQ13557
GPS
17TPhosphorylationKinaseCAMK2-Uniprot
17TPhosphorylationKinaseCCDPK-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
17TPhosphorylation

16690701

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 PPLA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT2A1_HUMANATP2A1physical
12032137
AT2A2_HUMANATP2A2physical
12032137
SARCO_HUMANSLNphysical
12032137
AT2A1_HUMANATP2A1physical
10551848
AT2A1_HUMANATP2A1physical
11526231
PPR3A_HUMANPPP1R3Aphysical
9845327
AT2A2_HUMANATP2A2physical
10809745
LRAD1_HUMANLDLRAD1physical
24722188
TMM79_HUMANTMEM79physical
24722188
EDA_HUMANEDAphysical
24722188
DMPK_HUMANDMPKphysical
15598648

Drug and Disease Associations
Kegg Disease
H00294 Dilated cardiomyopathy (DCM)
OMIM Disease
609909Cardiomyopathy, dilated 1P (CMD1P)
613874Cardiomyopathy, familial hypertrophic 18 (CMH18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPLA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Myotonic dystrophy protein kinase phosphorylates phospholamban andregulates calcium uptake in cardiomyocyte sarcoplasmic reticulum.";
Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C.,Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.;
J. Biol. Chem. 280:8016-8021(2005).
Cited for: PHOSPHORYLATION AT SER-16 BY DMPK.
"Ca2+-calmodulin-dependent protein kinase expression and signalling inskeletal muscle during exercise.";
Rose A.J., Kiens B., Richter E.A.;
J. Physiol. (Lond.) 574:889-903(2006).
Cited for: PHOSPHORYLATION AT THR-17 BY CAMK2.

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