CAC1A_RAT - dbPTM
CAC1A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1A_RAT
UniProt AC P54282
Protein Name Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Gene Name Cacna1a
Organism Rattus norvegicus (Rat).
Sequence Length 2212
Subcellular Localization Cell 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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA)..
Protein Sequence MARFGDEMPGRYGAGGGGSGPAAGVVVGAAGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIVALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDVEQRHPFDGALRRATLKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSAKLENSTFFHKKERRMRFYIRRMVKTQAFYWTVLSLVALNTLWLAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYGLGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAAIMTVFQILTGEDWNEVMYDEIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTSEMRKQNLLASREALYGDAAERWPTTYARPLRPDVKTHLDRPLVVDPQENRNNNTNKSRAPEALRQTARPRESARDPDARRAWPSSPERAPGREGPYGRESEPQQREHAPPREHVPWDADPERAKAGDAPRRHTHRPVAEGEPRRHRARRRPGDEPDDRPERRPRPRDATRPARAADGEGDDGERKRRHRHGPPAHDDRERRHRRRKESQGSGVPMSGPNLSTTRPIQQDLGRQDLPLAEDLDNMKNNKLATGEPASPHDSLGHSGLPPSPAKIGNSTNPGPALATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSSTQPNSAKTARKPEHMAVEIPPACPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEADPGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIALAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIVVSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNILIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFERDCRGKYLLYEKNEVKARDREWKKYDFHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMWQFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAFGILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDGEDEDSDEDEFQITEHNNFRTFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGIQKPECGNEFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAACGRIHYKDMYSLLRVISPPLGLGKKCPHRVACKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMDAELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQNRTPLMFQRMEPPSPTQEGGPSQNALPSTQLDPGGGLMAQESSMKESPSWVTQRAQEMFQKTGTWSPERGPPIDMPNSQPNSQSVEMREMGTDGYSDSEHYLPMEGQTRAASMPRLPAENQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRYHQRRRDRGHRTSERSLGRYTDVDTGLGTDLSMTTQSGDLPSKDRDQDRGRPKDRKHRPHHHHHHHHHHPPAPDRERYAQERPDTGRARAREQRWSRSPSEGREHATHRQ
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
64PhosphorylationRARTMALYNPIPVRQ
HHHHHHHHCCCCCCC		14.89-
285N-linked_GlycosylationEPARTCPNGTKCQPY
CCCCCCCCCCCCCCC		73.28-
411PhosphorylationVILAEDETDVEQRHP
EEECCCCCCHHHHCC		58.6327115346
431PhosphorylationRRATLKKSKTDLLNP
HHHHHCCCHHCCCCH		38.9222673903
433PhosphorylationATLKKSKTDLLNPEE
HHHCCCHHCCCCHHH		38.6822673903
450PhosphorylationDQLADIASVGSPFAR
HHHHHHHHCCCHHHH		27.6128551015
453PhosphorylationADIASVGSPFARASI
HHHHHCCCHHHHHHH		18.0628551015
752PhosphorylationAKEVAEVSPLSAANM
HHHHHHHCCCCHHHH		16.1930240740
755PhosphorylationVAEVSPLSAANMSIA
HHHHCCCCHHHHHHH		28.8125403869
760PhosphorylationPLSAANMSIAVKEQQ
CCCHHHHHHHHHHHH		13.7528551015
792PhosphorylationRKQNLLASREALYGD
HHHHHHHHHHHHHHC		30.5325403869
797PhosphorylationLASREALYGDAAERW
HHHHHHHHHCHHHHC		21.73-
866PhosphorylationDARRAWPSSPERAPG
CHHHHCCCCCCCCCC		48.0728432305
867PhosphorylationARRAWPSSPERAPGR
HHHHCCCCCCCCCCC		27.0528432305
1038PhosphorylationLATGEPASPHDSLGH
CCCCCCCCCCCCCCC		33.2225403869
1042PhosphorylationEPASPHDSLGHSGLP
CCCCCCCCCCCCCCC		32.96-
1046PhosphorylationPHDSLGHSGLPPSPA
CCCCCCCCCCCCCCC		39.9828432305
1051PhosphorylationGHSGLPPSPAKIGNS
CCCCCCCCCCCCCCC		35.2325403869
1607N-linked_GlycosylationEFGNNFINLSFLRLF
ECCCCCCCHHHHHHH		26.04-
1773PhosphorylationEYLTRDSSILGPHHL
HHHCCCCCCCCCCCH		26.56-
1859AcetylationIRTALDIKIAKGGAD
HHHHHHHHHHCCCCC		35.9622902405
1935PhosphorylationMREEQNRTPLMFQRM
HHHHHCCCCCCCEEC		28.4628432305
1946PhosphorylationFQRMEPPSPTQEGGP
CEECCCCCCCCCCCC		51.8222673903
1948PhosphorylationRMEPPSPTQEGGPSQ
ECCCCCCCCCCCCCC		43.5222673903
1981PhosphorylationSSMKESPSWVTQRAQ
CCCCCCCHHHHHHHH		43.3828432305
1994PhosphorylationAQEMFQKTGTWSPER
HHHHHHHHCCCCCCC		29.1222673903
1996PhosphorylationEMFQKTGTWSPERGP
HHHHHHCCCCCCCCC		28.1822673903
1998PhosphorylationFQKTGTWSPERGPPI
HHHHCCCCCCCCCCC		19.4030240740
2016PhosphorylationNSQPNSQSVEMREMG
CCCCCCCCCCHHHCC		21.62-
2024PhosphorylationVEMREMGTDGYSDSE
CCHHHCCCCCCCCCC		25.5822673903
2027PhosphorylationREMGTDGYSDSEHYL
HHCCCCCCCCCCCCC		16.4722673903
2028PhosphorylationEMGTDGYSDSEHYLP
HCCCCCCCCCCCCCC		39.9430240740
2030PhosphorylationGTDGYSDSEHYLPME
CCCCCCCCCCCCCCC		21.9722673903
2033PhosphorylationGYSDSEHYLPMEGQT
CCCCCCCCCCCCCCC		14.4022673903
2068PhosphorylationGNNLSTISDTSPMKR
CCCCCCCCCCCCCCC		34.6225403869
2070PhosphorylationNLSTISDTSPMKRSA
CCCCCCCCCCCCCCH		28.1222673903
2071PhosphorylationLSTISDTSPMKRSAS
CCCCCCCCCCCCCHH		28.1725403869
2076PhosphorylationDTSPMKRSASVLGPK
CCCCCCCCHHHHCCC		21.2728432305
2078PhosphorylationSPMKRSASVLGPKAR
CCCCCCHHHHCCCCC		21.0828432305
2090PhosphorylationKARRLDDYSLERVPP
CCCCCCCCCCCCCCC		18.1525403869
2091PhosphorylationARRLDDYSLERVPPE
CCCCCCCCCCCCCCH		30.651279681
2198PhosphorylationRAREQRWSRSPSEGR
HHHHHHHCCCCCCCC		25.6822673903
2200PhosphorylationREQRWSRSPSEGREH
HHHHHCCCCCCCCCC		27.5425403869
2202PhosphorylationQRWSRSPSEGREHAT
HHHCCCCCCCCCCCC		54.6625403869
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 CAC1A_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1A_RAT !!
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 CAC1A_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAP1B_RATMap1bphysical
25483588
RN138_RATRnf138physical
28167673
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAC1A_RAT

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Related Literatures of Post-Translational Modification

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