CAC1D_MOUSE - dbPTM
CAC1D_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1D_MOUSE
UniProt AC Q99246
Protein Name Voltage-dependent L-type calcium channel subunit alpha-1D
Gene Name Cacna1d
Organism Mus musculus (Mouse).
Sequence Length 2179
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 MMMMMMMKKMQHQRQHQEDHANEANYARGTRLPISGEGPTSQPNSSKQTVLSWQAAIDAARQAKAAQTMSTSAPPPVGSLSQRKRQQYAKSKKQGNSSNSRPARALFCLSLNNPIRRACISIVEWKPFDIFILLAIFANCVALAIYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVIVGLFSVILEQLTKETEGGNHSSGKSGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKTCFFADSDIVAEEDPAPCAFSGNGRQCTANGTECRSGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAIGWEWPWVYFVSLIILGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEEEGGEEGKRNTSMPTSETESVNTENVSGEGETQGCCGTLWCWWKRRGAAKTGPSGCRRWGQAISKSKLSRRWRRWNRFNRRRCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGITETILVELELMSPLGVSVFRCVRLLRIFKVTRHWTSLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKIARKESLENKKNNKPEVNQIANSDNKVTIDDYQEDAEDKDPYPPCDVPVGEEEEEEEEDEPEVPAGPRPRRISELNMKEKIAPIPEGSAFFILSKTNPIRVGCHKLINHHIFTNLILVFIMLSSAALAAEDPIRSHSFRNTILGYFDYAFTAIFTVEILLKMTTFGAFLHKGAFCRNYFNLLDMLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYRCTDEAKSNPEECRGLFILYKDGDVDSPVVRERIWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENVGPVYNYRVEISIFFIIYIIIVAFFMMNIFVGFVIVTFQEQGEKEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSSPFEYMMFVLIMLNTLCLAMQHYEQSKMFNDAMDILNMVFTGVFTVEMVLKVIAFKPKGYFSDAWNTFDSLIVIGSIIDVALSEADPSESETIPLPTATPGNSEESNRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQMFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKLCDPDSDYNPGEEYTCGSNFAIVYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEDSKPEEEDVFKRNGALLGNHVNHVNSDRRDSLQQTNTTHRPLHVQRPSMPPASDTEKPLFPPAGNSGCHNHHNHNSIGKQAPTSTNANLNNANMSKAAHGKPPSIGNLEHVSENGHYSCKHDRELQRRSSIKRTRYYETYIRSESGDEQFPTICREDPEIHGYFRDPRCLGEQEYFSSEECCEDDSSPTWSRQNYNYYNRYPGSSMDFERPRGYHHPQGFLEDDDSPTGYDSRRSPRRRLLPPTPPSHRRSSFNFECLRRQSSQDDVLPSPALPHRAALPLHLMQQQIMAVAGLDSSKAQKYSPSHSTRSWATPPATPPYRDWSPCYTPLIQVDRSESMDQVNGSLPSLHRSSWYTDEPDISYRTFTPASLTVPSSFRNKNSDKQRSADSLVEAVLISEGLGRYARDPKFVSATKHEIADACDLTIDEMESAASTLLNGSVCPRANGDMGPISHRQDYELQDFGPGYSDEEPDPGREEEDLADEMICITTL
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
68PhosphorylationRQAKAAQTMSTSAPP
HHHHHHHHCCCCCCC		14.3630635358
70PhosphorylationAKAAQTMSTSAPPPV
HHHHHHCCCCCCCCC		23.6930635358
71PhosphorylationKAAQTMSTSAPPPVG
HHHHHCCCCCCCCCC		20.3430635358
72PhosphorylationAAQTMSTSAPPPVGS
HHHHCCCCCCCCCCC		31.3230635358
79PhosphorylationSAPPPVGSLSQRKRQ
CCCCCCCCHHHHHHH		25.6930635358
81PhosphorylationPPPVGSLSQRKRQQY
CCCCCCHHHHHHHHH		29.6330635358
98PhosphorylationSKKQGNSSNSRPARA
HHCCCCCCCCCCHHH		42.71-
108S-palmitoylationRPARALFCLSLNNPI
CCHHHHHHHHCCCHH		2.3428680068
469PhosphorylationRNTSMPTSETESVNT
CCCCCCCCCCCCCCC		36.33-
473PhosphorylationMPTSETESVNTENVS
CCCCCCCCCCCCCCC		28.25-
499MethylationLWCWWKRRGAAKTGP
EHHHHHHCCCCCCCC		35.06-
802PhosphorylationKKIARKESLENKKNN
HHHHHHHHHHHHHCC		43.9827841257
869PhosphorylationGPRPRRISELNMKEK
CCCCCCHHHCCCCCC		33.9329899451
989PhosphorylationVVGVSLVSFGIQSSA
HHHHHHHHCCCCHHH		24.05-
1190UbiquitinationYKNCELDKNQRQCVE
HCCCCCCHHHHHHHH		68.55-
1495PhosphorylationDYLTRDWSILGPHHL
HHHHCCCHHCCHHHH		16.5420479240
1510PhosphorylationDEFKRIWSEYDPEAK
HHHHHHHHHCCHHHC		24.73-
1643AcetylationFRKFKKRKEQGLVGK
HHHHHHHHHCCCCCC		64.3719861999
1679PhosphorylationPEIRRAISCDLQDDE
HHHHHHHCCCCCCCC		10.7025521595
1719PhosphorylationVNSDRRDSLQQTNTT
CCCCCHHHHHHCCCC		26.68-
1792PhosphorylationAAHGKPPSIGNLEHV
HHCCCCCCCCCCCCC		52.2126745281
1800PhosphorylationIGNLEHVSENGHYSC
CCCCCCCCCCCCCCC		27.5326745281
1818PhosphorylationRELQRRSSIKRTRYY
HHHHHHHHCCCCHHE		30.25-
1827PhosphorylationKRTRYYETYIRSESG
CCCHHEEEEECCCCC		14.23-
1831PhosphorylationYYETYIRSESGDEQF
HEEEEECCCCCCCCC		26.9322807455
1833PhosphorylationETYIRSESGDEQFPT
EEEECCCCCCCCCCC		53.4421082442
1877PhosphorylationCEDDSSPTWSRQNYN
CCCCCCCCCCCCCCC		37.71-
1879PhosphorylationDDSSPTWSRQNYNYY
CCCCCCCCCCCCCCC		26.85-
1883PhosphorylationPTWSRQNYNYYNRYP
CCCCCCCCCCCCCCC		9.01-
1914PhosphorylationGFLEDDDSPTGYDSR
CCCCCCCCCCCCCCC		31.2125521595
1916PhosphorylationLEDDDSPTGYDSRRS
CCCCCCCCCCCCCCC		52.9429899451
1920PhosphorylationDSPTGYDSRRSPRRR
CCCCCCCCCCCCCCC		22.5529899451
1923PhosphorylationTGYDSRRSPRRRLLP
CCCCCCCCCCCCCCC		22.9629899451
1940PhosphorylationPPSHRRSSFNFECLR
CCCCCCCCCCHHHHH		23.5422817900
1950PhosphorylationFECLRRQSSQDDVLP
HHHHHCCCCCCCCCC		28.3127841257
1951PhosphorylationECLRRQSSQDDVLPS
HHHHCCCCCCCCCCC		29.3229899451
1958PhosphorylationSQDDVLPSPALPHRA
CCCCCCCCCCCCCHH		20.7427841257
2001PhosphorylationHSTRSWATPPATPPY
CCCCCCCCCCCCCCC		24.4422817900
2005PhosphorylationSWATPPATPPYRDWS
CCCCCCCCCCCCCCC		30.4822817900
2008PhosphorylationTPPATPPYRDWSPCY
CCCCCCCCCCCCCCC		23.5421082442
2053PhosphorylationEPDISYRTFTPASLT
CCCCCEEEECCHHHC		24.5128576409
2055PhosphorylationDISYRTFTPASLTVP
CCCEEEECCHHHCCC		19.8224759943
2058PhosphorylationYRTFTPASLTVPSSF
EEEECCHHHCCCHHH		26.2724759943
2075PhosphorylationKNSDKQRSADSLVEA
CCCCCCCCHHHHHHH		33.6527841257
2078PhosphorylationDKQRSADSLVEAVLI
CCCCCHHHHHHHHHH		33.7527841257
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1D_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX1A_MOUSEStx1aphysical
10468580
AT1A1_MOUSEAtp1a1physical
10468580
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAC1D_MOUSE

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Related Literatures of Post-Translational Modification

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