CACB1_HUMAN - dbPTM
CACB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CACB1_HUMAN
UniProt AC Q02641
Protein Name Voltage-dependent L-type calcium channel subunit beta-1
Gene Name CACNB1
Organism Homo sapiens (Human).
Sequence Length 598
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 MVQKTSMSRGPYPPSQEIPMEVFDPSPQGKYSKRKGRFKRSDGSTSSDTTSNSFVRQGSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQKLRQNRLGSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPPNPLLNRTMATAALAASPAPVSNLQGPYLASGDQPLERATGEHASMHEYPGELGQPPGLYPSSHPPGRAGTLRALSRQDTFDADTPGSRNSAYTELGDSCVDMETDPSEGPGLGDPAGGGTPPARQGSWEDEEEDYEEELTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGRGVYIR
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
8PhosphorylationMVQKTSMSRGPYPPS
CCCCCCCCCCCCCCC
33.5824719451
26PhosphorylationPMEVFDPSPQGKYSK
CCCCCCCCCCCCCCC
31.5324719451
31PhosphorylationDPSPQGKYSKRKGRF
CCCCCCCCCCCCCCC
26.6724719451
32PhosphorylationPSPQGKYSKRKGRFK
CCCCCCCCCCCCCCC
29.4824719451
44PhosphorylationRFKRSDGSTSSDTTS
CCCCCCCCCCCCCCC
30.0624719451
45PhosphorylationFKRSDGSTSSDTTSN
CCCCCCCCCCCCCCC
37.4730576142
46PhosphorylationKRSDGSTSSDTTSNS
CCCCCCCCCCCCCCC
28.1030576142
47PhosphorylationRSDGSTSSDTTSNSF
CCCCCCCCCCCCCCC
38.7824076635
50PhosphorylationGSTSSDTTSNSFVRQ
CCCCCCCCCCCCCCC
30.7924076635
51PhosphorylationSTSSDTTSNSFVRQG
CCCCCCCCCCCCCCC
32.3522210691
53PhosphorylationSSDTTSNSFVRQGSA
CCCCCCCCCCCCCCC
25.5322210691
59PhosphorylationNSFVRQGSAESYTSR
CCCCCCCCCCCCCCC
22.1123312004
62PhosphorylationVRQGSAESYTSRPSD
CCCCCCCCCCCCCCC
33.1727251275
63PhosphorylationRQGSAESYTSRPSDS
CCCCCCCCCCCCCCC
10.5525884760
64PhosphorylationQGSAESYTSRPSDSD
CCCCCCCCCCCCCCC
27.7827251275
65PhosphorylationGSAESYTSRPSDSDV
CCCCCCCCCCCCCCC
33.6827251275
68PhosphorylationESYTSRPSDSDVSLE
CCCCCCCCCCCCCHH
48.9527251275
70PhosphorylationYTSRPSDSDVSLEED
CCCCCCCCCCCHHHH
44.2227251275
73PhosphorylationRPSDSDVSLEEDREA
CCCCCCCCHHHHHHH
34.7523312004
175UbiquitinationLRLLQEQKLRQNRLG
HHHHHHHHHHHCCCC
44.9029967540
183PhosphorylationLRQNRLGSSKSGDNS
HHHCCCCCCCCCCCC
38.9022673903
184PhosphorylationRQNRLGSSKSGDNSS
HHCCCCCCCCCCCCC
29.1022673903
186PhosphorylationNRLGSSKSGDNSSSS
CCCCCCCCCCCCCCC
54.0126437602
190PhosphorylationSSKSGDNSSSSLGDV
CCCCCCCCCCCCCCC
36.0226437602
192PhosphorylationKSGDNSSSSLGDVVT
CCCCCCCCCCCCCCC
29.4219764811
193PhosphorylationSGDNSSSSLGDVVTG
CCCCCCCCCCCCCCC
38.0219764811
205 (in isoform 2)Phosphorylation-39.8422673903
209 (in isoform 2)Phosphorylation-41.6022673903
214 (in isoform 2)Phosphorylation-42.3022673903
241 (in isoform 2)Phosphorylation-29.1826437602
242PhosphorylationVGPSLKGYEVTDMMQ
ECCCCCCCCHHHHHH
12.9724275569
242 (in isoform 2)Phosphorylation-12.9728348404
244 (in isoform 2)Phosphorylation-4.0726437602
245PhosphorylationSLKGYEVTDMMQKAL
CCCCCCHHHHHHHHH
13.2624275569
247 (in isoform 2)Phosphorylation-1.9326437602
248 (in isoform 2)Phosphorylation-4.0427732954
261 (in isoform 2)Ubiquitination-45.4721906983
265PhosphorylationHRFDGRISITRVTAD
HHCCCCCEEEEEECC
19.2924719451
267PhosphorylationFDGRISITRVTADIS
CCCCCEEEEEECCHH
16.5823312004
270PhosphorylationRISITRVTADISLAK
CCEEEEEECCHHHHH
18.4723312004
274PhosphorylationTRVTADISLAKRSVL
EEEECCHHHHHHHHH
23.8729083192
335PhosphorylationHPAQLSKTSLAPIIV
CHHHCCCCCCCCEEE
26.1222210691
336PhosphorylationPAQLSKTSLAPIIVY
HHHCCCCCCCCEEEE
26.6922210691
343PhosphorylationSLAPIIVYIKITSPK
CCCCEEEEEEECCHH
6.0122210691
412PhosphorylationLEAYWKATHPPSSTP
HHHHHHHHCCCCCCC
31.0523312004
416PhosphorylationWKATHPPSSTPPNPL
HHHHCCCCCCCCCCC
51.8220886841
417PhosphorylationKATHPPSSTPPNPLL
HHHCCCCCCCCCCCC
51.1928348404
418PhosphorylationATHPPSSTPPNPLLN
HHCCCCCCCCCCCCC
47.2923312004
430 (in isoform 3)Phosphorylation-11.1422210691
441 (in isoform 3)Phosphorylation-30.6622210691
447PhosphorylationVSNLQGPYLASGDQP
HHHCCCCCCCCCCCC
23.0225884760
449 (in isoform 3)Phosphorylation-12.9622210691
450 (in isoform 3)Phosphorylation-40.0622210691
462PhosphorylationLERATGEHASMHEYP
CHHHCCCCCCHHCCC
25.1732142685
468 (in isoform 3)Phosphorylation-11.2326437602
475 (in isoform 2)Phosphorylation-24.1122210691
486 (in isoform 2)Phosphorylation-36.2022210691
494 (in isoform 2)Phosphorylation-3.3322210691
495PhosphorylationAGTLRALSRQDTFDA
HHHHHHHHCCCCCCC
27.23-
495 (in isoform 2)Phosphorylation-27.2322210691
499PhosphorylationRALSRQDTFDADTPG
HHHHCCCCCCCCCCC
18.3130624053
513 (in isoform 2)Phosphorylation-25.1726437602
540PhosphorylationGDPAGGGTPPARQGS
CCCCCCCCCCCCCCC
29.4024076635
547PhosphorylationTPPARQGSWEDEEED
CCCCCCCCCCCCHHH
20.9624719451
593MethylationNELEGWGRGVYIR--
CCCCCCCCCEECC--
25.54-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CACB1_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 CACB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NED4L_HUMANNEDD4Lphysical
19953087
A4_HUMANAPPphysical
21832049
CACB2_HUMANCACNB2physical
28514442
CACB3_HUMANCACNB3physical
28514442
CBARP_HUMANC19orf26physical
28514442
WDR75_HUMANWDR75physical
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
DB00898Ethanol
DB00308Ibutilide
DB00653Magnesium Sulfate
DB00393Nimodipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CACB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND MASSSPECTROMETRY.

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