CAC1H_HUMAN - dbPTM
CAC1H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1H_HUMAN
UniProt AC O95180
Protein Name Voltage-dependent T-type calcium channel subunit alpha-1H
Gene Name CACNA1H
Organism Homo sapiens (Human).
Sequence Length 2353
Subcellular Localization Cell membrane
Multi-pass membrane protein . Interaction with STAC increases expression at the cell membrane.
Protein Description Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation. [PubMed: 9670923]
Protein Sequence MTEGARAADEVRVPLGAPPPGPAALVGASPESPGAPGREAERGSELGVSPSESPAAERGAELGADEEQRVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHVSMLVIMLNCVTLGMFRPCEDVECGSERCNILEAFDAFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVVAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPGRRELRMPCTLGWEAYTQPQAEGVGAARNACINWNQYYNVCRSGDSNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRARHLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSAVQGQGPGHRQRRAGRHTASVHHLVYHHHHHHHHHYHFSHGSPRRPGPEPGACDTRLVRAGAPPSPPSPGRGPPDAESVHSIYHADCHIEGPQERARVAHAAATAAASLRLATGLGTMNYPTILPSGVGSGKGSTSPGPKGKWAGGPPGTGGHGPLSLNSPDPYEKIPHVVGEHGLGQAPGHLSGLSVPCPLPSPPAGTLTCELKSCPYCTRALEDPEGELSGSESGDSDGRGVYEFTQDVRHGDRWDPTRPPRATDTPGPGPGSPQRRAQQRAAPGEPGWMGRLWVTFSGKLRRIVDSKYFSRGIMMAILVNTLSMGVEYHEQPEELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIIVVISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLVKTMDNVATFCTLLMLFIFIFSILGMHLFGCKFSLKTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSDTDEDKTSVHFEEDFHKLRELQTTELKMCSLAVTPNGHLEGRGSLSPPLIMCTAATPMPTPKSSPFLDAAPSLPDSRRGSSSSGDPPLGDQKPPASLRSSPCAPWGPSGAWSSRRSSWSSLGRAPSLKRRGQCGERESLLSGEGKGSTDDEAEDGRAAPGPRATPLRRAESLDPRPLRPAALPPTKCRDRDGQVVALPSDFFLRIDSHREDAAELDDDSEDSCCLRLHKVLEPYKPQWCRSREAWALYLFSPQNRFRVSCQKVITHKMFDHVVLVFIFLNCVTIALERPDIDPGSTERVFLSVSNYIFTAIFVAEMMVKVVALGLLSGEHAYLQSSWNLLDGLLVLVSLVDIVVAMASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGPDTRNISTKAQCRAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGVDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPSPEAQRRPYYADYSPTRRSIHSLCTSHYLDLFITFIICVNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSLMGITLEEIEMSAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFSNFGMAFLTLFRVSTGDNWNGIMKDTLRECSREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAELDAEIELEMAQGPGSARRVDADRPPLPQESPGARDAPNLVARKVSVSRMLSLPNDSYMFRPVVPASAPHPRPLQEVEMETYGAGTPLGSVASVHSPPAESCASLQIPLAVSSPARSGEPLHALSPRGTARSPSLSRLLCRQEAVHTDSLEGKIDSPRDTLDPAEPGEKTPVRPVTQGGSLQSPPRSPRPASVRTRKHTFGQRCVSSRPAAPGGEEAEASDPADEEVSHITSSACPWQPTAEPHGPEASPVAGGERDLRRLYSVDAQGFLDKPGRADEQWRPSAELGSGEPGEAKAWGPEAEPALGARRKKKMSPPCISVEPPAEDEGSARPSAAEGGSTTLRRRTPSCEATPHRDSLEPTEGSGAGGDPAAKGERWGQASCRAEHLTVPSFAFEPLDLGVPSGDPFLDGSHSVTPESRASSSGAIVPLEPPESEPPMPVGDPPEKRRGLYLTVPQCPLEKPGSPSATPAPGGGADDPV
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
49PhosphorylationRGSELGVSPSESPAA
CCCCCCCCCCCCHHH		22.4027732954
51PhosphorylationSELGVSPSESPAAER
CCCCCCCCCCHHHHH		43.1127732954
53PhosphorylationLGVSPSESPAAERGA
CCCCCCCCHHHHHCC		24.9527732954
170PhosphorylationQKCYLGDTWNRLDFF
CCCCCCCCCCCCCEE		23.8829052541
192N-linked_GlycosylationEYSLDGHNVSLSAIR
EECCCCCCCCHHHHH		30.51UniProtKB CARBOHYD
215PhosphorylationRAINRVPSMRILVTL
HHHCCCCCHHHHHHH		20.1722617229
271N-linked_GlycosylationSAFVRNNNLTFLRPY
HHHHCCCCEEEEEEE		43.96UniProtKB CARBOHYD
343PhosphorylationACINWNQYYNVCRSG
HCCCHHHHHCCCCCC		8.1929759185
344PhosphorylationCINWNQYYNVCRSGD
CCCHHHHHCCCCCCC		7.4329759185
394PhosphorylationVMDAHSFYNFIYFIL
HHHHHHHHHHHHHHH		16.5126074081
398PhosphorylationHSFYNFIYFILLIIV
HHHHHHHHHHHHHHH		4.7626074081
446PhosphorylationRHLSNDSTLASFSEP
HHCCCCCCCHHHCCC		29.25-
475PhosphorylationFRKVKRRSLRLYARW
HHHHHHHHHHHHHHH		23.1329449344
479PhosphorylationKRRSLRLYARWQSRW
HHHHHHHHHHHHHHH		6.4129449344
484PhosphorylationRLYARWQSRWRKKVD
HHHHHHHHHHHHCCC		27.1829449344
558PhosphorylationVRAGAPPSPPSPGRG
EECCCCCCCCCCCCC		48.6723312004
561PhosphorylationGAPPSPPSPGRGPPD
CCCCCCCCCCCCCCC		43.2923312004
615PhosphorylationLGTMNYPTILPSGVG
CCCCCCCCCCCCCCC		25.45-
619PhosphorylationNYPTILPSGVGSGKG
CCCCCCCCCCCCCCC		42.54-
623PhosphorylationILPSGVGSGKGSTSP
CCCCCCCCCCCCCCC		34.62-
749PhosphorylationPTRPPRATDTPGPGP
CCCCCCCCCCCCCCC		41.5029691806
751PhosphorylationRPPRATDTPGPGPGS
CCCCCCCCCCCCCCC		26.2829691806
758PhosphorylationTPGPGPGSPQRRAQQ
CCCCCCCCHHHHHHH		22.4630266825
783PhosphorylationGRLWVTFSGKLRRIV
EEEEEEECCHHHHHH		26.1718187866
881PhosphorylationGQADGGLSVLRTFRL
CCCCCCHHHHHHHHH		23.5224719451
1044UbiquitinationHFEEDFHKLRELQTT
CHHHHHHHHHHHHCC		49.59-
1071PhosphorylationGHLEGRGSLSPPLIM
CCCCCCCCCCCCEEE		25.0627251275
1073PhosphorylationLEGRGSLSPPLIMCT
CCCCCCCCCCEEEEE		26.6028348404
1090PhosphorylationTPMPTPKSSPFLDAA
CCCCCCCCCCCHHCC		44.4329449344
1091PhosphorylationPMPTPKSSPFLDAAP
CCCCCCCCCCHHCCC		26.2929449344
1099PhosphorylationPFLDAAPSLPDSRRG
CCHHCCCCCCCCCCC		48.0527732954
1103PhosphorylationAAPSLPDSRRGSSSS
CCCCCCCCCCCCCCC		23.1827732954
1107PhosphorylationLPDSRRGSSSSGDPP
CCCCCCCCCCCCCCC		25.8219131331
1108PhosphorylationPDSRRGSSSSGDPPL
CCCCCCCCCCCCCCC		31.2028348404
1109PhosphorylationDSRRGSSSSGDPPLG
CCCCCCCCCCCCCCC		39.7828348404
1110PhosphorylationSRRGSSSSGDPPLGD
CCCCCCCCCCCCCCC		49.5228348404
1143PhosphorylationGAWSSRRSSWSSLGR
CCCCCCCCCCHHCCC		34.7428348404
1144PhosphorylationAWSSRRSSWSSLGRA
CCCCCCCCCHHCCCC		29.2128348404
1168PhosphorylationGERESLLSGEGKGST
CCCCCCCCCCCCCCC		39.8430278072
1174PhosphorylationLSGEGKGSTDDEAED
CCCCCCCCCCCCCCC		31.9530278072
1175PhosphorylationSGEGKGSTDDEAEDG
CCCCCCCCCCCCCCC		57.0230278072
1191PhosphorylationAAPGPRATPLRRAES
CCCCCCCCCCCCHHH		24.9217081983
1198PhosphorylationTPLRRAESLDPRPLR
CCCCCHHHCCCCCCC		36.7716917542
1275PhosphorylationSREAWALYLFSPQNR
CCCCHHHHHCCCCCC		9.6529083192
1278PhosphorylationAWALYLFSPQNRFRV
CHHHHHCCCCCCEEE		23.9929083192
1425PhosphorylationLVVETLISSLRPIGN
HHHHHHHHHCCCHHH		26.8224719451
1426PhosphorylationVVETLISSLRPIGNI
HHHHHHHHCCCHHHH		22.7725954137
1466N-linked_GlycosylationCEGPDTRNISTKAQC
EECCCCCCCCHHHHH		34.35UniProtKB CARBOHYD
1587PhosphorylationRLERRRRSTFPSPEA
HHHHHHHCCCCCHHH		32.3724719451
1805PhosphorylationFLTLFRVSTGDNWNG
HHHEEECCCCCCCCH		23.5526552605
1806PhosphorylationLTLFRVSTGDNWNGI
HHEEECCCCCCCCHH		45.7726552605
1817PhosphorylationWNGIMKDTLRECSRE
CCHHHHHHHHHHCCC		23.3826552605
1822PhosphorylationKDTLRECSREDKHCL
HHHHHHHCCCCHHHH		33.6726552605
1890PhosphorylationEMAQGPGSARRVDAD
EECCCCCCCCCCCCC		23.0329523821
1905PhosphorylationRPPLPQESPGARDAP
CCCCCCCCCCCCCCC		24.3228555341
1920PhosphorylationNLVARKVSVSRMLSL
CCCCCCCCHHHHHCC		19.8727282143
1926PhosphorylationVSVSRMLSLPNDSYM
CCHHHHHCCCCCCCC		32.2228348404
1991PhosphorylationAVSSPARSGEPLHAL
EECCCCCCCCCCCCC		50.00-
1999PhosphorylationGEPLHALSPRGTARS
CCCCCCCCCCCCCCC		17.2124719451
2057PhosphorylationTQGGSLQSPPRSPRP
CCCCCCCCCCCCCCC		42.0127732954
2073PhosphorylationSVRTRKHTFGQRCVS
CCCCCCCCCCCCCCC		32.28-
2136PhosphorylationERDLRRLYSVDAQGF
CCCHHHHHEECCCCC		12.5823312004
2137PhosphorylationRDLRRLYSVDAQGFL
CCHHHHHEECCCCCC		20.3628348404
2188PhosphorylationARRKKKMSPPCISVE
CCCCCCCCCCCEECC		34.27-
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
1107SPhosphorylationKinasePRKACAP17612
GPS
1198SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
1198SPhosphorylationKinaseCAMK2GQ13555
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1H_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 CAC1H_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLHL1_HUMANKLHL1physical
20147652
UBP5_HUMANUSP5physical
25889575
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611942Epilepsy, idiopathic generalized 6 (EIG6)
611942Epilepsy, childhood absence 6 (ECA6)
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)
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
DB01118Amiodarone
DB01244Bepridil
DB00568Cinnarizine
DB01023Felodipine
DB04841Flunarizine
DB00270Isradipine
DB01115Nifedipine
DB01054Nitrendipine
DB00421Spironolactone
DB00909Zonisamide
Regulatory Network of CAC1H_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASSSPECTROMETRY.
"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 THR-1191, AND MASSSPECTROMETRY.

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