CAC1C_HUMAN - dbPTM
CAC1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1C_HUMAN
UniProt AC Q13936
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1C
Gene Name CACNA1C
Organism Homo sapiens (Human).
Sequence Length 2221
Subcellular Localization Membrane
Multi-pass membrane protein . Cell membrane . The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane.
Protein Description Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. [PubMed: 29078335 The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function. STAC3 strongly decreases the rate of channel inactivation]
Protein Sequence MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL
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
6Phosphorylation--MVNENTRMYIPEE
--CCCCCCCEECCCC		15.61-
153N-linked_GlycosylationPFPEDDSNATNSNLE
CCCCCCCCCCCCHHH		58.75UniProtKB CARBOHYD
171PhosphorylationYLFLIIFTVEAFLKV
HHHHHHHHHHHHHHH		13.6626657352
260PhosphorylationSLQVVLNSIIKAMVP
CHHHHHHHHHHHHHH		22.8724719451
328N-linked_GlycosylationGHGRQCQNGTVCKPG
CCCCCCCCCCCCCCC		56.58UniProtKB CARBOHYD
465PhosphorylationEEKPRNMSMPTSETE
CCCCCCCCCCCCCCC		25.7622210691
468PhosphorylationPRNMSMPTSETESVN
CCCCCCCCCCCCCCC		30.4722210691
469PhosphorylationRNMSMPTSETESVNT
CCCCCCCCCCCCCCC		36.33-
476PhosphorylationSETESVNTENVAGGD
CCCCCCCCCCCCCCC		27.1222210691
808PhosphorylationEEKIELKSITADGES
HHCEEEEEEECCCCC		37.48-
815PhosphorylationSITADGESPPATKIN
EEECCCCCCCCEECC		41.5325307156
863PhosphorylationGPRPRPLSELHLKEK
CCCCCCHHHHCCCCC		40.5723312004
988PhosphorylationKGSFCRNYFNILDLL
CCCHHHHHHHHHHHH		4.43-
1003PhosphorylationVVSVSLISFGIQSSA
HHHHHHHHHCCCCHH		23.78-
1076PhosphorylationQLFKGKLYTCSDSSK
HHHCCEEEECCCCCC		14.80-
1077PhosphorylationLFKGKLYTCSDSSKQ
HHCCEEEECCCCCCC		18.90-
1130PhosphorylationAAMMALFTVSTFEGW
HHHHHHHHHHHCCCH		17.8822210691
1133PhosphorylationMALFTVSTFEGWPEL
HHHHHHHHCCCHHHH		22.7522210691
1142PhosphorylationEGWPELLYRSIDSHT
CCHHHHHHHHCCCCC		18.23-
1404PhosphorylationLLWTFIKSFQALPYV
HHHHHHHHCCHHHHH		20.13-
1410PhosphorylationKSFQALPYVALLIVM
HHCCHHHHHHHHHHH		10.13-
1436N-linked_GlycosylationVFGKIALNDTTEINR
HHHHHHCCCCCCCCC		35.24UniProtKB CARBOHYD
1487N-linked_GlycosylationAPESEPSNSTEGETP
CCCCCCCCCCCCCCC		64.76UniProtKB CARBOHYD
1535PhosphorylationDYLTRDWSILGPHHL
HHHHCCCHHCCHHHH		16.54-
1576 (in isoform 26)Phosphorylation-12.9722673903
1577 (in isoform 26)Phosphorylation-34.7322673903
1581 (in isoform 26)Phosphorylation-5.8622673903
1609PhosphorylationGTVMFNATLFALVRT
CCEEHHHHHHHHHHH		24.42-
1624 (in isoform 9)Phosphorylation-49.6122673903
1625 (in isoform 9)Phosphorylation-33.8922673903
1629 (in isoform 9)Phosphorylation-18.9422673903
1637 (in isoform 26)Phosphorylation-3.4726270265
1645PhosphorylationKKIWKRTSMKLLDQV
HHHHHHHCCHHHHCC		20.258664319
1667PhosphorylationEVTVGKFYATFLIQE
CEEHHHHHHHHHHHH		14.28-
1683AcetylationFRKFKKRKEQGLVGK
HHHHHHHHHHCCCCC		64.3711789837
1685 (in isoform 9)Phosphorylation-54.2626270265
1690AcetylationKEQGLVGKPSQRNAL
HHHCCCCCHHHHHHH		33.7311789853
1692PhosphorylationQGLVGKPSQRNALSL
HCCCCCHHHHHHHHH		45.3023312004
1718PhosphorylationPEIRRAISGDLTAEE
HHHHHHHCCCCCHHH		25.858664319
1736PhosphorylationKAMKEAVSAASEDDI
HHHHHHHHHHCCCHH		25.7627732954
1739PhosphorylationKEAVSAASEDDIFRR
HHHHHHHCCCHHHHH		41.0727732954
1760PhosphorylationNHVSYYQSDGRSAFP
CCEEEECCCCCCCCC		26.3828857561
1832PhosphorylationRLPRPAGYPSTVSTV
CCCCCCCCCCCCEEC		8.98-
1847PhosphorylationEGHGPPLSPAIRVQE
CCCCCCCCCCHHHHH		20.3323312004
1860PhosphorylationQEVAWKLSSNRERHV
HHHHHHCCCCCCCCC		23.1127542207
1861PhosphorylationEVAWKLSSNRERHVP
HHHHHCCCCCCCCCC		50.7927542207
1901PhosphorylationANPSRCHSRESQAAM
CCHHHCCCHHHHHHH		41.17-
1904PhosphorylationSRCHSRESQAAMAGQ
HHCCCHHHHHHHCCC		24.8222468782
1919PhosphorylationEETSQDETYEVKMNH
CCCCCCCCEEEECCC		33.0222468782
1920PhosphorylationETSQDETYEVKMNHD
CCCCCCCEEEECCCC		19.3717942635
1953PhosphorylationDDENRQLTLPEEDKR
CCCCCCCCCCHHHHH		31.7425690035
1973PhosphorylationPKRGFLRSASLGRRA
CCCCCCCHHHCCCHH		25.10-
1981PhosphorylationASLGRRASFHLECLK
HHCCCHHHHHHHHHH		16.0422310722
1998PhosphorylationKDRGGDISQKTVLPL
HHCCCCCCCCCCCCH		30.29-
2069PhosphorylationSSEKLNSSFPSIHCG
CHHHHHHCCCCCCCC		39.8530624053
2072PhosphorylationKLNSSFPSIHCGSWA
HHHHCCCCCCCCCCC		23.9730624053
2077PhosphorylationFPSIHCGSWAETTPG
CCCCCCCCCCCCCCC		28.6230624053
2081PhosphorylationHCGSWAETTPGGGGS
CCCCCCCCCCCCCCC		30.4630624053
2098PhosphorylationARRVRPVSLMVPSQA
HCCCCCEEEECCCCC		17.2723312004
2103PhosphorylationPVSLMVPSQAGAPGR
CEEEECCCCCCCCCC		22.66-
2126PhosphorylationLVEAVLISEGLGQFA
HHHHHHHHCCCHHHH		22.81-
2217PhosphorylationELQDSRVYVSSL---
HHHHCCEEECCC---		8.1017942635
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
1535SPhosphorylationKinasePRKACAP17612
GPS
1603TPhosphorylationKinaseCAMK2-FAMILY-GPS
1981SPhosphorylationKinasePKACAP17612
PSP
1981SPhosphorylationKinasePRKD1Q15139
PSP
1981SPhosphorylationKinasePKA-Uniprot
2217YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1981SPhosphorylation

28119464
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 CAC1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CABP1_HUMANCABP1physical
15140941
RYR2_HUMANRYR2physical
11576544
SORCN_HUMANSRIphysical
9668070
HDAC4_HUMANHDAC4physical
21464227
TERA_HUMANVCPphysical
21186355
DERL1_HUMANDERL1physical
21186355
TRI13_HUMANTRIM13physical
21186355
CSN5_HUMANCOPS5physical
16483597
KCNE2_HUMANKCNE2physical
24681347
Drug and Disease Associations
Kegg Disease
H00720 Long QT syndrome, including: Romano-Ward syndrome; Jervell and Lange-Nielsen syndrome (JLNS)
H00728 Brugada syndrome (BRS)
OMIM Disease
601005Timothy syndrome (TS)
611875Brugada syndrome 3 (BRGDA3)
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
DB06751Drotaverine
DB00898Ethanol
DB01023Felodipine
DB00308Ibutilide
DB00270Isradipine
DB00653Magnesium Sulfate
DB00622Nicardipine
DB01115Nifedipine
DB06712Nilvadipine
DB00393Nimodipine
DB00401Nisoldipine
DB01054Nitrendipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CAC1C_HUMAN

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