CAC1D_HUMAN - dbPTM
CAC1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1D_HUMAN
UniProt AC Q01668
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1D
Gene Name CACNA1D
Organism Homo sapiens (Human).
Sequence Length 2161
Subcellular Localization Membrane
Multi-pass membrane protein .
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. The isoform alpha-1D 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)..
Protein Sequence MMMMMMMKKMQHQRQQQADHANEANYARGTRLPLSGEGPTSQPNSSKQTVLSWQAAIDAARQAKAAQTMSTSAPPPVGSLSQRKRQQYAKSKKQGNSSNSRPARALFCLSLNNPIRRACISIVEWKPFDIFILLAIFANCVALAIYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVIVGLFSVILEQLTKETEGGNHSSGKSGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKTCFFADSDIVAEEDPAPCAFSGNGRQCTANGTECRSGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWMNDAMGFELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEEEGGEEGKRNTSMPTSETESVNTENVSGEGENRGCCGSLCQAISKSKLSRRWRRWNRFNRRRCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGITETILVELEIMSPLGISVFRCVRLLRIFKVTRHWTSLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKIARKESLENKKNNKPEVNQIANSDNKVTIDDYREEDEDKDPYPPCDVPVGEEEEEEEEDEPEVPAGPRPRRISELNMKEKIAPIPEGSAFFILSKTNPIRVGCHKLINHHIFTNLILVFIMLSSAALAAEDPIRSHSFRNTILGYFDYAFTAIFTVEILLKMTTFGAFLHKGAFCRNYFNLLDMLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYRCTDEAKSNPEECRGLFILYKDGDVDSPVVRERIWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENIGPIYNHRVEISIFFIIYIIIVAFFMMNIFVGFVIVTFQEQGEKEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSSPFEYMMFVLIMLNTLCLAMQHYEQSKMFNDAMDILNMVFTGVFTVEMVLKVIAFKPKGYFSDAWNTFDSLIVIGSIIDVALSEADPTESENVPVPTATPGNSEESNRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQMFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKLCDPESDYNPGEEYTCGSNFAIVYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEETKREEEDDVFKRNGALLGNHVNHVNSDRRDSLQQTNTTHRPLHVQRPSIPPASDTEKPLFPPAGNSVCHNHHNHNSIGKQVPTSTNANLNNANMSKAAHGKRPSIGNLEHVSENGHHSSHKHDREPQRRSSVKRTRYYETYIRSDSGDEQLPTICREDPEIHGYFRDPHCLGEQEYFSSEECYEDDSSPTWSRQNYGYYSRYPGRNIDSERPRGYHHPQGFLEDDDSPVCYDSRRSPRRRLLPPTPASHRRSSFNFECLRRQSSQEEVPSSPIFPHRTALPLHLMQQQIMAVAGLDSSKAQKYSPSHSTRSWATPPATPPYRDWTPCYTPLIQVEQSEALDQVNGSLPSLHRSSWYTDEPDISYRTFTPASLTVPSSFRNKNSDKQRSADSLVEAVLISEGLGRYARDPKFVSATKHEIADACDLTIDEMESAASTLLNGNVRPRANGDVGPLSHRQDYELQDFGPGYSDEEPDPGRDEEDLADEMICITTL
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
45PhosphorylationGPTSQPNSSKQTVLS
CCCCCCCCCCHHHHH		45.6719276368
71PhosphorylationKAAQTMSTSAPPPVG
HHHHHHCCCCCCCCC		20.3422210691
72PhosphorylationAAQTMSTSAPPPVGS
HHHHHCCCCCCCCCC		31.3222210691
79PhosphorylationSAPPPVGSLSQRKRQ
CCCCCCCCHHHHHHH		25.6922210691
81PhosphorylationPPPVGSLSQRKRQQY
CCCCCCHHHHHHHHH		29.6330387612
155N-linked_GlycosylationPFPEDDSNSTNHNLE
CCCCCCCCCCCCCHH		60.90UniProtKB CARBOHYD
225N-linked_GlycosylationTKETEGGNHSSGKSG
HCCCCCCCCCCCCCC		42.60UniProtKB CARBOHYD
263PhosphorylationSLQVVLNSIIKAMVP
CHHHHHHHHHHHHHH		22.8724719451
329N-linked_GlycosylationNGRQCTANGTECRSG
CCCEEECCCCCCCCC		39.50UniProtKB CARBOHYD
464PhosphorylationGEEGKRNTSMPTSET
CCCCCCCCCCCCCCC		30.3622210691
469PhosphorylationRNTSMPTSETESVNT
CCCCCCCCCCCCCCC		36.33-
473PhosphorylationMPTSETESVNTENVS
CCCCCCCCCCCCCCC		28.25-
476PhosphorylationSETESVNTENVSGEG
CCCCCCCCCCCCCCC		27.1222210691
480PhosphorylationSVNTENVSGEGENRG
CCCCCCCCCCCCCCC		42.5822210691
507 (in isoform 2)Phosphorylation-28.23-
637PhosphorylationTRHWTSLSNLVASLL
HCCHHHHHHHHHHHH		28.0819651622
642PhosphorylationSLSNLVASLLNSMKS
HHHHHHHHHHHHHHH		26.3819651622
799PhosphorylationEVNQIANSDNKVTID
HHHHHCCCCCCEEHH		33.2727794612
849PhosphorylationGPRPRRISELNMKEK
CCCCCCHHHCCCCCC		33.9324719451
869 (in isoform 2)Phosphorylation-3.4724719451
1346PhosphorylationLLWTFIKSFQALPYV
HHHHHHHHCCHHHHH		20.13-
1475PhosphorylationDYLTRDWSILGPHHL
HHHHCCCHHCCHHHH		16.54-
1490PhosphorylationDEFKRIWSEYDPEAK
HHHHHHHHHCCHHHC		24.7316763033
1510 (in isoform 2)Phosphorylation-36.4524719451
1540PhosphorylationAMNMPLNSDGTVMFN
HCCCCCCCCCCEEHH		45.1322210691
1543PhosphorylationMPLNSDGTVMFNATL
CCCCCCCCEEHHHHH		17.4922210691
1549PhosphorylationGTVMFNATLFALVRT
CCEEHHHHHHHHHHH		24.42-
1700PhosphorylationVNSDRRDSLQQTNTT
CCCCCHHHHHHCCCC		26.68-
1807PhosphorylationSVKRTRYYETYIRSD
HHCHHEEEEEEECCC		9.8618083107
1809PhosphorylationKRTRYYETYIRSDSG
CHHEEEEEEECCCCC		14.2324719451
1810PhosphorylationRTRYYETYIRSDSGD
HHEEEEEEECCCCCC		5.1718083107
1813PhosphorylationYYETYIRSDSGDEQL
EEEEEECCCCCCCCC		26.9426270265
1815PhosphorylationETYIRSDSGDEQLPT
EEEECCCCCCCCCCC		49.7626270265
1822PhosphorylationSGDEQLPTICREDPE
CCCCCCCCCCCCCCC		41.1026270265
1829 (in isoform 2)Phosphorylation-61.0024719451
1865PhosphorylationPTWSRQNYGYYSRYP
CCCCCCCCCCCCCCC		9.73-
1867PhosphorylationWSRQNYGYYSRYPGR
CCCCCCCCCCCCCCC		6.47-
1905PhosphorylationVCYDSRRSPRRRLLP
CCCCCCCCCCCCCCC		22.9617081983
2042PhosphorylationTFTPASLTVPSSFRN
EECCHHHCCCHHHCC		28.0726434552
2045PhosphorylationPASLTVPSSFRNKNS
CHHHCCCHHHCCCCC		37.4626434552
2046PhosphorylationASLTVPSSFRNKNSD
HHHCCCHHHCCCCCC		23.3526434552
2052PhosphorylationSSFRNKNSDKQRSAD
HHHCCCCCCCHHCHH		48.0426434552
2082PhosphorylationARDPKFVSATKHEIA
HCCCHHHCCCHHHHH		33.1022210691
2101PhosphorylationLTIDEMESAASTLLN
CCHHHHHHHHHHHHC		28.0222210691
2104PhosphorylationDEMESAASTLLNGNV
HHHHHHHHHHHCCCC		21.2122210691
2123PhosphorylationNGDVGPLSHRQDYEL
CCCCCCCCCCCCCCC		21.54-
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 CAC1D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1D_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 CAC1D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAC1D_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614896Sinoatrial node dysfunction and deafness (SANDD)
615474Primary aldosteronism, seizures, and neurologic abnormalities (PASNA)
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
DB00622Nicardipine
DB01115Nifedipine
DB06712Nilvadipine
DB00393Nimodipine
DB00401Nisoldipine
DB01054Nitrendipine
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CAC1D_HUMAN

loading...

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 SER-1905, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory