CAC1G_HUMAN - dbPTM
CAC1G_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1G_HUMAN
UniProt AC O43497
Protein Name Voltage-dependent T-type calcium channel subunit alpha-1G
Gene Name CACNA1G
Organism Homo sapiens (Human).
Sequence Length 2377
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cytoplasm .
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-1G gives rise to T-type calcium currents. T-type calcium channels belong to the "low-voltage activated (LVA)" group and are strongly blocked by mibefradil. A particularity of this type of channel 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..
Protein Sequence MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAAGVRVGLLSSPAPLGGQETQPSSSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRAPRASPEIQDRDANGSRRLMLPPPSTPALSGAPPGGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPETLKEKALVEVAASSGPPTLTSLNIPPGPYSSMHKLLETQSTGACQSSCKISSPCLKADSGACGPDSCPYCARAGAGEVELADREMPDSDSEAVYEFTQDAQHSDLRDPHSRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEISKREDASGQLSCIQLPVDSQGGDANKSESEPDFFSPSLDGDGDRKKCLALVSLGEHPELRKSLLPPLIIHTAATPMSLPKSTSTGLGEALGPASRRTSSSGSAEPGAAHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEERASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRGSASEHQDCNGKSASGRLARALRPDDPPLDGDDADDEGNLSKGERVRAWIRARLPACCLERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGPDSPDSPKPGALHPAAHARSASHFSLEHPTDRQLFDTISLLIQGSLEWELKLMDELAGPGGQPSAFPSAPSLGGSDPQIPLAEMEALSLTSEIVSEPSCSLALTDDSLPDDMHTLLLSALESNMQPHPTELPGPDLLTVRKSGVSRTHSLPNDSYMCRHGSTAEGPLGHRGWGLPKAQSGSVLSVHSQPADTSYILQLPKDAPHLLQPHSAPTWGTIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLAEVSGPSPPLARAYSFWGQSSTQAQQHSRSHSKISKHMTPPAPCPGPEPNWGKGPPETRSSLELDTELSWISGDLLPPGGQEEPPSPRDLKKCYSVEAQSCQRRPTSWLDEQRRHSIAVSCLDSGSQPHLGTDPSNLGGQPLGGPGSRPKKKLSPPSITIDPPESQGPRTPPSPGICLRRRAPSSDSKDPLASGPPDSMAASPSPKKDVLSLSGLSSDPADLDP
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
17MethylationAEESGQPRSFMRLND
CCCCCCCCCEEEHHH
34.34-
26PhosphorylationFMRLNDLSGAGGRPG
EEEHHHCCCCCCCCC
29.4724719451
36PhosphorylationGGRPGPGSAEKDPGS
CCCCCCCCCCCCCCC
36.0724719451
151PhosphorylationKKCYLGDTWNRLDFF
CCCCCCCCCHHHHHH
23.8829052541
173N-linked_GlycosylationEYSLDLQNVSFSAVR
HHCCCCCCCCHHHHH
38.40UniProtKB CARBOHYD
196PhosphorylationRAINRVPSMRILVTL
HHHCCCCCHHHHHHH
20.1722617229
246N-linked_GlycosylationNRCFLPENFSLPLSV
CCCCCCCCCCCCEEE
29.84UniProtKB CARBOHYD
258PhosphorylationLSVDLERYYQTENED
EEEEHHHHHCCCCCC
7.19-
259PhosphorylationSVDLERYYQTENEDE
EEEHHHHHCCCCCCC
18.38-
306N-linked_GlycosylationGLDYEAYNSSSNTTC
CCCCCEECCCCCCEE
42.33UniProtKB CARBOHYD
310N-linked_GlycosylationEAYNSSSNTTCVNWN
CEECCCCCCEEECHH
41.16UniProtKB CARBOHYD
322N-linked_GlycosylationNWNQYYTNCSAGEHN
CHHHHCCCCCCCCCC
11.13UniProtKB CARBOHYD
370PhosphorylationVMDAHSFYNFIYFIL
HHHHHHHHHHHHHHH
16.5126074081
374PhosphorylationHSFYNFIYFILLIIV
HHHHHHHHHHHHHHH
4.7626074081
467PhosphorylationVRVGLLSSPAPLGGQ
CCEEEECCCCCCCCC
25.67-
586PhosphorylationASGRTVGSGKVYPTV
CCCCEECCCCEECCE
30.9828985074
595PhosphorylationKVYPTVHTSPPPETL
CEECCEECCCCCCHH
38.3028985074
620PhosphorylationSSGPPTLTSLNIPPG
CCCCCCEEECCCCCC
33.3822210691
621PhosphorylationSGPPTLTSLNIPPGP
CCCCCEEECCCCCCC
23.6422210691
638PhosphorylationSMHKLLETQSTGACQ
HHHHHHHCCCCCCCC
27.9929978859
640PhosphorylationHKLLETQSTGACQSS
HHHHHCCCCCCCCCC
35.9129978859
641PhosphorylationKLLETQSTGACQSSC
HHHHCCCCCCCCCCC
20.9829978859
646PhosphorylationQSTGACQSSCKISSP
CCCCCCCCCCCCCCC
37.2729978859
647PhosphorylationSTGACQSSCKISSPC
CCCCCCCCCCCCCCC
8.1129978859
651PhosphorylationCQSSCKISSPCLKAD
CCCCCCCCCCCEECC
17.4528985074
659PhosphorylationSPCLKADSGACGPDS
CCCEECCCCCCCCCC
32.9028985074
669PhosphorylationCGPDSCPYCARAGAG
CCCCCCCCHHCCCCC
11.7628985074
715PhosphorylationPHSRRQRSLGPDAEP
CCHHHHHHCCCCCCH
29.37-
735PhosphorylationFWRLICDTFRKIVDS
HHHHHHHHHHHHHCC
22.4120058876
831PhosphorylationGQQGGGLSVLRTFRL
CCCCCCHHHHHHHHH
23.5224719451
974UbiquitinationFQAEEISKREDASGQ
CCHHHHHCCCCCCCC
66.5232015554
1091PhosphorylationKSPPSARSSPHSPWS
CCCCCCCCCCCCCCH
48.19-
1139PhosphorylationLSGEGQESQDEEESS
HCCCCCCCCCHHHCC
34.74-
1145PhosphorylationESQDEEESSEEERAS
CCCCHHHCCHHHHHC
46.45-
1146PhosphorylationSQDEEESSEEERASP
CCCHHHCCHHHHHCC
52.92-
1152PhosphorylationSSEEERASPAGSDHR
CCHHHHHCCCCCCCC
22.85-
1163PhosphorylationSDHRHRGSLEREAKS
CCCCCCCHHHHHHHH
27.3217081983
1170PhosphorylationSLEREAKSSFDLPDT
HHHHHHHHCCCCCCC
43.2028348404
1171PhosphorylationLEREAKSSFDLPDTL
HHHHHHHCCCCCCCC
23.2924719451
1448N-linked_GlycosylationCQGEDTRNITNKSDC
EECCCCCCCCCHHHH
47.75UniProtKB CARBOHYD
1451N-linked_GlycosylationEDTRNITNKSDCAEA
CCCCCCCCHHHHHHH
37.73UniProtKB CARBOHYD
1541 (in isoform 23)Phosphorylation-39.63-
1542 (in isoform 23)Phosphorylation-27.29-
1552 (in isoform 27)Phosphorylation-17.35-
1552 (in isoform 3)Phosphorylation-17.35-
1553 (in isoform 3)Phosphorylation-41.28-
1553 (in isoform 27)Phosphorylation-41.28-
1575 (in isoform 15)Phosphorylation-3.83-
1575 (in isoform 30)Phosphorylation-3.83-
1575 (in isoform 16)Phosphorylation-3.83-
1575 (in isoform 13)Phosphorylation-3.83-
1576 (in isoform 30)Phosphorylation-3.04-
1576 (in isoform 16)Phosphorylation-3.04-
1576 (in isoform 13)Phosphorylation-3.04-
1576 (in isoform 15)Phosphorylation-3.04-
1593PhosphorylationSEAQCKPYYSDYSRF
HHHHCCCCCCCHHHH
10.90-
1594PhosphorylationEAQCKPYYSDYSRFR
HHHCCCCCCCHHHHH
12.00-
1598PhosphorylationKPYYSDYSRFRLLVH
CCCCCCHHHHHHHHH
29.90-
1698N-linked_GlycosylationTLEEIEVNASLPINP
CHHHEHHCCCCCCCH
15.83UniProtKB CARBOHYD
1870 (in isoform 22)Phosphorylation-33.14-
1875 (in isoform 23)Phosphorylation-6.67-
1882 (in isoform 26)Phosphorylation-33.05-
1886 (in isoform 3)Phosphorylation-13.71-
1889 (in isoform 36)Phosphorylation-26.93-
1891 (in isoform 35)Phosphorylation-6.48-
1893 (in isoform 2)Phosphorylation-38.81-
1893 (in isoform 24)Phosphorylation-38.81-
1893 (in isoform 5)Phosphorylation-38.81-
1900 (in isoform 34)Phosphorylation-33.47-
1902 (in isoform 15)Phosphorylation-79.93-
1904 (in isoform 9)Phosphorylation-55.00-
1909 (in isoform 13)Phosphorylation-6.52-
1916 (in isoform 19)Phosphorylation-23.92-
1916 (in isoform 6)Phosphorylation-23.92-
1917PhosphorylationHPAAHARSASHFSLE
CCCHHCCCCCCCCCC
34.60-
1919PhosphorylationAAHARSASHFSLEHP
CHHCCCCCCCCCCCC
26.72-
1920 (in isoform 17)Phosphorylation-18.94-
1922PhosphorylationARSASHFSLEHPTDR
CCCCCCCCCCCCCHH
27.68-
1927PhosphorylationHFSLEHPTDRQLFDT
CCCCCCCCHHHHHHH
45.80-
1927 (in isoform 11)Phosphorylation-45.80-
1927 (in isoform 18)Phosphorylation-45.80-
1934 (in isoform 21)Phosphorylation-12.72-
2046PhosphorylationSGVSRTHSLPNDSYM
CCCCCCCCCCCCCCC
44.9324719451
2076PhosphorylationWGLPKAQSGSVLSVH
CCCCCCCCCCEEEEE
37.5829978859
2078PhosphorylationLPKAQSGSVLSVHSQ
CCCCCCCCEEEEECC
25.7329978859
2081PhosphorylationAQSGSVLSVHSQPAD
CCCCCEEEEECCCCC
18.6729978859
2084PhosphorylationGSVLSVHSQPADTSY
CCEEEEECCCCCCEE
35.3929978859
2089PhosphorylationVHSQPADTSYILQLP
EECCCCCCEEEEECC
26.0729978859
2090PhosphorylationHSQPADTSYILQLPK
ECCCCCCEEEEECCC
15.6629978859
2091PhosphorylationSQPADTSYILQLPKD
CCCCCCEEEEECCCC
14.0329978859
2122MethylationPKLPPPGRSPLAQRP
CCCCCCCCCCHHCCC
40.66-
2128MethylationGRSPLAQRPLRRQAA
CCCCHHCCCHHHHHH
26.98-
2131MethylationPLAQRPLRRQAAIRT
CHHCCCHHHHHHHCC
31.20-
2132MethylationLAQRPLRRQAAIRTD
HHCCCHHHHHHHCCC
37.87-
2247PhosphorylationPRDLKKCYSVEAQSC
HHHHHHHEEECCHHC
25.32-
2357PhosphorylationDSMAASPSPKKDVLS
CCCCCCCCCCCCCCC
47.0215302935

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 CAC1G_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1G_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 CAC1G_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RANB9_HUMANRANBP9physical
18801335

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)
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
DB00593Ethosuximide
DB04841Flunarizine
DB05246Methsuximide
DB00421Spironolactone
DB00347Trimethadione
DB00661Verapamil
DB00909Zonisamide
Regulatory Network of CAC1G_HUMAN

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Related Literatures of Post-Translational Modification

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