AT1A2_RAT - dbPTM
AT1A2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT1A2_RAT
UniProt AC P06686
Protein Name Sodium/potassium-transporting ATPase subunit alpha-2
Gene Name Atp1a2
Organism Rattus norvegicus (Rat).
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..
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
20.7027097102
10PhosphorylationRGAGREYSPAATTAE
CCCCCCCCCCCCCCC
11.8727097102
34AcetylationEKELDELKKEVAMDD
HHHHHHHHHHHCCCC
44.8522902405
35UbiquitinationKELDELKKEVAMDDH
HHHHHHHHHHCCCCC
70.78-
43AcetylationEVAMDDHKLSLDELG
HHCCCCCCCCHHHHC
46.9222902405
43UbiquitinationEVAMDDHKLSLDELG
HHCCCCCCCCHHHHC
46.92-
45PhosphorylationAMDDHKLSLDELGRK
CCCCCCCCHHHHCHH
38.28-
53PhosphorylationLDELGRKYQVDLSKG
HHHHCHHHCCCCCCC
16.65-
58PhosphorylationRKYQVDLSKGLTNQR
HHHCCCCCCCCCCHH
21.8825403869
59AcetylationKYQVDLSKGLTNQRA
HHCCCCCCCCCCHHH
66.3022902405
59UbiquitinationKYQVDLSKGLTNQRA
HHCCCCCCCCCCHHH
66.30-
154UbiquitinationYQEAKSSKIMDSFKN
HHHHHHCHHHHHHHH
49.49-
160UbiquitinationSKIMDSFKNMVPQQA
CHHHHHHHHCCCCEE
48.35-
192UbiquitinationVGDLVEVKGGDRVPA
EECEEEEECCCCCCC
43.61-
210UbiquitinationIISSHGCKVDNSSLT
EEECCCCEECCCCCC
58.16-
214PhosphorylationHGCKVDNSSLTGESE
CCCEECCCCCCCCCC
23.4329779826
215PhosphorylationGCKVDNSSLTGESEP
CCEECCCCCCCCCCC
35.8830411139
217PhosphorylationKVDNSSLTGESEPQT
EECCCCCCCCCCCCC
40.6327097102
220PhosphorylationNSSLTGESEPQTRSP
CCCCCCCCCCCCCCC
56.7927097102
224PhosphorylationTGESEPQTRSPEFTH
CCCCCCCCCCCCCCC
43.7828689409
226PhosphorylationESEPQTRSPEFTHEN
CCCCCCCCCCCCCCC
31.9725403869
230PhosphorylationQTRSPEFTHENPLET
CCCCCCCCCCCCCCC
26.9825403869
273PhosphorylationGRIATLASGLEVGQT
HHHHHHHHCCCCCCC
47.20-
364PhosphorylationKNLEAVETLGSTSTI
CCHHHHHHHCCCCCC
29.8028551015
367PhosphorylationEAVETLGSTSTICSD
HHHHHHCCCCCCCCC
23.4628551015
368PhosphorylationAVETLGSTSTICSDK
HHHHHCCCCCCCCCC
28.2628551015
369PhosphorylationVETLGSTSTICSDKT
HHHHCCCCCCCCCCC
19.9228551015
370PhosphorylationETLGSTSTICSDKTG
HHHCCCCCCCCCCCC
26.5428551015
373PhosphorylationGSTSTICSDKTGTLT
CCCCCCCCCCCCCCC
37.9928551015
376PhosphorylationSTICSDKTGTLTQNR
CCCCCCCCCCCCCCC
40.1522108457
378PhosphorylationICSDKTGTLTQNRMT
CCCCCCCCCCCCCEE
31.6828551015
380PhosphorylationSDKTGTLTQNRMTVA
CCCCCCCCCCCEEEE
24.5228551015
385PhosphorylationTLTQNRMTVAHMWFD
CCCCCCEEEEHHHCC
16.0025403869
400PhosphorylationNQIHEADTTEDQSGA
CCCCCCCCCCCCCCC
38.8525403869
413PhosphorylationGATFDKRSPTWTALS
CCCCCCCCCHHHHHH
32.2122673903
415PhosphorylationTFDKRSPTWTALSRI
CCCCCCCHHHHHHHH
36.3722673903
417PhosphorylationDKRSPTWTALSRIAG
CCCCCHHHHHHHHHH
21.8722673903
420PhosphorylationSPTWTALSRIAGLCN
CCHHHHHHHHHHHHH
21.1228689409
432AcetylationLCNRAVFKAGQENIS
HHHHHHHHCCHHCCC
45.0422902405
432UbiquitinationLCNRAVFKAGQENIS
HHHHHHHHCCHHCCC
45.04-
439PhosphorylationKAGQENISVSKRDTA
HCCHHCCCCCCCCCC
31.7430411139
441PhosphorylationGQENISVSKRDTAGD
CHHCCCCCCCCCCCC
18.3825403869
442UbiquitinationQENISVSKRDTAGDA
HHCCCCCCCCCCCCC
52.73-
445PhosphorylationISVSKRDTAGDASES
CCCCCCCCCCCCCHH
36.2528551015
450PhosphorylationRDTAGDASESALLKC
CCCCCCCCHHHHHHH
36.5028551015
452PhosphorylationTAGDASESALLKCIE
CCCCCCHHHHHHHHH
23.0128551015
461PhosphorylationLLKCIELSCGSVRKM
HHHHHHHHCCCHHHH
12.0228551015
464PhosphorylationCIELSCGSVRKMRDR
HHHHHCCCHHHHHCC
24.0728551015
482PhosphorylationVAEIPFNSTNKYQLS
EEECCCCCCCCEEEE
33.4625403869
483PhosphorylationAEIPFNSTNKYQLSI
EECCCCCCCCEEEEE
36.5128551015
485AcetylationIPFNSTNKYQLSIHE
CCCCCCCCEEEEEEE
34.1722902405
496PhosphorylationSIHEREDSPQSHVLV
EEEECCCCCCCEEEE
21.7825403869
499PhosphorylationEREDSPQSHVLVMKG
ECCCCCCCEEEEECC
20.9628551015
505AcetylationQSHVLVMKGAPERIL
CCEEEEECCCHHHHH
44.4322902405
516PhosphorylationERILDRCSTILVQGK
HHHHHHCCEEEECCC
21.2625403869
529AcetylationGKEIPLDKEMQDAFQ
CCCCCCCHHHHHHHH
63.8722902405
529UbiquitinationGKEIPLDKEMQDAFQ
CCCCCCCHHHHHHHH
63.87-
539PhosphorylationQDAFQNAYMELGGLG
HHHHHHHHHHHCCHH
9.93-
559PhosphorylationFCQLNLPSGKFPRGF
EEEECCCCCCCCCCC
58.7528551015
561UbiquitinationQLNLPSGKFPRGFKF
EECCCCCCCCCCCCC
57.44-
561AcetylationQLNLPSGKFPRGFKF
EECCCCCCCCCCCCC
57.4422902405
567UbiquitinationGKFPRGFKFDTDELN
CCCCCCCCCCHHHCC
45.19-
567AcetylationGKFPRGFKFDTDELN
CCCCCCCCCCHHHCC
45.1922902405
570PhosphorylationPRGFKFDTDELNFPT
CCCCCCCHHHCCCCH
34.21-
587PhosphorylationLCFVGLMSMIDPPRA
HHHHHHHHCCCCCHH
20.03-
602UbiquitinationAVPDAVGKCRSAGIK
CCCCHHHHHHHCCCE
21.63-
609AcetylationKCRSAGIKVIMVTGD
HHHHCCCEEEEEECC
25.45-
622AcetylationGDHPITAKAIAKGVG
CCCCCCHHHHHHCCE
31.5142502065
632PhosphorylationAKGVGIISEGNETVE
HHCCEEEECCCCCHH
37.2125403869
637PhosphorylationIISEGNETVEDIAAR
EEECCCCCHHHHHHH
32.9428551015
650PhosphorylationARLNIPVSQVNPREA
HHCCCCHHHCCHHHC
24.0527097102
658UbiquitinationQVNPREAKACVVHGS
HCCHHHCCEEEEECH
37.25-
671PhosphorylationGSDLKDMTSEQLDEI
CHHHHCCCHHHHHHH
38.9722673903
672PhosphorylationSDLKDMTSEQLDEIL
HHHHCCCHHHHHHHH
19.3922673903
719PhosphorylationTGDGVNDSPALKKAD
ECCCCCCCHHHHHCC
13.5830240740
723UbiquitinationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE
48.28-
723AcetylationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE
48.284256543
724UbiquitinationNDSPALKKADIGIAM
CCCHHHHHCCEEEEC
52.74-
724AcetylationNDSPALKKADIGIAM
CCCHHHHHCCEEEEC
52.744256545
826PhosphorylationLAYEAAESDIMKRQP
HHHHHHHHHHHHCCC
27.92-
840AcetylationPRNSQTDKLVNERLI
CCCCHHHHHHHHHHH
58.6922902405
840UbiquitinationPRNSQTDKLVNERLI
CCCCHHHHHHHHHHH
58.69-
891PhosphorylationRLDWDDRTTNDLEDS
ECCCCCCCCCCCHHH
36.6212692561
940PhosphorylationICKTRRNSVFQQGMK
EECCCCCHHHHHHHC
23.6125403869
1016UbiquitinationYPGGWVEKETYY---
CCCCCEEEEECC---
45.82-
1019PhosphorylationGWVEKETYY------
CCEEEEECC------
14.31-
1020PhosphorylationWVEKETYY-------
CEEEEECC-------
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
940SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT1A2_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITPR1_RATItpr1physical
14593108
NAC1_RATSlc8a1physical
14593108
AT2B1_RATAtp2b1physical
14593108
SPTN1_RATSptan1physical
14593108

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT1A2_RAT

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Related Literatures of Post-Translational Modification

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