CACB1_MOUSE - dbPTM
CACB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACB1_MOUSE
UniProt AC Q8R3Z5
Protein Name Voltage-dependent L-type calcium channel subunit beta-1
Gene Name Cacnb1
Organism Mus musculus (Mouse).
Sequence Length 597
Subcellular Localization Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side.
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 MVQKSGMSRGPYPPSQEIPMEVFDPSPQGKYSKRKGRFKRSDGSTSSDTTSNSFVRQGSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQTLRQNRLSSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPPNPLLNRTMATAALAASPAPVSNLQGPYLASGDQPLDRATGEHASVHEYPGELGQPPGLYPSNHPLGRAGTLRALSRQDTFDADTPGSRNSAYTEPGDSCVDMETDPSEGPGPGDPAGGGTPPARQGSWEDEEDYEEEMTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGQGVYTR
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
12PhosphorylationSGMSRGPYPPSQEIP
CCCCCCCCCCHHCCC
30.51-
15PhosphorylationSRGPYPPSQEIPMEV
CCCCCCCHHCCCCCC
35.62-
16PhosphorylationRGPYPPSQEIPMEVF
CCCCCCHHCCCCCCC
59.41-
23PhosphorylationQEIPMEVFDPSPQGK
HCCCCCCCCCCCCCC
7.92-
26PhosphorylationPMEVFDPSPQGKYSK
CCCCCCCCCCCCCCC
31.5329899451
41PhosphorylationRKGRFKRSDGSTSSD
CCCCCCCCCCCCCCC
47.0825521595
44PhosphorylationRFKRSDGSTSSDTTS
CCCCCCCCCCCCCCC
30.0625521595
45PhosphorylationFKRSDGSTSSDTTSN
CCCCCCCCCCCCCCC
37.4726643407
46PhosphorylationKRSDGSTSSDTTSNS
CCCCCCCCCCCCCCC
28.1029899451
47PhosphorylationRSDGSTSSDTTSNSF
CCCCCCCCCCCCCCC
38.7825521595
49PhosphorylationDGSTSSDTTSNSFVR
CCCCCCCCCCCCCCC
33.7929899451
51PhosphorylationSTSSDTTSNSFVRQG
CCCCCCCCCCCCCCC
32.3524899341
53PhosphorylationSSDTTSNSFVRQGSA
CCCCCCCCCCCCCCC
25.5325521595
59PhosphorylationNSFVRQGSAESYTSR
CCCCCCCCCCCCCCC
22.1124899341
62PhosphorylationVRQGSAESYTSRPSD
CCCCCCCCCCCCCCC
33.1729899451
63PhosphorylationRQGSAESYTSRPSDS
CCCCCCCCCCCCCCC
10.5529899451
64PhosphorylationQGSAESYTSRPSDSD
CCCCCCCCCCCCCCC
27.7829899451
65PhosphorylationGSAESYTSRPSDSDV
CCCCCCCCCCCCCCC
33.6829899451
68PhosphorylationESYTSRPSDSDVSLE
CCCCCCCCCCCCCHH
48.9521183079
70PhosphorylationYTSRPSDSDVSLEED
CCCCCCCCCCCHHHH
44.2221183079
73PhosphorylationRPSDSDVSLEEDREA
CCCCCCCCHHHHHHH
34.7520415495
182PhosphorylationTLRQNRLSSSKSGDN
HHHHHCCCCCCCCCC
29.3624899341
183PhosphorylationLRQNRLSSSKSGDNS
HHHHCCCCCCCCCCC
46.5124899341
184PhosphorylationRQNRLSSSKSGDNSS
HHHCCCCCCCCCCCC
27.7122210690
185UbiquitinationQNRLSSSKSGDNSSS
HHCCCCCCCCCCCCC
61.48-
186PhosphorylationNRLSSSKSGDNSSSS
HCCCCCCCCCCCCCC
54.0125521595
190PhosphorylationSSKSGDNSSSSLGDV
CCCCCCCCCCCCCCC
36.0224899341
191PhosphorylationSKSGDNSSSSLGDVV
CCCCCCCCCCCCCCC
30.1525521595
192PhosphorylationKSGDNSSSSLGDVVT
CCCCCCCCCCCCCCC
29.4227742792
193PhosphorylationSGDNSSSSLGDVVTG
CCCCCCCCCCCCCCC
38.0225521595
199PhosphorylationSSLGDVVTGTRRPTP
CCCCCCCCCCCCCCC
32.4620415495
201PhosphorylationLGDVVTGTRRPTPPA
CCCCCCCCCCCCCCC
17.7120415495
205 (in isoform 4)Phosphorylation-39.8422817900
205PhosphorylationVTGTRRPTPPASAKQ
CCCCCCCCCCCCHHH
39.8429899451
205 (in isoform 2)Phosphorylation-39.8422817900
209 (in isoform 4)Phosphorylation-41.6022210690
209 (in isoform 2)Phosphorylation-41.6022210690
214 (in isoform 2)Phosphorylation-42.3022210690
214 (in isoform 4)Phosphorylation-42.3022210690
216PhosphorylationSAKQKQKSTEHVPPY
CHHHHHCCCCCCCCC
36.2119060867
217PhosphorylationAKQKQKSTEHVPPYD
HHHHHCCCCCCCCCC
36.8319060867
238 (in isoform 2)Phosphorylation-36.4622210690
238 (in isoform 4)Phosphorylation-36.4622210690
241 (in isoform 2)Phosphorylation-29.1822210690
241 (in isoform 4)Phosphorylation-29.1822210690
242 (in isoform 2)Phosphorylation-12.9722210690
242 (in isoform 4)Phosphorylation-12.9722210690
244 (in isoform 2)Phosphorylation-4.0722210690
244 (in isoform 4)Phosphorylation-4.0722210690
245 (in isoform 4)Phosphorylation-13.2624899341
245 (in isoform 2)Phosphorylation-13.2624899341
247 (in isoform 4)Phosphorylation-1.9322210690
247 (in isoform 2)Phosphorylation-1.9322210690
248 (in isoform 4)Phosphorylation-4.0428464351
248 (in isoform 2)Phosphorylation-4.0428464351
248PhosphorylationGYEVTDMMQKALFDF
CCCHHHHHHHHHHHH
4.0424719451
285PhosphorylationRSVLNNPSKHIIIER
HHHHCCCCCEEEEEC
38.7028464351
293PhosphorylationKHIIIERSNTRSSLA
CEEEEECCCCCHHHH
29.7521183079
295PhosphorylationIIIERSNTRSSLAEV
EEEECCCCCHHHHHH
32.9216452087
297PhosphorylationIERSNTRSSLAEVQS
EECCCCCHHHHHHHH
27.8916452087
298PhosphorylationERSNTRSSLAEVQSE
ECCCCCHHHHHHHHH
28.4525521595
412PhosphorylationLEAYWKATHPPSSTP
HHHHHHHHCCCCCCC
31.0520415495
416PhosphorylationWKATHPPSSTPPNPL
HHHHCCCCCCCCCCC
51.8219060867
417PhosphorylationKATHPPSSTPPNPLL
HHHCCCCCCCCCCCC
51.1925521595
418PhosphorylationATHPPSSTPPNPLLN
HHCCCCCCCCCCCCC
47.2924899341
436PhosphorylationATAALAASPAPVSNL
HHHHHHCCCCCHHHC
18.9129899451
456 (in isoform 3)Phosphorylation-44.8722817900
495PhosphorylationAGTLRALSRQDTFDA
HHHHHHHHCCCCCCC
27.2322324799
499PhosphorylationRALSRQDTFDADTPG
HHHHCCCCCCCCCCC
18.3125521595
501 (in isoform 2)Phosphorylation-45.7022817900
501PhosphorylationLSRQDTFDADTPGSR
HHCCCCCCCCCCCCC
45.7024719451
540PhosphorylationGDPAGGGTPPARQGS
CCCCCCCCCCCCCCC
29.4025521595
547PhosphorylationTPPARQGSWEDEEDY
CCCCCCCCCCCHHHH
20.9625521595

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 CACB1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CACB1_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 CACB1_MOUSE !!

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

Oops, there are no PPI records of CACB1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CACB1_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-186, 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 THR-499, AND MASSSPECTROMETRY.

TOP