CAC1I_HUMAN - dbPTM
CAC1I_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1I_HUMAN
UniProt AC Q9P0X4
Protein Name Voltage-dependent T-type calcium channel subunit alpha-1I
Gene Name CACNA1I
Organism Homo sapiens (Human).
Sequence Length 2223
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. This channel gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by nickel and mibefradil. A particularity of this type of channels is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes. Gates in voltage ranges similar to, but higher than alpha 1G or alpha 1H (By similarity)..
Protein Sequence MAESASPPSSSAAAPAAEPGVTTEQPGPRSPPSSPPGLEEPLDGADPHVPHPDLAPIAFFCLRQTTSPRNWCIKMVCNPWFECVSMLVILLNCVTLGMYQPCDDMDCLSDRCKILQVFDDFIFIFFAMEMVLKMVALGIFGKKCYLGDTWNRLDFFIVMAGMVEYSLDLQNINLSAIRTVRVLRPLKAINRVPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIIGVQLWAGLLRNRCFLEENFTIQGDVALPPYYQPEEDDEMPFICSLSGDNGIMGCHEIPPLKEQGRECCLSKDDVYDFGAGRQDLNASGLCVNWNRYYNVCRTGSANPHKGAINFDNIGYAWIVIFQVITLEGWVEIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQREHRLMLEQRQRYLSSSTVASYAEPGDCYEEIFQYVCHILRKAKRRALGLYQALQSRRQALGPEAPAPAKPGPHAKEPRHYHGKTKGQGDEGRHLGSRHCQTLHGPASPGNDHSGRELCPQHSPLDATPHTLVQPIPATLASDPASCPCCQHEDGRRPSGLGSTDSGQEGSGSGSSAGGEDEADGDGARSSEDGASSELGKEEEEEEQADGAVWLCGDVWRETRAKLRGIVDSKYFNRGIMMAILVNTVSMGIEHHEQPEELTNILEICNVVFTSMFALEMILKLAAFGLFDYLRNPYNIFDSIIVIISIWEIVGQADGGLSVLRTFRLLRVLKLVRFMPALRRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHIFGCKFSLRTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSPWASLYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSYSDEDQSSSNIEEFDKLQEGLDSSGDPKLCPIPMTPNGHLDPSLPLGGHLGPAGAAGPAPRLSLQPDPMLVALGSRKSSVMSLGRMSYDQRSLSSSRSSYYGPWGRSAAWASRRSSWNSLKHKPPSAEHESLLSAERGGGARVCEVAADEGPPRAAPLHTPHAHHIHHGPHLAHRHRHHRRTLSLDNRDSVDLAELVPAVGAHPRAAWRAAGPAPGHEDCNGRMPSIAKDVFTKMGDRGDRGEDEEEIDYTLCFRVRKMIDVYKPDWCEVREDWSVYLFSPENRFRVLCQTIIAHKLFDYVVLAFIFLNCITIALERPQIEAGSTERIFLTVSNYIFTAIFVGEMTLKVVSLGLYFGEQAYLRSSWNVLDGFLVFVSIIDIVVSLASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLKPIGNIVLICCAFFIIFGILGVQLFKGKFYHCLGVDTRNITNRSDCMAANYRWVHHKYNFDNLGQALMSLFVLASKDGWVNIMYNGLDAVAVDQQPVTNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLEKKRRKAQRLPYYATYCHTRLLIHSMCTSHYLDIFITFIICLNVVTMSLEHYNQPTSLETALKYCNYMFTTVFVLEAVLKLVAFGLRRFFKDRWNQLDLAIVLLSVMGITLEEIEINAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGKLVCNDENPCEGMSRHATFENFGMAFLTLFQVSTGDNWNGIMKDTLRDCTHDERSCLSSLQFVSPLYFVSFVLTAQFVLINVVVAVLMKHLDDSNKEAQEDAEMDAELELEMAHGLGPGPRLPTGSPGAPGRGPGGAGGGGDTEGGLCRRCYSPAQENLWLDSVSLIIKDSLEGELTIIDNLSGSIFHHYSSPAGCKKCHHDKQEVQLAETEAFSLNSDRSSSILLGDDLSLEDPTACPPGRKDSKGELDPPEPMRVGDLGECFFPLSSTAVSPDPENFLCEMEEIPFNPVRSWLKHDSSQAPPSPFSPDASSPLLPMPAEFFHPAVSASQKGPEKGTGTGTLPKIALQGSWASLRSPRVNCTLLRQATGSDTSLDASPSSSAGSLQTTLEDSLTLSDSPRRALGPPAPAPGPRAGLSPAARRRLSLRGRGLFSLRGLRAHQRSHSSGGSTSPGCTHHDSMDPSDEEGRGGAGGGGAGSEHSETLSSLSLTSLFCPPPPPPAPGLTPARKFSSTSSLAAPGRPHAAALAHGLARSPSWAADRSKDPPGRAPLPMGLGPLAPPPQPLPGELEPGDAASKRKR
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
22PhosphorylationPAAEPGVTTEQPGPR
CCCCCCCCCCCCCCC		30.4529978859
23PhosphorylationAAEPGVTTEQPGPRS
CCCCCCCCCCCCCCC		30.1629978859
149PhosphorylationKKCYLGDTWNRLDFF
CCCCCCCCCHHCCEE		23.8829052541
173N-linked_GlycosylationSLDLQNINLSAIRTV
ECCCCCCCHHHHHHH		35.18UniProtKB CARBOHYD
175PhosphorylationDLQNINLSAIRTVRV
CCCCCCHHHHHHHHH		19.7018785766
244N-linked_GlycosylationNRCFLEENFTIQGDV
CCCCCCCCEEEECCE		29.95UniProtKB CARBOHYD
311N-linked_GlycosylationGAGRQDLNASGLCVN
CCCCCCCCCCCCCCC		40.11UniProtKB CARBOHYD
373PhosphorylationVMDAHSFYNFIYFIL
HHHHHHHHHHHHHHH		16.5126074081
377PhosphorylationHSFYNFIYFILLIIV
HHHHHHHHHHHHHHH		4.7626074081
728PhosphorylationGQADGGLSVLRTFRL
CCCCCCHHHHHHHHH		23.5224719451
758PhosphorylationQLVVLMKTMDNVATF
HHHHHHHHCHHHHHH		18.7830576142
789PhosphorylationHIFGCKFSLRTDTGD
HHHCCCEEECCCCCC		11.4825394399
881PhosphorylationSYSDEDQSSSNIEEF
CCCCCCCCCCCHHHH		48.32-
882PhosphorylationYSDEDQSSSNIEEFD
CCCCCCCCCCHHHHH		23.05-
883PhosphorylationSDEDQSSSNIEEFDK
CCCCCCCCCHHHHHH		47.26-
953PhosphorylationALGSRKSSVMSLGRM
ECCCCCHHHHHHCCC		25.5221712546
956PhosphorylationSRKSSVMSLGRMSYD
CCCHHHHHHCCCCCC		26.0521712546
993PhosphorylationSRRSSWNSLKHKPPS
HHHHHHHHCCCCCCC		32.3224719451
1008PhosphorylationAEHESLLSAERGGGA
HHHHHHHHHHCCCCC		33.1224719451
1058PhosphorylationRHHRRTLSLDNRDSV
HHHCCCCCCCCCCCC		32.82-
1298PhosphorylationGLKLVVETLISSLKP
CHHHHHHHHHHHCCC		20.1329978859
1301PhosphorylationLVVETLISSLKPIGN
HHHHHHHHHCCCHHH		32.5024719451
1302PhosphorylationVVETLISSLKPIGNI
HHHHHHHHCCCHHHH		33.1629978859
1342N-linked_GlycosylationCLGVDTRNITNRSDC
HHCCCCCCCCCHHHH		47.75UniProtKB CARBOHYD
1345N-linked_GlycosylationVDTRNITNRSDCMAA
CCCCCCCCHHHHHHH		37.35UniProtKB CARBOHYD
1354PhosphorylationSDCMAANYRWVHHKY
HHHHHHCCCEEECCC		10.9222210691
1372PhosphorylationNLGQALMSLFVLASK
CHHHHHHHHHHHHCC		21.3622210691
1378PhosphorylationMSLFVLASKDGWVNI
HHHHHHHCCCCCEEE		27.4122210691
1873PhosphorylationILLGDDLSLEDPTAC
EEECCCCCCCCCCCC		36.39-
1999PhosphorylationGSWASLRSPRVNCTL
CCHHHHCCCCCCEEE		23.5017081983
2015PhosphorylationRQATGSDTSLDASPS
EEHHCCCCCCCCCCC		32.6519690332
2022PhosphorylationTSLDASPSSSAGSLQ
CCCCCCCCCCCCCCE		34.1419690332
2023PhosphorylationSLDASPSSSAGSLQT
CCCCCCCCCCCCCEE		27.8219690332
2031PhosphorylationSAGSLQTTLEDSLTL
CCCCCEEEHHHCCCC		18.39-
2039PhosphorylationLEDSLTLSDSPRRAL
HHHCCCCCCCCHHHC		30.70-
2041PhosphorylationDSLTLSDSPRRALGP
HCCCCCCCCHHHCCC		19.55-
2068PhosphorylationPAARRRLSLRGRGLF
HHHHHHHHHCCCCCC		17.7623532336
2088PhosphorylationRAHQRSHSSGGSTSP
HHHHCCCCCCCCCCC		31.74-
2219PhosphorylationLEPGDAASKRKR---
CCCCCHHHHCCC---		34.4124260401
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 CAC1I_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1I_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 CAC1I_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAC1I_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00304 Divalproex sodium (USP); Valproate semisodium (INN); Depakote (TN)
D00399 Valproic acid (USP); Depakene (TN)
D00538 Zonisamide (JAN/USAN/INN); Excegran (TN)
D00539 Ethosuximide (JP16/USP/INN); Zarontin (TN)
D00553 Propitocaine (JAN); Prilocaine (USP/INN)
D00631 Bepridil hydrochloride hydrate (JAN); Bepridil hydrochloride (USAN); Vascor (TN)
D00710 Sodium valproate (JP16); Valproate sodium (USAN); Depakene (TN); Selenica (TN)
D01303 Flunarizine hydrochloride (JAN/USAN)
D01562 Aranidipine (JAN/INN); Sapresta (TN)
D01604 Efonidipine hydrochloride ethanolate (JAN); Efonidipine hydrochloride ethanol; Efonidipine hydrochlo
D02630 Penfluridol (USAN/INN); Semap (TN)
D05024 Mibefradil dihydrochloride (USAN); Posicor (TN)
D07520 Bepridil (INN); Bepadin (TN)
D07886 Efonidipine (INN)
D07971 Flunarizine (INN); Sibelium (TN)
D08217 Mibefradil (INN)
D08667 Calcium valproate; Valproic acid calcium salt; Convulsofin (TN)
DrugBank
DB00568Cinnarizine
DB04841Flunarizine
DB00617Paramethadione
DB00421Spironolactone
DB00661Verapamil
DB00909Zonisamide
Regulatory Network of CAC1I_HUMAN

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Related Literatures of Post-Translational Modification

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