AT1A2_HUMAN - dbPTM
AT1A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT1A2_HUMAN
UniProt AC P50993
Protein Name Sodium/potassium-transporting ATPase subunit alpha-2
Gene Name ATP1A2
Organism Homo sapiens (Human).
Sequence Length 1020
Subcellular Localization Membrane
Multi-pass membrane protein . Cell membrane
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, providing the energy for active transport of various nutrients..
Protein Sequence MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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
9PhosphorylationGRGAGREYSPAATTA
CCCCCCCCCCCCCCC		20.7024927040
10PhosphorylationRGAGREYSPAATTAE
CCCCCCCCCCCCCCC		11.8724076635
14PhosphorylationREYSPAATTAENGGG
CCCCCCCCCCCCCCC		28.7520071362
15PhosphorylationEYSPAATTAENGGGK
CCCCCCCCCCCCCCC		27.5220071362
43UbiquitinationEVAMDDHKLSLDELG
HHCCCCCCCCHHHHC		46.92-
45PhosphorylationAMDDHKLSLDELGRK
CCCCCCCCHHHHCHH		38.28-
58PhosphorylationRKYQVDLSKGLTNQR
HHHCCCCCCCCCCHH		21.8825307156
79PhosphorylationRDGPNALTPPPTTPE
CCCCCCCCCCCCCHH		31.19-
153O-linked_GlycosylationYYQEAKSSKIMDSFK
HHHHHHHCHHHHHHH		26.0429351928
214PhosphorylationHGCKVDNSSLTGESE
CCCEECCCCCCCCCC		23.4323401153
215PhosphorylationGCKVDNSSLTGESEP
CCEECCCCCCCCCCC		35.8823927012
217PhosphorylationKVDNSSLTGESEPQT
EECCCCCCCCCCCCC		40.6323927012
220PhosphorylationNSSLTGESEPQTRSP
CCCCCCCCCCCCCCC		56.7923927012
224PhosphorylationTGESEPQTRSPEFTH
CCCCCCCCCCCCCCC		43.7818510355
226PhosphorylationESEPQTRSPEFTHEN
CCCCCCCCCCCCCCC		31.9724076635
259PhosphorylationARGIVIATGDRTVMG
CCEEEEECCCCCHHH		28.6120068231
263PhosphorylationVIATGDRTVMGRIAT
EEECCCCCHHHHHHH		21.4225332170
273PhosphorylationGRIATLASGLEVGRT
HHHHHHHHCCCCCCC		47.20-
357UbiquitinationARKNCLVKNLEAVET
HHCCCEECCHHHHHH		42.7521890473
367PhosphorylationEAVETLGSTSTICSD
HHHHHHCCCCCCCCC		23.4628857561
368PhosphorylationAVETLGSTSTICSDK
HHHHHCCCCCCCCCC		28.2628857561
369PhosphorylationVETLGSTSTICSDKT
HHHHCCCCCCCCCCC		19.9228857561
370PhosphorylationETLGSTSTICSDKTG
HHHCCCCCCCCCCCC		26.5428857561
373PhosphorylationGSTSTICSDKTGTLT
CCCCCCCCCCCCCCC		37.9928857561
375UbiquitinationTSTICSDKTGTLTQN
CCCCCCCCCCCCCCC		32.3421890473
376PhosphorylationSTICSDKTGTLTQNR
CCCCCCCCCCCCCCC		40.1528857561
378PhosphorylationICSDKTGTLTQNRMT
CCCCCCCCCCCCCEE		31.6828857561
380PhosphorylationSDKTGTLTQNRMTVA
CCCCCCCCCCCEEEE		24.5228857561
439PhosphorylationKAGQENISVSKRDTA
HCCHHCCCCCCCCCC		31.7420886841
450PhosphorylationRDTAGDASESALLKC
CCCCCCCCHHHHHHH		36.5024076635
452PhosphorylationTAGDASESALLKCIE
CCCCCCHHHHHHHHH		23.0125332170
464PhosphorylationCIELSCGSVRKMRDR
HHHHHCCCHHHHHCC		24.0726437602
486PhosphorylationPFNSTNKYQLSIHER
CCCCCCCEEEEEEEC		19.4326437602
496PhosphorylationSIHEREDSPQSHVLV
EEEECCCCCCCEEEE		21.7826437602
499PhosphorylationEREDSPQSHVLVMKG
ECCCCCCCEEEEECC		20.9625307156
539PhosphorylationQDAFQNAYMELGGLG
HHHHHHHHHHHCCHH		9.9324927040
559PhosphorylationFCQLNLPSGKFPRGF
EEEECCCCCCCCCCC		58.7524719451
570PhosphorylationPRGFKFDTDELNFPT
CCCCCCCHHHCCCCH		34.2118669648
587PhosphorylationLCFVGLMSMIDPPRA
HHHHHHHHCCCCCHH		20.0318669648
602UbiquitinationAVPDAVGKCRSAGIK
CCCCHHHHHHHCCCE		21.6321890473
605PhosphorylationDAVGKCRSAGIKVIM
CHHHHHHHCCCEEEE		40.0720068231
609UbiquitinationKCRSAGIKVIMVTGD
HHHHCCCEEEEEECC		25.4521890473
614PhosphorylationGIKVIMVTGDHPITA
CCEEEEEECCCCCCH		21.3620068231
620PhosphorylationVTGDHPITAKAIAKG
EECCCCCCHHHHHHC		26.9320068231
622UbiquitinationGDHPITAKAIAKGVG
CCCCCCHHHHHHCCE		31.5121890473
626UbiquitinationITAKAIAKGVGIISE
CCHHHHHHCCEEEEC		48.2721890473
632PhosphorylationAKGVGIISEGNETVE
HHCCEEEECCCCCHH		37.2125072903
637PhosphorylationIISEGNETVEDIAAR
EEECCCCCHHHHHHH		32.9424076635
650PhosphorylationARLNIPMSQVNPREA
HHCCCCHHHCCHHHC		26.1421082442
660S-palmitoylationNPREAKACVVHGSDL
CHHHCCEEEEECHHH		3.0226865113
665PhosphorylationKACVVHGSDLKDMTS
CEEEEECHHHHCCCH		25.5425332170
672PhosphorylationSDLKDMTSEQLDEIL
HHHHCCCHHHHHHHH		19.39-
695UbiquitinationARTSPQQKLIIVEGC
EECCCCCEEEEEECC		36.0821890473
702S-palmitoylationKLIIVEGCQRQGAIV
EEEEEECCCCCCCEE		1.5829575903
712PhosphorylationQGAIVAVTGDGVNDS
CCCEEEEECCCCCCC		21.5924076635
719PhosphorylationTGDGVNDSPALKKAD
ECCCCCCCHHHHHCC		13.5829255136
723UbiquitinationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE		48.2821890473
724UbiquitinationNDSPALKKADIGIAM
CCCHHHHHCCEEEEC		52.74-
770UbiquitinationRLIFDNLKKSIAYTL
EECCCCHHHHHHHHH		51.2121890473
826PhosphorylationLAYEAAESDIMKRQP
HHHHHHHHHHHHCCC		27.92-
830UbiquitinationAAESDIMKRQPRNSQ
HHHHHHHHCCCCCCH		48.49-
840UbiquitinationPRNSQTDKLVNERLI
CCCCHHHHHHHHHHH		58.6921890473
845MethylationTDKLVNERLISMAYG
HHHHHHHHHHHHHHH		31.92-
845DimethylationTDKLVNERLISMAYG
HHHHHHHHHHHHHHH		31.92-
904PhosphorylationDSYGQEWTYEQRKVV
HHCCCCCCHHHHHEE		19.21-
905PhosphorylationSYGQEWTYEQRKVVE
HCCCCCCHHHHHEEE		15.90-
940PhosphorylationICKTRRNSVFQQGMK
EECCCCCHHHHHHHC		23.6125954137
947UbiquitinationSVFQQGMKNKILIFG
HHHHHHHCCCHHEEC		63.0121890473
949UbiquitinationFQQGMKNKILIFGLL
HHHHHCCCHHEECCC		33.11-
1018PhosphorylationGGWVEKETYY-----
CCCEEEEECC-----		38.91-
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
940SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT1A2_HUMAN !!
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 AT1A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VA0D1_HUMANATP6V0D1physical
26344197
VATA_HUMANATP6V1Aphysical
26344197
TCPH_HUMANCCT7physical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
Drug and Disease Associations
Kegg Disease
H00775 Familial or sporadic hemiplegic migraine
H00998 Alternating hemiplegia of childhood
OMIM Disease
602481Migraine, familial hemiplegic, 2 (FHM2)
104290Alternating hemiplegia of childhood 1 (AHC1)
Kegg Drug
D00112 G-Strophanthin (JAN); Ouabain; Ouabain octahydrate
D00297 Digitoxin (JP16/USP/INN); Crystodigin (TN)
D00298 Digoxin (JP16/USP); Lanoxicaps (TN); Lanoxin (TN)
D01240 Deslanoside (JP16/USP/INN); Cedilanid-d (TN)
D01379 Proscillaridin (JAN/USAN/INN); Talusin (TN)
D01972 Lanatoside C (JP16/INN); Digilanogen C (TN)
D02587 Metildigoxin (JP16); Lanirapid (TN)
D06881 Acetyldigitoxin (INN); Acylanid (TN)
D07147 Gitoformate (INN)
D07555 Acetyldigoxin; Cedigossima (TN)
D07556 beta-Acetyldigoxin; Acetyldigoxin beta isomer; Corotal (TN)
D09847 Metildigoxin (INN); Medigoxin (BAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT1A2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-570 AND SER-587, ANDMASS SPECTROMETRY.

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