CACB4_HUMAN - dbPTM
CACB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACB4_HUMAN
UniProt AC O00305
Protein Name Voltage-dependent L-type calcium channel subunit beta-4 {ECO:0000305}
Gene Name CACNB4 {ECO:0000312|HGNC:HGNC:1404}
Organism Homo sapiens (Human).
Sequence Length 520
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 MSSSSYAKNGTADGPHSPTSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTSTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTTSSTPMTPLLGRNLGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGYSHDSRHRL
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------MSSSSYAKN
------CCCHHCCCC		38.6422210691
3Phosphorylation-----MSSSSYAKNG
-----CCCHHCCCCC		23.2322210691
11PhosphorylationSSYAKNGTADGPHSP
HHCCCCCCCCCCCCC		30.85-
13 (in isoform 2)Phosphorylation-71.6222210691
21 (in isoform 2)Phosphorylation-35.0522210691
39PhosphorylationRLKRSDGSTTSTSFI
HCCCCCCCCCCCEEE		33.24-
51PhosphorylationSFILRQGSADSYTSR
EEEEECCCCCCCCCC		22.1423312004
54PhosphorylationLRQGSADSYTSRPSD
EECCCCCCCCCCCCC		29.9923312004
55PhosphorylationRQGSADSYTSRPSDS
ECCCCCCCCCCCCCC		14.8523312004
56PhosphorylationQGSADSYTSRPSDSD
CCCCCCCCCCCCCCC		23.3923312004
57PhosphorylationGSADSYTSRPSDSDV
CCCCCCCCCCCCCCC		33.6823312004
60PhosphorylationDSYTSRPSDSDVSLE
CCCCCCCCCCCCCHH		48.9523312004
62PhosphorylationYTSRPSDSDVSLEED
CCCCCCCCCCCHHHH		44.2223312004
65PhosphorylationRPSDSDVSLEEDREA
CCCCCCCCHHHHHHH		34.7523312004
99PhosphorylationPVAFAVKTNVSYCGA
CEEEEEECCCCCCCC		33.9618220336
102PhosphorylationFAVKTNVSYCGALDE
EEEECCCCCCCCCCC		19.4418220336
103PhosphorylationAVKTNVSYCGALDED
EEECCCCCCCCCCCC		7.2218220336
180PhosphorylationGGKSSGNSSSSLGEM
CCCCCCCCCCCHHHH		34.81-
182PhosphorylationKSSGNSSSSLGEMVS
CCCCCCCCCHHHHHC		29.42-
183PhosphorylationSSGNSSSSLGEMVSG
CCCCCCCCHHHHHCC		42.20-
207PhosphorylationAKQKQKVTEHIPPYD
HHHHHHCCCCCCCCC		28.9624719451
213PhosphorylationVTEHIPPYDVVPSMR
CCCCCCCCCCCCCCC		18.93-
218PhosphorylationPPYDVVPSMRPVVLV
CCCCCCCCCCCEEEE		18.8024275569
228PhosphorylationPVVLVGPSLKGYEVT
CEEEECCCCCCCCHH		36.4624275569
232PhosphorylationVGPSLKGYEVTDMMQ
ECCCCCCCCHHHHHH		12.9724275569
235PhosphorylationSLKGYEVTDMMQKAL
CCCCCCHHHHHHHHH		13.2624275569
255PhosphorylationHRFDGRISITRVTAD
HHCCCCCEEEEEECC		19.2924719451
257PhosphorylationFDGRISITRVTADIS
CCCCCEEEEEECCHH		16.5823312004
260PhosphorylationRISITRVTADISLAK
CCEEEEEECCHHHHH		18.4723312004
264PhosphorylationTRVTADISLAKRSVL
EEEECCHHHHHHHHH		23.8729083192
276AcetylationSVLNNPSKRAIIERS
HHHCCHHHHHHHHCC		47.2921466224
337PhosphorylationIIVHVKVSSPKVLQR
EEEEEECCCHHHHHH		34.8924719451
411PhosphorylationTTSSTPMTPLLGRNL
CCCCCCCCCCCCCCC		16.4024076635
421PhosphorylationLGRNLGSTALSPYPT
CCCCCCCCCCCCCCC		29.80-
435PhosphorylationTAISGLQSQRMRHSN
CHHHHHHHHHHHCCC		25.46-
448PhosphorylationSNHSTENSPIERRSL
CCCCCCCCHHHHHHC		22.48-
476PhosphorylationKSRNRLSSSSQHSRD
HHHHHHCCCCCCCCC		38.3021712546
477PhosphorylationSRNRLSSSSQHSRDH
HHHHHCCCCCCCCCC		30.5521712546
481PhosphorylationLSSSSQHSRDHYPLV
HCCCCCCCCCCCCCC		31.5921712546
499PhosphorylationYPDSYQDTYKPHRNR
CCCCCCCCCCCCCCC		20.23-
500PhosphorylationPDSYQDTYKPHRNRG
CCCCCCCCCCCCCCC		30.71-
506MethylationTYKPHRNRGSPGGYS
CCCCCCCCCCCCCCC		47.09-
508PhosphorylationKPHRNRGSPGGYSHD
CCCCCCCCCCCCCCC		19.68-
512PhosphorylationNRGSPGGYSHDSRHR
CCCCCCCCCCCCCCC		14.56-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CACB4_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 CACB4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBL3_HUMANTBL3physical
16169070
MED31_HUMANMED31physical
16169070
PTN_HUMANPTNphysical
16169070
CAC1A_HUMANCACNA1Aphysical
10212211
CBX3_HUMANCBX3physical
21220418
CACB3_HUMANCACNB3physical
28514442
GT252_HUMANCOLGALT2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607682Epilepsy, idiopathic generalized 9 (EIG9)
607682Juvenile myoclonic epilepsy 6 (EJM6)
613855Episodic ataxia 5 (EA5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB04855Dronedarone
DB00393Nimodipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CACB4_HUMAN

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Related Literatures of Post-Translational Modification

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