AT2B2_MOUSE - dbPTM
AT2B2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT2B2_MOUSE
UniProt AC Q9R0K7
Protein Name Plasma membrane calcium-transporting ATPase 2
Gene Name Atp2b2
Organism Mus musculus (Mouse).
Sequence Length 1198
Subcellular Localization Cell junction, synapse . Cell membrane
Multi-pass membrane protein .
Protein Description This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. Plays a role in maintaining balance and hearing..
Protein Sequence MGDMTNSDFYSKNQRNESSHGGEFGCTMEELRSLMELRGTEAVVKIKETYGDTEAICRRLKTSPVEGLPGTAPDLEKRKQIFGQNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIISLGLSFYHPPGESNEGCATAQGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVVRAGQVVQIPVAEIVVGDIAQIKYGDLLPADGLFIQGNDLKIDESSLTGESDQVRKSVDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDKKAKQQDGAAAMEMQPLKSAEGGDADDKKKANMHKKEKSVLQGKLTKLAVQIGKAGLVMSAITVIILVLYFTVDTFVVNKKPWLTECTPVYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQAYVGDVHYKEIPDPSSINAKTLELLVNAIAINSAYTTKILPPEKEGALPRQVGNKTECGLLGFVLDLRQDYEPVRSQMPEEKLYKVYTFNSVRKSMSTVIKMPDESFRMYSKGASEIVLKKCCKILSGAGEARVFRPRDRDEMVKKVIEPMACDGLRTICVAYRDFPSSPEPDWDNENDILNELTCICVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAIKCGIIHPGEDFLCLEGKEFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTHTEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTETLLLRKPYGRNKPLISRTMMKNILGHAVYQLTLIFTLLFVGEKMFQIDSGRNAPLHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFRNPIFCTIVLGTFAIQIVIVQFGGKPFSCSPLQLDQWMWCIFIGLGELVWGQVIATIPTSRLKFLKEAGRLTQKEEIPEEELNEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVKAFRSSLYEGLEKPESRTSIHNFMAHPEFRIEDSQPHIPLIDDTDLEEDAALKQNSSPPSSLNKNNSAIDSGINLTTDTSKSATSSSPGSPIHSLETSL
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
7Phosphorylation-MGDMTNSDFYSKNQ
-CCCCCHHHHHCCCC
21.67-
12UbiquitinationTNSDFYSKNQRNESS
CHHHHHCCCCCCCCC
45.80-
18PhosphorylationSKNQRNESSHGGEFG
CCCCCCCCCCCCCCC
31.0525521595
19PhosphorylationKNQRNESSHGGEFGC
CCCCCCCCCCCCCCC
21.7022324799
45UbiquitinationRGTEAVVKIKETYGD
HCCEEEEEEEHHHCC
41.27-
47UbiquitinationTEAVVKIKETYGDTE
CEEEEEEEHHHCCHH
37.98-
49PhosphorylationAVVKIKETYGDTEAI
EEEEEEHHHCCHHHH
28.0025367039
50PhosphorylationVVKIKETYGDTEAIC
EEEEEHHHCCHHHHH
17.6925367039
53PhosphorylationIKETYGDTEAICRRL
EEHHHCCHHHHHHHH
23.9725367039
61UbiquitinationEAICRRLKTSPVEGL
HHHHHHHCCCCCCCC
45.18-
62PhosphorylationAICRRLKTSPVEGLP
HHHHHHCCCCCCCCC
42.7429899451
63PhosphorylationICRRLKTSPVEGLPG
HHHHHCCCCCCCCCC
25.9229899451
77UbiquitinationGTAPDLEKRKQIFGQ
CCCCCHHHHHHHHCC
72.67-
191UbiquitinationSRIEQEQKFTVVRAG
HHHHHHCCEEEEECC
42.10-
218PhosphorylationGDIAQIKYGDLLPAD
CCHHHCCCCCEECCC
19.9429899451
239PhosphorylationNDLKIDESSLTGESD
CCEEECHHHCCCCCH
27.2225521595
240PhosphorylationDLKIDESSLTGESDQ
CEEECHHHCCCCCHH
28.0920415495
242PhosphorylationKIDESSLTGESDQVR
EECHHHCCCCCHHHH
40.6329899451
245PhosphorylationESSLTGESDQVRKSV
HHHCCCCCHHHHHHC
34.3929899451
254UbiquitinationQVRKSVDKDPMLLSG
HHHHHCCCCCCCCCC
62.67-
262PhosphorylationDPMLLSGTHVMEGSG
CCCCCCCCEEECCCC
14.12-
268PhosphorylationGTHVMEGSGRMVVTA
CCEEECCCCCEEEEE
15.21-
282PhosphorylationAVGVNSQTGIIFTLL
EEEECCCCCEEEEEE
30.1228059163
304UbiquitinationEKKDKKAKQQDGAAA
HHHHHHHHHHCCCHH
58.32-
318UbiquitinationAMEMQPLKSAEGGDA
HHHCCCCCCCCCCCC
55.06-
319PhosphorylationMEMQPLKSAEGGDAD
HHCCCCCCCCCCCCC
38.9629899451
431UbiquitinationYSVKKMMKDNNLVRH
HHHHHHHCCCCHHHH
54.53-
456PhosphorylationTAICSDKTGTLTTNR
EEEECCCCCCEECCC
40.1525521595
458PhosphorylationICSDKTGTLTTNRMT
EECCCCCCEECCCEE
26.6022324799
460PhosphorylationSDKTGTLTTNRMTVV
CCCCCCEECCCEEEE
23.1222324799
477UbiquitinationYVGDVHYKEIPDPSS
EECCEECCCCCCHHH
34.00-
512UbiquitinationTKILPPEKEGALPRQ
CCCCCCCCCCCCCCC
68.19-
526S-nitrosylationQVGNKTECGLLGFVL
CCCCCCCCCHHHHHH
5.8722588120
550UbiquitinationRSQMPEEKLYKVYTF
HHCCCHHHHHEEEEH
56.29-
553UbiquitinationMPEEKLYKVYTFNSV
CCHHHHHEEEEHHHH
38.92-
555PhosphorylationEEKLYKVYTFNSVRK
HHHHHEEEEHHHHCH
11.0625195567
559PhosphorylationYKVYTFNSVRKSMST
HEEEEHHHHCHHHCC
21.0729899451
569UbiquitinationKSMSTVIKMPDESFR
HHHCCEEECCCHHHC
39.79-
583PhosphorylationRMYSKGASEIVLKKC
CHHCCCCHHHHHHHH
36.2028464351
588AcetylationGASEIVLKKCCKILS
CCHHHHHHHHHHHHC
32.6319860257
613UbiquitinationRDRDEMVKKVIEPMA
CCHHHHHHHHHHHHH
39.76-
614UbiquitinationDRDEMVKKVIEPMAC
CHHHHHHHHHHHHHC
36.71-
681PhosphorylationKCQRAGITVRMVTGD
HHHHCCCEEEEECCC
10.9228059163
692PhosphorylationVTGDNINTARAIAIK
ECCCCHHHHHHHHHH
17.4528059163
699UbiquitinationTARAIAIKCGIIHPG
HHHHHHHHCCEECCC
19.86-
715UbiquitinationDFLCLEGKEFNRRIR
CEEEECCHHHHHHHH
50.16-
725UbiquitinationNRRIRNEKGEIEQER
HHHHHCCCCCCCHHH
66.45-
735UbiquitinationIEQERIDKIWPKLRV
CCHHHHHHHHHHHHH
44.28-
747PhosphorylationLRVLARSSPTDKHTL
HHHHHCCCCCCHHHH
26.68-
777PhosphorylationVAVTGDGTNDGPALK
EEEECCCCCCCHHHH
34.5720415495
784AcetylationTNDGPALKKADVGFA
CCCCHHHHHCCCEEE
48.2819847399
784UbiquitinationTNDGPALKKADVGFA
CCCCHHHHHCCCEEE
48.28-
785UbiquitinationNDGPALKKADVGFAM
CCCHHHHHCCCEEEH
51.15-
804PhosphorylationTDVAKEASDIILTDD
CHHHHHHHHEEECCC
30.3629899451
814PhosphorylationILTDDNFSSIVKAVM
EECCCCHHHHHHHHH
25.9620415495
815PhosphorylationLTDDNFSSIVKAVMW
ECCCCHHHHHHHHHC
27.5420415495
1056UbiquitinationEAGRLTQKEEIPEEE
HHCCCCCCHHCCHHH
52.67-
1087MethylationRGQILWFRGLNRIQT
HCCEEEEECCCHHHH
36.79-
1087DimethylationRGQILWFRGLNRIQT
HCCEEEEECCCHHHH
36.79-
1094PhosphorylationRGLNRIQTQIRVVKA
ECCCHHHHHHHHHHH
24.4829899451
1104PhosphorylationRVVKAFRSSLYEGLE
HHHHHHHHHHHHCCC
20.4525521595
1105PhosphorylationVVKAFRSSLYEGLEK
HHHHHHHHHHHCCCC
30.6227742792
1107PhosphorylationKAFRSSLYEGLEKPE
HHHHHHHHHCCCCCC
15.2025159016
1112UbiquitinationSLYEGLEKPESRTSI
HHHHCCCCCCCCCCH
60.16-
1112AcetylationSLYEGLEKPESRTSI
HHHHCCCCCCCCCCH
60.167632155
1115PhosphorylationEGLEKPESRTSIHNF
HCCCCCCCCCCHHHH
49.7625521595
1117PhosphorylationLEKPESRTSIHNFMA
CCCCCCCCCHHHHCC
41.1125521595
1118PhosphorylationEKPESRTSIHNFMAH
CCCCCCCCHHHHCCC
22.2725521595
1133PhosphorylationPEFRIEDSQPHIPLI
CCEECCCCCCCCCCC
32.5925521595
1143PhosphorylationHIPLIDDTDLEEDAA
CCCCCCCCCHHHHHH
38.4425521595
1155PhosphorylationDAALKQNSSPPSSLN
HHHHHCCCCCCHHHC
41.5525521595
1156PhosphorylationAALKQNSSPPSSLNK
HHHHCCCCCCHHHCC
48.6725521595
1159PhosphorylationKQNSSPPSSLNKNNS
HCCCCCCHHHCCCCC
51.3325521595
1160PhosphorylationQNSSPPSSLNKNNSA
CCCCCCHHHCCCCCC
41.5625521595
1166PhosphorylationSSLNKNNSAIDSGIN
HHHCCCCCCCCCCCC
35.6720415495
1170PhosphorylationKNNSAIDSGINLTTD
CCCCCCCCCCCCCCC
35.1425521595
1179PhosphorylationINLTTDTSKSATSSS
CCCCCCCCCCCCCCC
27.6725521595
1181PhosphorylationLTTDTSKSATSSSPG
CCCCCCCCCCCCCCC
36.2225619855
1183PhosphorylationTDTSKSATSSSPGSP
CCCCCCCCCCCCCCC
35.9125619855
1184PhosphorylationDTSKSATSSSPGSPI
CCCCCCCCCCCCCCC
28.6525619855
1185PhosphorylationTSKSATSSSPGSPIH
CCCCCCCCCCCCCCC
35.8824925903
1186PhosphorylationSKSATSSSPGSPIHS
CCCCCCCCCCCCCCC
32.8024925903
1189PhosphorylationATSSSPGSPIHSLET
CCCCCCCCCCCCCCC
24.8625521595
1193PhosphorylationSPGSPIHSLETSL--
CCCCCCCCCCCCC--
28.7225521595
1196PhosphorylationSPIHSLETSL-----
CCCCCCCCCC-----
40.3925521595
1197PhosphorylationPIHSLETSL------
CCCCCCCCC------
23.7824925903

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
1094TPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT2B2_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 AT2B2_MOUSE !!

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

Oops, there are no PPI records of AT2B2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT2B2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND MASSSPECTROMETRY.
"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-1189 AND THR-1196, ANDMASS SPECTROMETRY.

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