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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MEKVQYLT -------CHHHHHHH | 11.53 | - | |
8 | Phosphorylation | MEKVQYLTRSAIRRA CHHHHHHHHHHHHHH | 20.04 | 26437602 | |
10 | Phosphorylation | KVQYLTRSAIRRAST HHHHHHHHHHHHHHH | 23.86 | 22210691 | |
16 | Phosphorylation | RSAIRRASTIEMPQQ HHHHHHHHHCCCCHH | 28.27 | 3759968 | |
17 | Phosphorylation | SAIRRASTIEMPQQA HHHHHHHHCCCCHHH | 21.70 | 3759968 | |
36 | S-palmitoylation | QNLFINFCLILICLL HHHHHHHHHHHHHHH | 1.68 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
16 | S | Phosphorylation | Kinase | DMPK | Q09013 | Uniprot |
16 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
16 | S | Phosphorylation | Kinase | CAMK2D | Q13557 | GPS |
16 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
16 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
16 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
17 | T | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
17 | T | Phosphorylation | Kinase | CAMK2B | Q13554 | GPS |
17 | T | Phosphorylation | Kinase | CAMK2D | Q13557 | GPS |
17 | T | Phosphorylation | Kinase | CAMK2 | - | Uniprot |
17 | T | Phosphorylation | Kinase | CCDPK | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
17 | T | Phosphorylation |
| 16690701 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AT2A1_HUMAN | ATP2A1 | physical | 12032137 | |
AT2A2_HUMAN | ATP2A2 | physical | 12032137 | |
SARCO_HUMAN | SLN | physical | 12032137 | |
AT2A1_HUMAN | ATP2A1 | physical | 10551848 | |
AT2A1_HUMAN | ATP2A1 | physical | 11526231 | |
PPR3A_HUMAN | PPP1R3A | physical | 9845327 | |
AT2A2_HUMAN | ATP2A2 | physical | 10809745 | |
LRAD1_HUMAN | LDLRAD1 | physical | 24722188 | |
TMM79_HUMAN | TMEM79 | physical | 24722188 | |
EDA_HUMAN | EDA | physical | 24722188 | |
DMPK_HUMAN | DMPK | physical | 15598648 |
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Phosphorylation | |
Reference | PubMed |
"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. |