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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
17 | Methylation | AEESGQPRSFMRLND CCCCCCCCCEEEHHH | 34.34 | - | |
26 | Phosphorylation | FMRLNDLSGAGGRPG EEEHHHCCCCCCCCC | 29.47 | 24719451 | |
36 | Phosphorylation | GGRPGPGSAEKDPGS CCCCCCCCCCCCCCC | 36.07 | 24719451 | |
151 | Phosphorylation | KKCYLGDTWNRLDFF CCCCCCCCCHHHHHH | 23.88 | 29052541 | |
173 | N-linked_Glycosylation | EYSLDLQNVSFSAVR HHCCCCCCCCHHHHH | 38.40 | UniProtKB CARBOHYD | |
196 | Phosphorylation | RAINRVPSMRILVTL HHHCCCCCHHHHHHH | 20.17 | 22617229 | |
246 | N-linked_Glycosylation | NRCFLPENFSLPLSV CCCCCCCCCCCCEEE | 29.84 | UniProtKB CARBOHYD | |
258 | Phosphorylation | LSVDLERYYQTENED EEEEHHHHHCCCCCC | 7.19 | - | |
259 | Phosphorylation | SVDLERYYQTENEDE EEEHHHHHCCCCCCC | 18.38 | - | |
306 | N-linked_Glycosylation | GLDYEAYNSSSNTTC CCCCCEECCCCCCEE | 42.33 | UniProtKB CARBOHYD | |
310 | N-linked_Glycosylation | EAYNSSSNTTCVNWN CEECCCCCCEEECHH | 41.16 | UniProtKB CARBOHYD | |
322 | N-linked_Glycosylation | NWNQYYTNCSAGEHN CHHHHCCCCCCCCCC | 11.13 | UniProtKB CARBOHYD | |
370 | Phosphorylation | VMDAHSFYNFIYFIL HHHHHHHHHHHHHHH | 16.51 | 26074081 | |
374 | Phosphorylation | HSFYNFIYFILLIIV HHHHHHHHHHHHHHH | 4.76 | 26074081 | |
467 | Phosphorylation | VRVGLLSSPAPLGGQ CCEEEECCCCCCCCC | 25.67 | - | |
586 | Phosphorylation | ASGRTVGSGKVYPTV CCCCEECCCCEECCE | 30.98 | 28985074 | |
595 | Phosphorylation | KVYPTVHTSPPPETL CEECCEECCCCCCHH | 38.30 | 28985074 | |
620 | Phosphorylation | SSGPPTLTSLNIPPG CCCCCCEEECCCCCC | 33.38 | 22210691 | |
621 | Phosphorylation | SGPPTLTSLNIPPGP CCCCCEEECCCCCCC | 23.64 | 22210691 | |
638 | Phosphorylation | SMHKLLETQSTGACQ HHHHHHHCCCCCCCC | 27.99 | 29978859 | |
640 | Phosphorylation | HKLLETQSTGACQSS HHHHHCCCCCCCCCC | 35.91 | 29978859 | |
641 | Phosphorylation | KLLETQSTGACQSSC HHHHCCCCCCCCCCC | 20.98 | 29978859 | |
646 | Phosphorylation | QSTGACQSSCKISSP CCCCCCCCCCCCCCC | 37.27 | 29978859 | |
647 | Phosphorylation | STGACQSSCKISSPC CCCCCCCCCCCCCCC | 8.11 | 29978859 | |
651 | Phosphorylation | CQSSCKISSPCLKAD CCCCCCCCCCCEECC | 17.45 | 28985074 | |
659 | Phosphorylation | SPCLKADSGACGPDS CCCEECCCCCCCCCC | 32.90 | 28985074 | |
669 | Phosphorylation | CGPDSCPYCARAGAG CCCCCCCCHHCCCCC | 11.76 | 28985074 | |
715 | Phosphorylation | PHSRRQRSLGPDAEP CCHHHHHHCCCCCCH | 29.37 | - | |
735 | Phosphorylation | FWRLICDTFRKIVDS HHHHHHHHHHHHHCC | 22.41 | 20058876 | |
831 | Phosphorylation | GQQGGGLSVLRTFRL CCCCCCHHHHHHHHH | 23.52 | 24719451 | |
974 | Ubiquitination | FQAEEISKREDASGQ CCHHHHHCCCCCCCC | 66.52 | 32015554 | |
1091 | Phosphorylation | KSPPSARSSPHSPWS CCCCCCCCCCCCCCH | 48.19 | - | |
1139 | Phosphorylation | LSGEGQESQDEEESS HCCCCCCCCCHHHCC | 34.74 | - | |
1145 | Phosphorylation | ESQDEEESSEEERAS CCCCHHHCCHHHHHC | 46.45 | - | |
1146 | Phosphorylation | SQDEEESSEEERASP CCCHHHCCHHHHHCC | 52.92 | - | |
1152 | Phosphorylation | SSEEERASPAGSDHR CCHHHHHCCCCCCCC | 22.85 | - | |
1163 | Phosphorylation | SDHRHRGSLEREAKS CCCCCCCHHHHHHHH | 27.32 | 17081983 | |
1170 | Phosphorylation | SLEREAKSSFDLPDT HHHHHHHHCCCCCCC | 43.20 | 28348404 | |
1171 | Phosphorylation | LEREAKSSFDLPDTL HHHHHHHCCCCCCCC | 23.29 | 24719451 | |
1448 | N-linked_Glycosylation | CQGEDTRNITNKSDC EECCCCCCCCCHHHH | 47.75 | UniProtKB CARBOHYD | |
1451 | N-linked_Glycosylation | EDTRNITNKSDCAEA CCCCCCCCHHHHHHH | 37.73 | UniProtKB 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 | - | |
1593 | Phosphorylation | SEAQCKPYYSDYSRF HHHHCCCCCCCHHHH | 10.90 | - | |
1594 | Phosphorylation | EAQCKPYYSDYSRFR HHHCCCCCCCHHHHH | 12.00 | - | |
1598 | Phosphorylation | KPYYSDYSRFRLLVH CCCCCCHHHHHHHHH | 29.90 | - | |
1698 | N-linked_Glycosylation | TLEEIEVNASLPINP CHHHEHHCCCCCCCH | 15.83 | UniProtKB 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 | - | |
1917 | Phosphorylation | HPAAHARSASHFSLE CCCHHCCCCCCCCCC | 34.60 | - | |
1919 | Phosphorylation | AAHARSASHFSLEHP CHHCCCCCCCCCCCC | 26.72 | - | |
1920 (in isoform 17) | Phosphorylation | - | 18.94 | - | |
1922 | Phosphorylation | ARSASHFSLEHPTDR CCCCCCCCCCCCCHH | 27.68 | - | |
1927 | Phosphorylation | HFSLEHPTDRQLFDT CCCCCCCCHHHHHHH | 45.80 | - | |
1927 (in isoform 11) | Phosphorylation | - | 45.80 | - | |
1927 (in isoform 18) | Phosphorylation | - | 45.80 | - | |
1934 (in isoform 21) | Phosphorylation | - | 12.72 | - | |
2046 | Phosphorylation | SGVSRTHSLPNDSYM CCCCCCCCCCCCCCC | 44.93 | 24719451 | |
2076 | Phosphorylation | WGLPKAQSGSVLSVH CCCCCCCCCCEEEEE | 37.58 | 29978859 | |
2078 | Phosphorylation | LPKAQSGSVLSVHSQ CCCCCCCCEEEEECC | 25.73 | 29978859 | |
2081 | Phosphorylation | AQSGSVLSVHSQPAD CCCCCEEEEECCCCC | 18.67 | 29978859 | |
2084 | Phosphorylation | GSVLSVHSQPADTSY CCEEEEECCCCCCEE | 35.39 | 29978859 | |
2089 | Phosphorylation | VHSQPADTSYILQLP EECCCCCCEEEEECC | 26.07 | 29978859 | |
2090 | Phosphorylation | HSQPADTSYILQLPK ECCCCCCEEEEECCC | 15.66 | 29978859 | |
2091 | Phosphorylation | SQPADTSYILQLPKD CCCCCCEEEEECCCC | 14.03 | 29978859 | |
2122 | Methylation | PKLPPPGRSPLAQRP CCCCCCCCCCHHCCC | 40.66 | - | |
2128 | Methylation | GRSPLAQRPLRRQAA CCCCHHCCCHHHHHH | 26.98 | - | |
2131 | Methylation | PLAQRPLRRQAAIRT CHHCCCHHHHHHHCC | 31.20 | - | |
2132 | Methylation | LAQRPLRRQAAIRTD HHCCCHHHHHHHCCC | 37.87 | - | |
2247 | Phosphorylation | PRDLKKCYSVEAQSC HHHHHHHEEECCHHC | 25.32 | - | |
2357 | Phosphorylation | DSMAASPSPKKDVLS CCCCCCCCCCCCCCC | 47.02 | 15302935 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAC1G_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RANB9_HUMAN | RANBP9 | physical | 18801335 |
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 | |
DB00568 | Cinnarizine |
DB00593 | Ethosuximide |
DB04841 | Flunarizine |
DB05246 | Methsuximide |
DB00421 | Spironolactone |
DB00347 | Trimethadione |
DB00661 | Verapamil |
DB00909 | Zonisamide |
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