CAC1S_HUMAN - dbPTM
CAC1S_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1S_HUMAN
UniProt AC Q13698
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1S
Gene Name CACNA1S
Organism Homo sapiens (Human).
Sequence Length 1873
Subcellular Localization Cell membrane, sarcolemma
Multi-pass membrane protein . Detected on T-tubules (extensions of the sarcolemma).
Protein Description Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group..
Protein Sequence MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLENPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFTIVFLGVFTVILEQVNVIQSHTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEEPSPCARTGSGRRCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLDEDLRGYMSWITQGEVMDVEDFREGKLSLDEGGSDTESLYEIAGLNKIIQFIRHWRQWNRIFRWKCHDIVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTRLQDIANRVLLSLFTTEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRIFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIVIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWTSMMYNGIMAYGGPSYPGMLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEEKKRRKMSKGLPDKSEEEKSTMAKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPLSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILKHFDIGFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNMLDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCMFVAISTIGNIVLVTTLLQFMFACIGVQLFKGKFFRCTDLSKMTEEECRGYYYVYKDGDPMQIELRHREWVHSDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNAEDVGPIYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYIVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLMAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLVINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDIVQIQAGLRTIEEEAAPEICRTVSGDLAAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEEMESPVFLEDFPQDPRTNPLARANTNNANANVAYGNSNHSNSHVFSSVHYEREFPEETETPATRGRALGQPCRVLGPHSKPCVEMLKGLLTQRAMPRGQAPPAPCQCPRVESSMPEDRKSSTPGSLHEETPHSRSTRENTSRCSAPATALLIQKALVRGGLGTLAADANFIMATGQALADACQMEPEEVEIMATELLKGREAPEGMASSLGCLNLGSSLGSLDQHQGSQETLIPPRL
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
79N-linked_GlycosylationLPMPEDDNNSLNLGL
CCCCCCCCCCCCCCH		52.92UniProtKB CARBOHYD
188PhosphorylationSLQVVLNSIFKAMLP
CHHHHHHHHHHHHHH		25.8224719451
225PhosphorylationFKGKMHKTCYFIGTD
HCCCCCCCEEEECCC		9.58-
231PhosphorylationKTCYFIGTDIVATVE
CCEEEECCCEEEEEC		20.10-
236PhosphorylationIGTDIVATVENEEPS
ECCCEEEEECCCCCC		19.91-
257N-linked_GlycosylationSGRRCTINGSECRGG
CCCCCEECCCCCCCC		29.77UniProtKB CARBOHYD
343AcetylationEFTKEREKAKSRGTF
CCHHHHHHHHHCHHH		68.307718085
345AcetylationTKEREKAKSRGTFQK
HHHHHHHHHCHHHHH		52.327824037
352AcetylationKSRGTFQKLREKQQL
HHCHHHHHHHHHHCC		45.377824049
387PhosphorylationDFREGKLSLDEGGSD
HHHCCCEECCCCCCC		36.9422673903
393PhosphorylationLSLDEGGSDTESLYE
EECCCCCCCHHHHHH		52.8222673903
395PhosphorylationLDEGGSDTESLYEIA
CCCCCCCHHHHHHHH		29.2122673903
397PhosphorylationEGGSDTESLYEIAGL
CCCCCHHHHHHHHCH		38.0422673903
399PhosphorylationGSDTESLYEIAGLNK
CCCHHHHHHHHCHHH		17.99-
473PhosphorylationIANRVLLSLFTTEML
HHHHHHHHHHHHHHH		19.7824719451
476PhosphorylationRVLLSLFTTEMLMKM
HHHHHHHHHHHHHHH		27.4324719451
477PhosphorylationVLLSLFTTEMLMKMY
HHHHHHHHHHHHHHH		16.4424719451
555PhosphorylationLVASLLNSIRSIASL
HHHHHHHHHHHHHHH		21.2424719451
687PhosphorylationEKKRRKMSKGLPDKS
HHHHHHHHCCCCCCC		26.972844809
694PhosphorylationSKGLPDKSEEEKSTM
HCCCCCCCHHHHHHH		58.5826437602
799PhosphorylationCHRIVNATWFTNFIL
HHHHHCHHHHHHHHH		18.86-
802PhosphorylationIVNATWFTNFILLFI
HHCHHHHHHHHHHHH		22.30-
958PhosphorylationKGKFFRCTDLSKMTE
CCCEEEECCHHHCCH		35.4030242111
961PhosphorylationFFRCTDLSKMTEEEC
EEEECCHHHCCHHHH		24.1630242111
964PhosphorylationCTDLSKMTEEECRGY
ECCHHHCCHHHHCCE		43.9430242111
971PhosphorylationTEEECRGYYYVYKDG
CHHHHCCEEEEEECC		3.3922817900
972PhosphorylationEEECRGYYYVYKDGD
HHHHCCEEEEEECCC		6.8422817900
973PhosphorylationEECRGYYYVYKDGDP
HHHCCEEEEEECCCE		6.7122817900
975PhosphorylationCRGYYYVYKDGDPMQ
HCCEEEEEECCCEEE		6.2922817900
1035PhosphorylationAEDVGPIYNNRVEMA
CCCCCCCCCCHHHHH		14.98-
1141N-linked_GlycosylationCLGMQHYNQSEQMNH
HHHCCCCCCHHHHHH		36.46UniProtKB CARBOHYD
1263PhosphorylationLLWTFIKSFQALPYV
HHHHHHHHHCHHHHH		20.13-
1269PhosphorylationKSFQALPYVALLIVM
HHHCHHHHHHHHHHH		10.13-
1392PhosphorylationDYLTRDWSILGPHHL
HHHHCCCHHCCCCCH		16.54-
1502PhosphorylationKKIWKRTSMKLLDQV
HHHHHHHHCHHHHCC		20.258664319
1524PhosphorylationEVTVGKFYATFLIQE
CEECHHHHHHHHHHH		14.28-
1573PhosphorylationAAPEICRTVSGDLAA
HHHHHHHHHCCCCCH		18.0219764811
1575PhosphorylationPEICRTVSGDLAAEE
HHHHHHHCCCCCHHH		26.4419764811
1601PhosphorylationEEGIFRRTGGLFGQV
HHCCHHHCCCHHHCH		31.2029396449
1617PhosphorylationNFLERTNSLPPVMAN
HHHHHHCCCCCCCCC		41.462844809
1716AcetylationRVLGPHSKPCVEMLK
EECCCCCHHHHHHHH		39.1318586639
1723AcetylationKPCVEMLKGLLTQRA
HHHHHHHHHHHHHCC		46.3218586649
1757PhosphorylationMPEDRKSSTPGSLHE
CCCCHHCCCCCCCCC		41.471322891
1844PhosphorylationEAPEGMASSLGCLNL
CCCCHHHHHCCCCCC		19.7330257219
1854PhosphorylationGCLNLGSSLGSLDQH
CCCCCCCCCCCCCCC		34.641322891
1867PhosphorylationQHQGSQETLIPPRL-
CCCCCCCCCCCCCC-		23.5030257219
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
687SPhosphorylationKinasePKA-Uniprot
1575SPhosphorylationKinasePKA-Uniprot
1575SPhosphorylationKinaseCAMK2-Uniprot
1617SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1575SPhosphorylation

-
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 CAC1S_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SORCN_HUMANSRIphysical
9668070
2ABA_HUMANPPP2R2Aphysical
22863883
NHRF4_HUMANPDZD3physical
25416956
Drug and Disease Associations
Kegg Disease
H00746 Hypokalemic periodic paralysis (HypoPP)
OMIM Disease
170400Periodic paralysis hypokalemic 1 (HOKPP1)
601887Malignant hyperthermia 5 (MHS5)
188580Thyrotoxic periodic paralysis 1 (TTPP1)
Kegg Drug
D00319 Felodipine (JAN/USP/INN); Plendil (TN)
D00349 Isradipine (USP/INN); Dynacirc (TN)
D00437 Nifedipine (JP16/USP/INN); Adalat (TN); Afeditab CR (TN); Procardia (TN)
D00438 Nimodipine (USAN/INN); Nimotop (TN); Nymalize (TN)
D00537 Topiramate (JAN/USAN/INN); Topamax (TN); Trokendi xr (TN)
D00615 Amlodipine besilate (JP16); Amlodipine besylate (USAN); Norvasc (TN)
D00616 Diltiazem hydrochloride (JP16/USP); Cardizem (TN); Cartia XT (TN); Dilacor XR (TN); Dilt-CD (TN)
D00617 Nicardipine hydrochloride (JP16/USAN); Cardene (TN)
D00618 Nisoldipine (JAN/USAN/INN); Sular (TN)
D00619 Verapamil hydrochloride (JP16/USP); Calan (TN); Covera-hs (TN); Vasolan (TN); Verelan (TN)
D00629 Nitrendipine (JP16/USAN/INN); Baypress (TN)
D00631 Bepridil hydrochloride hydrate (JAN); Bepridil hydrochloride (USAN); Vascor (TN)
D01104 Barnidipine hydrochloride (JAN); Hypoca (TN)
D01145 Azelnidipine (JP16/INN); Calblock (TN)
D01173 Cilnidipine (JAN/INN); Atelec (TN)
D01553 Manidipine hydrochloride (JP16); Manidipine dihydrochloride; Calslot (TN)
D01562 Aranidipine (JAN/INN); Sapresta (TN)
D01604 Efonidipine hydrochloride ethanolate (JAN); Efonidipine hydrochloride ethanol; Efonidipine hydrochlo
D01849 Lercanidipine hydrochloride (JAN/USAN); Cardiovasc (TN)
D01908 Nilvadipine (JP16/USAN/INN); Nivadil (TN)
D01969 Gallopamil hydrochloride (JAN)
D02045 Benidipine hydrochloride (JP16); KW 3049; Coniel (TN)
D02356 Verapamil (USAN/INN)
D02537 Dronedarone (INN)
D02914 Amlodipine maleate (USAN); Amvaz (TN)
D03655 Darodipine (USAN/INN)
D03830 Diltiazem malate (USAN); Tiamate (TN)
D03914 Dronedarone hydrochloride (USAN); Multaq (TN)
D04657 Lacidipine (USAN/INN); Motens (TN)
D05442 Perhexiline maleate (USAN)
D07185 Fendiline (INN)
D07450 Amlodipine (INN); Norvasc (TN)
D07494 Barnidipine (INN); Vasexten (TN)
D07509 Benidipine (INN)
D07520 Bepridil (INN); Bepadin (TN)
D07845 Diltiazem (INN); Surazem (TN)
D07886 Efonidipine (INN)
D08009 Gallopamil (INN)
D08111 Lercanidipine (INN); Lercanil (TN)
D08155 Manidipine (INN); Manidipine 6300; Artedil (TN)
D08270 Nicardipine (INN); Cardene (TN)
D08340 Perhexiline (INN)
D08892 Clevidipine (USAN/INN); Clevidipine butyrate; Cleviprex (TN)
D09789 Kirenidipine hydrochloride (JAN)
DrugBank
DB00381Amlodipine
DB00568Cinnarizine
DB04920Clevidipine
DB04855Dronedarone
DB00898Ethanol
DB01023Felodipine
DB00270Isradipine
DB00653Magnesium Sulfate
DB01115Nifedipine
DB06712Nilvadipine
DB00393Nimodipine
DB00401Nisoldipine
DB01054Nitrendipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CAC1S_HUMAN

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Related Literatures of Post-Translational Modification

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