dbPTM

AT1A1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AT1A1_RAT
UniProt AC	P06685
Protein Name	Sodium/potassium-transporting ATPase subunit alpha-1
Gene Name	Atp1a1
Organism	Rattus norvegicus (Rat).
Sequence Length	1023
Subcellular Localization	Cell membrane, sarcolemma Multi-pass membrane protein .
Protein Description	This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients..
Protein Sequence	MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYTKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Acetylation	GKGVGRDKYEPAAVS CCCCCCCCCCCCHHH	50.59	-
9	Ubiquitination	GKGVGRDKYEPAAVS CCCCCCCCCCCCHHH	50.59	-
10	Phosphorylation	KGVGRDKYEPAAVSE CCCCCCCCCCCHHHC	31.28	25403869
16	Phosphorylation	KYEPAAVSEHGDKKS CCCCCHHHCCCCHHC	21.10	14976217
21	Acetylation	AVSEHGDKKSKKAKK HHHCCCCHHCHHHHH	64.64	-
21	Ubiquitination	AVSEHGDKKSKKAKK HHHCCCCHHCHHHHH	64.64	-
22	Ubiquitination	VSEHGDKKSKKAKKE HHCCCCHHCHHHHHH	72.71	-
23	Phosphorylation	SEHGDKKSKKAKKER HCCCCHHCHHHHHHH	45.16	19286978
24	Ubiquitination	EHGDKKSKKAKKERD CCCCHHCHHHHHHHC	66.68	-
25	Ubiquitination	HGDKKSKKAKKERDM CCCHHCHHHHHHHCH	72.95	-
36	Ubiquitination	ERDMDELKKEVSMDD HHCHHHHHHHHCCCC	44.85	-
36	Acetylation	ERDMDELKKEVSMDD HHCHHHHHHHHCCCC	44.85	22902405
37	Ubiquitination	RDMDELKKEVSMDDH HCHHHHHHHHCCCCC	75.79	-
40	Phosphorylation	DELKKEVSMDDHKLS HHHHHHHCCCCCCCC	20.00	25403869
45	Ubiquitination	EVSMDDHKLSLDELH HHCCCCCCCCHHHHH	46.92	-
45	Acetylation	EVSMDDHKLSLDELH HHCCCCCCCCHHHHH	46.92	22902405
47	Phosphorylation	SMDDHKLSLDELHRK CCCCCCCCHHHHHHH	38.28	25403869
55	Phosphorylation	LDELHRKYGTDLSRG HHHHHHHHCCCCCCC	25.80	22108457
64	Phosphorylation	TDLSRGLTPARAAEI CCCCCCCCHHHHHHH	20.09	25403869
156	Acetylation	YQEAKSSKIMESFKN HHHHHHHHHHHHHHH	53.84	22902405
156	Ubiquitination	YQEAKSSKIMESFKN HHHHHHHHHHHHHHH	53.84	-
162	Ubiquitination	SKIMESFKNMVPQQA HHHHHHHHHCCCCCE	54.11	-
162	Acetylation	SKIMESFKNMVPQQA HHHHHHHHHCCCCCE	54.11	22902405
177	Ubiquitination	LVIRNGEKMSINAED EEEECCCCCEECHHH	39.07	-
179	Phosphorylation	IRNGEKMSINAEDVV EECCCCCEECHHHCE	24.61	22108457
212	Ubiquitination	IISANGCKVDNSSLT EEECCCCEECCCCCC	54.76	-
216	Phosphorylation	NGCKVDNSSLTGESE CCCEECCCCCCCCCC	23.43	29779826
217	Phosphorylation	GCKVDNSSLTGESEP CCEECCCCCCCCCCC	35.88	28689409
219	Phosphorylation	KVDNSSLTGESEPQT EECCCCCCCCCCCCC	40.63	27097102
222	Phosphorylation	NSSLTGESEPQTRSP CCCCCCCCCCCCCCC	56.79	27097102
226	Phosphorylation	TGESEPQTRSPDFTN CCCCCCCCCCCCCCC	43.78	22673903
228	Phosphorylation	ESEPQTRSPDFTNEN CCCCCCCCCCCCCCC	32.01	30411139
232	Phosphorylation	QTRSPDFTNENPLET CCCCCCCCCCCCCCC	49.34	28689409
239	Phosphorylation	TNENPLETRNIAFFS CCCCCCCCCCEEEEE	36.38	25575281
260	Phosphorylation	TARGIVVYTGDRTVM CCCEEEEECCCCCHH	8.29	22108457
261	Phosphorylation	ARGIVVYTGDRTVMG CCEEEEECCCCCHHH	22.46	28689409
366	Phosphorylation	KNLEAVETLGSTSTI CCHHHHHHHCCCCCC	29.80	28551015
369	Phosphorylation	EAVETLGSTSTICSD HHHHHHCCCCCCCCC	23.46	28551015
370	Phosphorylation	AVETLGSTSTICSDK HHHHHCCCCCCCCCC	28.26	28551015
371	Phosphorylation	VETLGSTSTICSDKT HHHHCCCCCCCCCCC	19.92	28551015
372	Phosphorylation	ETLGSTSTICSDKTG HHHCCCCCCCCCCCC	26.54	28551015
375	Phosphorylation	GSTSTICSDKTGTLT CCCCCCCCCCCCCCC	37.99	28551015
378	Phosphorylation	STICSDKTGTLTQNR CCCCCCCCCCCCCCC	40.15	22108457
380	Phosphorylation	ICSDKTGTLTQNRMT CCCCCCCCCCCCCEE	31.68	28551015
382	Phosphorylation	SDKTGTLTQNRMTVA CCCCCCCCCCCEEEE	24.52	28551015
387	Phosphorylation	TLTQNRMTVAHMWFD CCCCCCEEEEHHHCC	16.00	25403869
407	Phosphorylation	ADTTENQSGVSFDKT CCCCCCCCCCCCCHH	53.39	20841356
444	Ubiquitination	QENLPILKRAVAGDA HHCCHHHHHHHCCCC	38.74	-
444	Acetylation	QENLPILKRAVAGDA HHCCHHHHHHHCCCC	38.74	22902405
452	Phosphorylation	RAVAGDASESALLKC HHHCCCCCHHHHHHH	36.50	22108457
454	Phosphorylation	VAGDASESALLKCIE HCCCCCHHHHHHHHH	23.01	25403869
473	Acetylation	SVMEMREKYTKIVEI CHHHHHHHHEEEEEE	48.10	22902405
474	Phosphorylation	VMEMREKYTKIVEIP HHHHHHHHEEEEEEC	14.44	11859087
476	Acetylation	EMREKYTKIVEIPFN HHHHHHEEEEEECCC	41.48	22902405
484	Phosphorylation	IVEIPFNSTNKYQLS EEEECCCCCCCEEEE	33.46	27097102
485	Phosphorylation	VEIPFNSTNKYQLSI EEECCCCCCCEEEEE	36.51	27097102
487	Acetylation	IPFNSTNKYQLSIHK ECCCCCCCEEEEEEC	34.17	22902405
494	Ubiquitination	KYQLSIHKNPNASEP CEEEEEECCCCCCCC	72.87	-
494	Acetylation	KYQLSIHKNPNASEP CEEEEEECCCCCCCC	72.87	22902405
502	Acetylation	NPNASEPKHLLVMKG CCCCCCCCEEEEECC	42.72	22902405
508	Acetylation	PKHLLVMKGAPERIL CCEEEEECCCHHHHH	44.43	42259189
526	Ubiquitination	SSILLHGKEQPLDEE HHHHHCCCCCCCCHH	42.29	-
542	Phosphorylation	KDAFQNAYLELGGLG HHHHHHHHHHHCCHH	14.30	11859087
605	Ubiquitination	AVPDAVGKCRSAGIK CCCCHHHHHHHCCCE	21.63	-
612	Acetylation	KCRSAGIKVIMVTGD HHHHCCCEEEEEECC	25.45	22902405
625	Acetylation	GDHPITAKAIAKGVG CCCCCCHHHHHHCCE	31.51	42259201
629	Ubiquitination	ITAKAIAKGVGIISE CCHHHHHHCCEEEEC	48.27	-
635	Phosphorylation	AKGVGIISEGNETVE HHCCEEEECCCCCHH	37.21	25403869
640	Phosphorylation	IISEGNETVEDIAAR EEECCCCCHHHHHHH	32.94	28551015
661	Ubiquitination	QVNPRDAKACVVHGS HCCHHHCCEEEEECH	46.75	-
661	Succinylation	QVNPRDAKACVVHGS HCCHHHCCEEEEECH	46.75	-
661	Succinylation	QVNPRDAKACVVHGS HCCHHHCCEEEEECH	46.75	-
668	Phosphorylation	KACVVHGSDLKDMTS CEEEEECHHHCCCCH	25.54	-
671	Ubiquitination	VVHGSDLKDMTSEEL EEECHHHCCCCHHHH	50.90	-
671	Acetylation	VVHGSDLKDMTSEEL EEECHHHCCCCHHHH	50.90	22902405
675	Phosphorylation	SDLKDMTSEELDDIL HHHCCCCHHHHHHHH	23.57	22673903
684	Phosphorylation	ELDDILRYHTEIVFA HHHHHHHHHHEEEEE	15.06	25403869
722	Phosphorylation	TGDGVNDSPALKKAD ECCCCCCCHHHHHCC	13.58	30240740
726	Acetylation	VNDSPALKKADIGVA CCCCHHHHHCCCEEE	48.28	130349
726	Ubiquitination	VNDSPALKKADIGVA CCCCHHHHHCCCEEE	48.28	-
726	Methylation	VNDSPALKKADIGVA CCCCHHHHHCCCEEE	48.28	12692561
727	Acetylation	NDSPALKKADIGVAM CCCHHHHHCCCEEEE	52.74	130345
727	Ubiquitination	NDSPALKKADIGVAM CCCHHHHHCCCEEEE	52.74	-
727	Methylation	NDSPALKKADIGVAM CCCHHHHHCCCEEEE	52.74	12692561
773	Acetylation	RLIFDNLKKSIAYTL EECCCCHHHHHHHHH	51.21	22902405
773	Methylation	RLIFDNLKKSIAYTL EECCCCHHHHHHHHH	51.21	12692561
774	Acetylation	LIFDNLKKSIAYTLT ECCCCHHHHHHHHHH	50.70	22902405
774	Methylation	LIFDNLKKSIAYTLT ECCCCHHHHHHHHHH	50.70	12692561
843	Acetylation	PRNPKTDKLVNERLI CCCCCHHHHHHHHHH	60.61	22902405
843	Ubiquitination	PRNPKTDKLVNERLI CCCCCHHHHHHHHHH	60.61	-
943	Phosphorylation	ICKTRRNSVFQQGMK EECCCCCHHHHHHCC	23.61	7510709
1019	Acetylation	RPGGWVEKETYY--- CCCCCCCCCCCC---	45.82	22902405
1022	Phosphorylation	GWVEKETYY------ CCCCCCCCC------	14.31	-
1023	Phosphorylation	WVEKETYY------- CCCCCCCC-------	21.35	-

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
16	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
16	S	Phosphorylation	Kinase	PKC	-	Uniprot
16	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
16	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
16	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
16	S	Phosphorylation	Kinase	PRKCI	F1M7Y5	GPS
16	S	Phosphorylation	Kinase	MAPK3	P21708	GPS
16	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
16	S	Phosphorylation	Kinase	PRKCZ	P09217	GPS
23	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
23	S	Phosphorylation	Kinase	PKC	-	Uniprot
23	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
23	S	Phosphorylation	Kinase	PRKCZ	P09217	GPS
23	S	Phosphorylation	Kinase	PRKCI	F1M7Y5	GPS
23	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
23	S	Phosphorylation	Kinase	PKCA	P05696	PSP
23	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
943	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
943	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
943	S	Phosphorylation	Kinase	PKA	-	Uniprot
943	S	Phosphorylation	Kinase	PKACA	P17612	PSP
943	S	Phosphorylation	Kinase	PKACA	P00517	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
943	S	Phosphorylation		9435504
Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC.

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 AT1A1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COF1_RAT	Cfl1	physical	11139403
AT2B1_RAT	Atp2b1	physical	14593108
ANK3_RAT	Ank3	physical	14593108
FXYD4_MOUSE	Fxyd4	physical	15743908

Drug and Disease Associations

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

Regulatory Network of AT1A1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Insulin-induced stimulation of Na+,K(+)-ATPase activity in kidneyproximal tubule cells depends on phosphorylation of the alpha-subunitat Tyr-10."; Feraille E., Carranza M.L., Gonin S., Beguin P., Pedemonte C.,Rousselot M., Caverzasio J., Geering K., Martin P.Y., Favre H.; Mol. Biol. Cell 10:2847-2859(1999). Cited for: PHOSPHORYLATION AT TYR-10.	10473631 [Abstract]

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