AT1A2_MOUSE - dbPTM
AT1A2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT1A2_MOUSE
UniProt AC Q6PIE5
Protein Name Sodium/potassium-transporting ATPase subunit alpha-2
Gene Name Atp1a2
Organism Mus musculus (Mouse).
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 ions, providing the energy for active transport of various nutrients (By similarity)..
Protein Sequence MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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
20.7025521595
10PhosphorylationRGAGREYSPAATTAE
CCCCCCCCCCCCCCC
11.8725521595
14PhosphorylationREYSPAATTAENGGG
CCCCCCCCCCCCCCC
28.7520415495
15PhosphorylationEYSPAATTAENGGGK
CCCCCCCCCCCCCCC
27.5220415495
28UbiquitinationGKKKQKEKELDELKK
CCCCHHHHHHHHHHH
71.29-
35UbiquitinationKELDELKKEVAMDDH
HHHHHHHHHHCCCCC
70.78-
43UbiquitinationEVAMDDHKLSLDELG
HHCCCCCCCCHHHHC
46.92-
45PhosphorylationAMDDHKLSLDELGRK
CCCCCCCCHHHHCHH
38.2829899451
52UbiquitinationSLDELGRKYQVDLSK
CHHHHCHHHCCCCCC
37.93-
58PhosphorylationRKYQVDLSKGLTNQR
HHHCCCCCCCCCCHH
21.8825521595
59UbiquitinationKYQVDLSKGLTNQRA
HHCCCCCCCCCCHHH
66.30-
79PhosphorylationRDGPNALTPPPTTPE
CCCCCCCCCCCCCHH
31.1922817900
83PhosphorylationNALTPPPTTPEWVKF
CCCCCCCCCHHHHHH
61.8420415495
84PhosphorylationALTPPPTTPEWVKFC
CCCCCCCCHHHHHHH
25.6125521595
91S-palmitoylationTPEWVKFCRQLFGGF
CHHHHHHHHHHHCHH
1.9428680068
124PhosphorylationAAMEDEPSNDNLYLG
HHCCCCCCCCCHHHH
55.56-
154UbiquitinationYQEAKSSKIMDSFKN
HHHHHHCHHHHHHHH
49.49-
160UbiquitinationSKIMDSFKNMVPQQA
CHHHHHHHHCCCCEE
48.35-
175UbiquitinationLVIREGEKMQINAEE
EEEECCCEEEECCEE
47.14-
192UbiquitinationVGDLVEVKGGDRVPA
EECEEEEECCCCCCC
43.61-
205PhosphorylationPADLRIISSHGCKVD
CCCEEEEECCCCEEC
17.5722817900
206PhosphorylationADLRIISSHGCKVDN
CCEEEEECCCCEECC
17.3129899451
209S-nitrosocysteineRIISSHGCKVDNSSL
EEEECCCCEECCCCC
3.04-
209S-nitrosylationRIISSHGCKVDNSSL
EEEECCCCEECCCCC
3.0424895380
210UbiquitinationIISSHGCKVDNSSLT
EEECCCCEECCCCCC
58.16-
214PhosphorylationHGCKVDNSSLTGESE
CCCEECCCCCCCCCC
23.4330635358
215PhosphorylationGCKVDNSSLTGESEP
CCEECCCCCCCCCCC
35.8825521595
217PhosphorylationKVDNSSLTGESEPQT
EECCCCCCCCCCCCC
40.6327742792
220PhosphorylationNSSLTGESEPQTRSP
CCCCCCCCCCCCCCC
56.7925521595
224PhosphorylationTGESEPQTRSPEFTH
CCCCCCCCCCCCCCC
43.7825521595
226PhosphorylationESEPQTRSPEFTHEN
CCCCCCCCCCCCCCC
31.9725521595
241S-nitrosylationPLETRNICFFSTNCV
CCCCCCEEEEECCCC
3.0024895380
247S-nitrosylationICFFSTNCVEGTARG
EEEEECCCCCCCCCE
2.7424895380
270PhosphorylationTVMGRIATLASGLEV
CHHHHHHHHHHCCCC
22.08-
273PhosphorylationGRIATLASGLEVGQT
HHHHHHHHCCCCCCC
47.20-
357UbiquitinationARKNCLVKNLEAVET
HHCCCEECCHHHHHH
42.75-
364PhosphorylationKNLEAVETLGSTSTI
CCHHHHHHHCCCCCC
29.8023140645
367PhosphorylationEAVETLGSTSTICSD
HHHHHHCCCCCCCCC
23.4625521595
368PhosphorylationAVETLGSTSTICSDK
HHHHHCCCCCCCCCC
28.2624925903
369PhosphorylationVETLGSTSTICSDKT
HHHHCCCCCCCCCCC
19.9223140645
370PhosphorylationETLGSTSTICSDKTG
HHHCCCCCCCCCCCC
26.5424925903
372S-nitrosocysteineLGSTSTICSDKTGTL
HCCCCCCCCCCCCCC
4.33-
372S-nitrosylationLGSTSTICSDKTGTL
HCCCCCCCCCCCCCC
4.3322588120
373PhosphorylationGSTSTICSDKTGTLT
CCCCCCCCCCCCCCC
37.9925521595
375AcetylationTSTICSDKTGTLTQN
CCCCCCCCCCCCCCC
32.346569671
375UbiquitinationTSTICSDKTGTLTQN
CCCCCCCCCCCCCCC
32.34-
376PhosphorylationSTICSDKTGTLTQNR
CCCCCCCCCCCCCCC
40.1522324799
378PhosphorylationICSDKTGTLTQNRMT
CCCCCCCCCCCCCEE
31.6822324799
380PhosphorylationSDKTGTLTQNRMTVA
CCCCCCCCCCCEEEE
24.5224925903
405PhosphorylationADTTEDQSGATFDKR
CCCCCCCCCCCCCCC
42.5929899451
411UbiquitinationQSGATFDKRSPTWTA
CCCCCCCCCCCHHHH
51.05-
413PhosphorylationGATFDKRSPTWTALS
CCCCCCCCCHHHHHH
32.2122817900
432UbiquitinationLCNRAVFKAGQENIS
HHHHHHHHCCHHCCC
45.04-
439PhosphorylationKAGQENISVSKRDTA
HCCHHCCCCCCCCCC
31.7425521595
441PhosphorylationGQENISVSKRDTAGD
CHHCCCCCCCCCCCC
18.3822324799
442UbiquitinationQENISVSKRDTAGDA
HHCCCCCCCCCCCCC
52.73-
445PhosphorylationISVSKRDTAGDASES
CCCCCCCCCCCCCHH
36.2523984901
450PhosphorylationRDTAGDASESALLKC
CCCCCCCCHHHHHHH
36.5025521595
452PhosphorylationTAGDASESALLKCIE
CCCCCCHHHHHHHHH
23.0125521595
457S-nitrosylationSESALLKCIELSCGS
CHHHHHHHHHHHCCC
2.7024895380
457S-palmitoylationSESALLKCIELSCGS
CHHHHHHHHHHHCCC
2.7028680068
461PhosphorylationLLKCIELSCGSVRKM
HHHHHHHHCCCHHHH
12.0222817900
462S-nitrosylationLKCIELSCGSVRKMR
HHHHHHHCCCHHHHH
8.0224895380
464PhosphorylationCIELSCGSVRKMRDR
HHHHHCCCHHHHHCC
24.0722324799
474UbiquitinationKMRDRNPKVAEIPFN
HHHCCCCCEEECCCC
58.59-
482PhosphorylationVAEIPFNSTNKYQLS
EEECCCCCCCCEEEE
33.4622324799
483PhosphorylationAEIPFNSTNKYQLSI
EECCCCCCCCEEEEE
36.5125521595
496PhosphorylationSIHEREDSPQSHVLV
EEEECCCCCCCEEEE
21.7825521595
499PhosphorylationEREDSPQSHVLVMKG
ECCCCCCCEEEEECC
20.9625521595
505UbiquitinationQSHVLVMKGAPERIL
CCEEEEECCCHHHHH
44.43-
515S-nitrosylationPERILDRCSTILVQG
HHHHHHHCCEEEECC
4.1424895380
516PhosphorylationERILDRCSTILVQGK
HHHHHHCCEEEECCC
21.2622324799
517PhosphorylationRILDRCSTILVQGKE
HHHHHCCEEEECCCC
23.1925521595
523UbiquitinationSTILVQGKEIPLDKE
CEEEECCCCCCCCHH
35.07-
529UbiquitinationGKEIPLDKEMQDAFQ
CCCCCCCHHHHHHHH
63.87-
539PhosphorylationQDAFQNAYMELGGLG
HHHHHHHHHHHCCHH
9.9329899451
553S-nitrosylationGERVLGFCQLNLPSG
HHHHHEEEEECCCCC
4.2224895380
559PhosphorylationFCQLNLPSGKFPRGF
EEEECCCCCCCCCCC
58.7525521595
561UbiquitinationQLNLPSGKFPRGFKF
EECCCCCCCCCCCCC
57.44-
567UbiquitinationGKFPRGFKFDTDELN
CCCCCCCCCCHHHCC
45.19-
570PhosphorylationPRGFKFDTDELNFPT
CCCCCCCHHHCCCCH
34.21-
587PhosphorylationLCFVGLMSMIDPPRA
HHHHHHHHCCCCCHH
20.03-
602UbiquitinationAVPDAVGKCRSAGIK
CCCCHHHHHHHCCCE
21.63-
605PhosphorylationDAVGKCRSAGIKVIM
CHHHHHHHCCCEEEE
40.0729899451
614O-linked_GlycosylationGIKVIMVTGDHPITA
CCEEEEEECCCCCCH
21.3651462353
614PhosphorylationGIKVIMVTGDHPITA
CCEEEEEECCCCCCH
21.3628638064
620PhosphorylationVTGDHPITAKAIAKG
EECCCCCCHHHHHHC
26.93-
622UbiquitinationGDHPITAKAIAKGVG
CCCCCCHHHHHHCCE
31.51-
626UbiquitinationITAKAIAKGVGIISE
CCHHHHHHCCEEEEC
48.27-
632PhosphorylationAKGVGIISEGNETVE
HHCCEEEECCCCCHH
37.2129899451
637PhosphorylationIISEGNETVEDIAAR
EEECCCCCHHHHHHH
32.9422324799
650O-linked_GlycosylationARLNIPVSQVNPREA
HHCCCCHHHCCHHHC
24.05179353
650PhosphorylationARLNIPVSQVNPREA
HHCCCCHHHCCHHHC
24.0527180971
658UbiquitinationQVNPREAKACVVHGS
HCCHHHCCEEEEECH
37.25-
660S-nitrosocysteineNPREAKACVVHGSDL
CHHHCCEEEEECHHH
3.02-
660S-nitrosylationNPREAKACVVHGSDL
CHHHCCEEEEECHHH
3.0224895380
665PhosphorylationKACVVHGSDLKDMTS
CEEEEECHHHHCCCH
25.5422324799
668UbiquitinationVVHGSDLKDMTSEQL
EEECHHHHCCCHHHH
50.90-
671PhosphorylationGSDLKDMTSEQLDEI
CHHHHCCCHHHHHHH
38.9720495213
672PhosphorylationSDLKDMTSEQLDEIL
HHHHCCCHHHHHHHH
19.3920495213
683PhosphorylationDEILRDHTEIVFART
HHHHHHCCEEEEEEC
31.5329899451
695UbiquitinationARTSPQQKLIIVEGC
EECCCCCEEEEEECC
36.08-
702S-nitrosocysteineKLIIVEGCQRQGAIV
EEEEEECCCCCCCEE
1.58-
702S-nitrosylationKLIIVEGCQRQGAIV
EEEEEECCCCCCCEE
1.5824895380
712PhosphorylationQGAIVAVTGDGVNDS
CCCEEEEECCCCCCC
21.5924925903
719PhosphorylationTGDGVNDSPALKKAD
ECCCCCCCHHHHHCC
13.5825521595
723AcetylationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE
48.2822902405
723UbiquitinationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE
48.28-
724UbiquitinationNDSPALKKADIGIAM
CCCHHHHHCCEEEEC
52.74-
770UbiquitinationRLIFDNLKKSIAYTL
EEEECCHHHHHHHHH
51.21-
826PhosphorylationLAYEAAESDIMKRQP
HHHHHHHHHHHHCCC
27.92-
840UbiquitinationPRNSQTDKLVNERLI
CCCCHHHHHHHHHHH
58.69-
891PhosphorylationRLDWDDRTTNDLEDS
ECCCCCCCCCCCHHH
36.6217203969
892PhosphorylationLDWDDRTTNDLEDSY
CCCCCCCCCCCHHHC
27.8517203969
940PhosphorylationICKTRRNSVFQQGMK
EECCCCCHHHHHHHC
23.6119060867
947UbiquitinationSVFQQGMKNKILIFG
HHHHHHHCCCHHEEC
63.01-
1016UbiquitinationYPGGWVEKETYY---
CCCCCEEEEECC---
45.82-
1020PhosphorylationWVEKETYY-------
CEEEEECC-------
21.3518034455

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_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAC1_MOUSESlc8a1physical
15485817

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT1A2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND MASSSPECTROMETRY.

TOP