dbPTM

PLM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLM_HUMAN
UniProt AC	O00168
Protein Name	Phospholemman {ECO:0000250\|UniProtKB:P56513}
Gene Name	FXYD1 {ECO:0000312\|HGNC:HGNC:4025}
Organism	Homo sapiens (Human).
Sequence Length	92
Subcellular Localization	Cell membrane, sarcolemma Single-pass type I membrane protein . Apical cell membrane Single-pass type I membrane protein . Membrane, caveola . Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and inte
Protein Description	Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone..
Protein Sequence	MASLGHILVFCVGLLTMAKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSTRRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Phosphorylation	VFCVGLLTMAKAESP HHHHHHHHHHHCCCC	21.81	24719451
44	Alanine amide	QIGGLVIAGILFILG HHHHHHHHHHHHHHH	7.47	-
44	Amidation	QIGGLVIAGILFILG HHHHHHHHHHHHHHH	7.47	18052119
60	S-palmitoylation	LIVLSRRCRCKFNQQ HHHHHHHCCCCCCCC	6.10	25422474
62	Glutathionylation	VLSRRCRCKFNQQQR HHHHHCCCCCCCCCC	7.26	-
62	S-palmitoylation	VLSRRCRCKFNQQQR HHHHHCCCCCCCCCC	7.26	25422474
70	Phosphorylation	KFNQQQRTGEPDEEE CCCCCCCCCCCCCCC	41.37	26437602
79	Phosphorylation	EPDEEEGTFRSSIRR CCCCCCCCHHHHHHH	21.10	24972180
82	Phosphorylation	EEEGTFRSSIRRLST CCCCCHHHHHHHHHH	26.40	24972180
83	Phosphorylation	EEGTFRSSIRRLSTR CCCCHHHHHHHHHHC	18.83	15621037
88	Phosphorylation	RSSIRRLSTRRR--- HHHHHHHHHCCC---	20.32	15621037
89	Phosphorylation	SSIRRLSTRRR---- HHHHHHHHCCC----	32.55	27282143

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
83	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
83	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
83	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
83	S	Phosphorylation	Kinase	PKA	-	Uniprot
83	S	Phosphorylation	Kinase	PKC	-	Uniprot
83	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
88	S	Phosphorylation	Kinase	PKACA	P17612	PSP
88	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
88	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
88	S	Phosphorylation	Kinase	PKCA	P05696	PSP
88	S	Phosphorylation	Kinase	PKA	-	Uniprot
89	T	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
83	S	Phosphorylation	10811636
Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3 (By similarity).
88	S	Palmitoylation	21868384
Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA.
88	S	Phosphorylation	21868384
Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA.
88	S	Phosphorylation	21868384
Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity (By similarity).

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 PLM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NDRG1_HUMAN	NDRG1	physical	28514442
NDRG3_HUMAN	NDRG3	physical	28514442
NDRG4_HUMAN	NDRG4	physical	28514442
THNS1_HUMAN	THNSL1	physical	28514442
GFRP_HUMAN	GCHFR	physical	28514442
VATD_HUMAN	ATP6V1D	physical	28514442
GOPC_HUMAN	GOPC	physical	28514442
F204A_HUMAN	FAM204A	physical	28514442
PRDC1_HUMAN	PRTFDC1	physical	28514442
DPOE4_HUMAN	POLE4	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLM_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"The inhibitory effect of phospholemman on the sodium pump requiresits palmitoylation."; Tulloch L.B., Howie J., Wypijewski K.J., Wilson C.R., Bernard W.G.,Shattock M.J., Fuller W.; J. Biol. Chem. 286:36020-36031(2011). Cited for: PALMITOYLATION AT CYS-60 AND CYS-62, PHOSPHORYLATION AT SER-88, ANDMUTAGENESIS OF CYS-60 AND CYS-62.	21868384 [Abstract]
Phosphorylation
Reference	PubMed
"The inhibitory effect of phospholemman on the sodium pump requiresits palmitoylation."; Tulloch L.B., Howie J., Wypijewski K.J., Wilson C.R., Bernard W.G.,Shattock M.J., Fuller W.; J. Biol. Chem. 286:36020-36031(2011). Cited for: PALMITOYLATION AT CYS-60 AND CYS-62, PHOSPHORYLATION AT SER-88, ANDMUTAGENESIS OF CYS-60 AND CYS-62.	21868384 [Abstract]