CACB3_HUMAN - dbPTM
CACB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACB3_HUMAN
UniProt AC P54284
Protein Name Voltage-dependent L-type calcium channel subunit beta-3
Gene Name CACNB3
Organism Homo sapiens (Human).
Sequence Length 484
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 MYDDSYVPGFEDSEAGSADSYTSRPSLDSDVSLEEDRESARREVESQAQQQLERAKHKPVAFAVRTNVSYCGVLDEECPVQGSGVNFEAKDFLHIKEKYSNDWWIGRLVKEGGDIAFIPSPQRLESIRLKQEQKARRSGNPSSLSDIGNRRSPPPSLAKQKQKQAEHVPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADLSLAKRSVLNNPGKRTIIERSSARSSIAEVQSEIERIFELAKSLQLVVLDADTINHPAQLAKTSLAPIIVFVKVSSPKVLQRLIRSRGKSQMKHLTVQMMAYDKLVQCPPESFDVILDENQLEDACEHLAEYLEVYWRATHHPAPGPGLLGPPSAIPGLQNQQLLGERGEEHSPLERDSLMPSDEASESSRQAWTGSSQRSSRHLEEDYADAYQDLYQPHRQHTSGLPSANGHDPQDRLLAQDSEHNHSDRNWQRNRPWPKDSY
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
2Phosphorylation------MYDDSYVPG
------CCCCCCCCC		28.5824043423
2 (in isoform 4)Phosphorylation-28.5823663014
4 (in isoform 4)Phosphorylation-25.1223663014
5Phosphorylation---MYDDSYVPGFED
---CCCCCCCCCCCC		25.7324043423
6 (in isoform 4)Phosphorylation-20.0523663014
6Phosphorylation--MYDDSYVPGFEDS
--CCCCCCCCCCCCC		20.0524043423
7 (in isoform 4)Phosphorylation-4.2923663014
9 (in isoform 4)Phosphorylation-28.6523663014
13PhosphorylationYVPGFEDSEAGSADS
CCCCCCCCCCCCCCC		23.3424043423
16 (in isoform 4)Phosphorylation-21.2223663014
17PhosphorylationFEDSEAGSADSYTSR
CCCCCCCCCCCCCCC		35.6324043423
19 (in isoform 4)Phosphorylation-43.8223663014
20PhosphorylationSEAGSADSYTSRPSL
CCCCCCCCCCCCCCC		29.9924043423
20 (in isoform 4)Phosphorylation-29.9923663014
21PhosphorylationEAGSADSYTSRPSLD
CCCCCCCCCCCCCCC		14.8524043423
21 (in isoform 4)Phosphorylation-14.8523663014
22 (in isoform 4)Phosphorylation-23.3923663014
22PhosphorylationAGSADSYTSRPSLDS
CCCCCCCCCCCCCCC		23.3924043423
23PhosphorylationGSADSYTSRPSLDSD
CCCCCCCCCCCCCCC		33.6824043423
39PhosphorylationSLEEDRESARREVES
CHHHHHHHHHHHHHH		28.15-
46PhosphorylationSARREVESQAQQQLE
HHHHHHHHHHHHHHH		35.67-
111PhosphorylationWIGRLVKEGGDIAFI
EHHHHHHCCCCEEEE		62.0132142685
120PhosphorylationGDIAFIPSPQRLESI
CCEEEECCHHHHHHH		28.93-
126PhosphorylationPSPQRLESIRLKQEQ
CCHHHHHHHHHHHHH		20.0125106551
138PhosphorylationQEQKARRSGNPSSLS
HHHHHHHCCCCCHHH		37.0521815630
139PhosphorylationEQKARRSGNPSSLSD
HHHHHHCCCCCHHHH		48.5332142685
142PhosphorylationARRSGNPSSLSDIGN
HHHCCCCCHHHHCCC		48.1623403867
143PhosphorylationRRSGNPSSLSDIGNR
HHCCCCCHHHHCCCC		32.9023403867
145PhosphorylationSGNPSSLSDIGNRRS
CCCCCHHHHCCCCCC		29.1823403867
151PhosphorylationLSDIGNRRSPPPSLA
HHHCCCCCCCCHHHH		58.4732142685
152PhosphorylationSDIGNRRSPPPSLAK
HHCCCCCCCCHHHHH		38.2230266825
156PhosphorylationNRRSPPPSLAKQKQK
CCCCCCHHHHHHHHH		46.8923403867
171PhosphorylationQAEHVPPYDVVPSMR
HHCCCCCCCCCCCCC		18.4622817900
176PhosphorylationPPYDVVPSMRPVVLV
CCCCCCCCCCCEEEE		18.8024275569
186PhosphorylationPVVLVGPSLKGYEVT
CEEEECCCCCCCCHH		36.4624275569
190PhosphorylationVGPSLKGYEVTDMMQ
ECCCCCCCCHHHHHH		12.9724275569
193PhosphorylationSLKGYEVTDMMQKAL
CCCCCCHHHHHHHHH		13.2624275569
213PhosphorylationHRFDGRISITRVTAD
HHCCCCCEEEEEECC		19.2924719451
295PhosphorylationIIVFVKVSSPKVLQR
EEEEEECCCHHHHHH		34.8924719451
316PhosphorylationKSQMKHLTVQMMAYD
HHHHHHHHHHHHHHH		14.38-
322PhosphorylationLTVQMMAYDKLVQCP
HHHHHHHHHHHHCCC		8.84-
374PhosphorylationPGLLGPPSAIPGLQN
CCCCCCCCCCCCHHH		41.8029523821
393PhosphorylationGERGEEHSPLERDSL
CCCCCCCCCCCHHCC		34.1629523821
399PhosphorylationHSPLERDSLMPSDEA
CCCCCHHCCCCCCHH		32.5624732914
403PhosphorylationERDSLMPSDEASESS
CHHCCCCCCHHCHHH		33.8324732914
407PhosphorylationLMPSDEASESSRQAW
CCCCCHHCHHHHHHH		35.6424732914
409PhosphorylationPSDEASESSRQAWTG
CCCHHCHHHHHHHHC		28.4624732914
410PhosphorylationSDEASESSRQAWTGS
CCHHCHHHHHHHHCC		25.1022210691
422PhosphorylationTGSSQRSSRHLEEDY
HCCCHHHHHHHCHHH		26.3824719451
429PhosphorylationSRHLEEDYADAYQDL
HHHHCHHHHHHHHHH		15.0628796482
433PhosphorylationEEDYADAYQDLYQPH
CHHHHHHHHHHHHHH		11.7828796482
437PhosphorylationADAYQDLYQPHRQHT
HHHHHHHHHHHHHCC		28.4328796482
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 CACB3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CACB3_HUMAN !!
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 CACB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAC1C_HUMANCACNA1Cphysical
15170217
CACB2_HUMANCACNB2physical
28514442
CBARP_HUMANC19orf26physical
28514442
PLCG1_HUMANPLCG1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB04855Dronedarone
DB00393Nimodipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CACB3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-171, AND MASSSPECTROMETRY.

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