CACB4_MOUSE - dbPTM
CACB4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACB4_MOUSE
UniProt AC Q8R0S4
Protein Name Voltage-dependent L-type calcium channel subunit beta-4 {ECO:0000305}
Gene Name Cacnb4 {ECO:0000312|MGI:MGI:103301}
Organism Mus musculus (Mouse).
Sequence Length 519
Subcellular Localization
Protein Description The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting..
Protein Sequence MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTTTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTSSSTPMTPLLGRNVGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGCSHDSRHRL
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
16PhosphorylationGAADGPHSPSSQVAR
CCCCCCCCCHHHHCC		29.6122324799
18PhosphorylationADGPHSPSSQVARGT
CCCCCCCHHHHCCCC		36.1022324799
19PhosphorylationDGPHSPSSQVARGTT
CCCCCCHHHHCCCCC		31.8722324799
38PhosphorylationRLKRSDGSTTSTSFI
HCCCCCCCCCCCEEE		33.2425521595
39PhosphorylationLKRSDGSTTSTSFIL
CCCCCCCCCCCEEEE		30.2329899451
40PhosphorylationKRSDGSTTSTSFILR
CCCCCCCCCCEEEEE		31.5322807455
41PhosphorylationRSDGSTTSTSFILRQ
CCCCCCCCCEEEEEC		23.3422817900
42PhosphorylationSDGSTTSTSFILRQG
CCCCCCCCEEEEECC		26.0922817900
43PhosphorylationDGSTTSTSFILRQGS
CCCCCCCEEEEECCC		15.2821183079
50PhosphorylationSFILRQGSADSYTSR
EEEEECCCCCCCCCC		22.1422817900
53PhosphorylationLRQGSADSYTSRPSD
EECCCCCCCCCCCCC		29.9929899451
54PhosphorylationRQGSADSYTSRPSDS
ECCCCCCCCCCCCCC		14.8525521595
56PhosphorylationGSADSYTSRPSDSDV
CCCCCCCCCCCCCCC		33.6829899451
59PhosphorylationDSYTSRPSDSDVSLE
CCCCCCCCCCCCCHH		48.9525521595
61PhosphorylationYTSRPSDSDVSLEED
CCCCCCCCCCCHHHH		44.2221183079
64PhosphorylationRPSDSDVSLEEDREA
CCCCCCCCHHHHHHH		34.7525521595
102PhosphorylationAVKTNVSYCGALDED
EEECCCCCCCCCCCC		7.2228059163
175PhosphorylationGRFHGGKSSGNSSSS
CCCCCCCCCCCCCCC		46.9121082442
176PhosphorylationRFHGGKSSGNSSSSL
CCCCCCCCCCCCCCH		45.5419060867
179PhosphorylationGGKSSGNSSSSLGEM
CCCCCCCCCCCHHHH		34.8119060867
180PhosphorylationGKSSGNSSSSLGEMV
CCCCCCCCCCHHHHH		28.1322807455
181PhosphorylationKSSGNSSSSLGEMVS
CCCCCCCCCHHHHHC		29.4219060867
182PhosphorylationSSGNSSSSLGEMVSG
CCCCCCCCHHHHHCC		42.2025521595
188PhosphorylationSSLGEMVSGTFRATP
CCHHHHHCCEEEECC		30.7029899451
194PhosphorylationVSGTFRATPTTTAKQ
HCCEEEECCCCCHHH		19.5328576409
227PhosphorylationPVVLVGPSLKGYEVT
CEEEECCCCCCCCHH		36.46-
282PhosphorylationKRAIIERSNTRSSLA
HHHHHHCCCCCHHHH		29.7529899451
284PhosphorylationAIIERSNTRSSLAEV
HHHHCCCCCHHHHHH		32.9221082442
287PhosphorylationERSNTRSSLAEVQSE
HCCCCCHHHHHHHHH		28.4525521595
401PhosphorylationLEAYWRATHTSSSTP
HHHHHHHHCCCCCCC		19.6724925903
403PhosphorylationAYWRATHTSSSTPMT
HHHHHHCCCCCCCCC		26.4222324799
404PhosphorylationYWRATHTSSSTPMTP
HHHHHCCCCCCCCCC		18.0622324799
405PhosphorylationWRATHTSSSTPMTPL
HHHHCCCCCCCCCCC		39.1122324799
406PhosphorylationRATHTSSSTPMTPLL
HHHCCCCCCCCCCCC		35.9822324799
407PhosphorylationATHTSSSTPMTPLLG
HHCCCCCCCCCCCCC		21.0122324799
410PhosphorylationTSSSTPMTPLLGRNV
CCCCCCCCCCCCCCC		16.4025521595
420PhosphorylationLGRNVGSTALSPYPT
CCCCCCCCCCCCCCC		26.2029899451
423PhosphorylationNVGSTALSPYPTAIS
CCCCCCCCCCCCHHH		21.66-
425PhosphorylationGSTALSPYPTAISGL
CCCCCCCCCCHHHHH		15.1629899451
427PhosphorylationTALSPYPTAISGLQS
CCCCCCCCHHHHHHH		30.6829899451
434PhosphorylationTAISGLQSQRMRHSN
CHHHHHHHHHHHCCC		25.4625521595
440PhosphorylationQSQRMRHSNHSTENS
HHHHHHCCCCCCCCC		26.3522324799
443PhosphorylationRMRHSNHSTENSPIE
HHHCCCCCCCCCHHH		41.4929899451
444PhosphorylationMRHSNHSTENSPIER
HHCCCCCCCCCHHHH		31.4722324799
447PhosphorylationSNHSTENSPIERRSL
CCCCCCCCHHHHHHC		22.4822324799
453PhosphorylationNSPIERRSLMTSDEN
CCHHHHHHCCCCCCH		28.8129899451
456PhosphorylationIERRSLMTSDENYHN
HHHHHCCCCCCHHHH		38.0229899451
474PhosphorylationRKSRNRLSSSSQHSR
HHHHHHHCCCCCCCC		25.5722807455
475PhosphorylationKSRNRLSSSSQHSRD
HHHHHHCCCCCCCCC		38.3021183079
476PhosphorylationSRNRLSSSSQHSRDH
HHHHHCCCCCCCCCC		30.5522807455
477PhosphorylationRNRLSSSSQHSRDHY
HHHHCCCCCCCCCCC		33.5819060867
480PhosphorylationLSSSSQHSRDHYPLV
HCCCCCCCCCCCCCC		31.5921183079
484PhosphorylationSQHSRDHYPLVEEDY
CCCCCCCCCCCCCCC		11.5321183079
505MethylationTYKPHRNRGSPGGCS
CCCCCCCCCCCCCCC		47.0924129315
507PhosphorylationKPHRNRGSPGGCSHD
CCCCCCCCCCCCCCC		19.6822324799
512PhosphorylationRGSPGGCSHDSRHRL
CCCCCCCCCCCCCCC		33.3422817900
515PhosphorylationPGGCSHDSRHRL---
CCCCCCCCCCCC---		25.2729899451
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

Oops, there are no upstream regulatory protein records of CACB4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CACB4_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 CACB4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CACB4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CACB4_MOUSE

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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-38 AND SER-405, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASSSPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-410, ANDMASS SPECTROMETRY.

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