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Protein Page:
CACNA1S (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CACNA1S 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-1S gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle. Defects in CACNA1S are the cause of periodic paralysis hypokalemic type 1 (HOKPP1); also designated HYPOPP. HOKPP1 is an autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels. Defects in CACNA1S are the cause of malignant hyperthermia susceptibility type 5 (MHS5); an autosomal dominant disorder that is potentially lethal in susceptible individuals on exposure to commonly used inhalational anesthetics and depolarizing muscle relaxants. Defects in CACNA1S are the cause of susceptibility to thyrotoxic periodic paralysis type 1 (TTPP1). A sporadic muscular disorder characterized by episodic weakness and hypokalemia during a thyrotoxic state. It is clinically similar to hereditary hypokalemic periodic paralysis, except for the fact that hyperthyroidism is an absolute requirement for disease manifestation. The disease presents with recurrent episodes of acute muscular weakness of the four extremities that vary in severity from paresis to complete paralysis. Attacks are triggered by ingestion of a high carbohydrate load or strenuous physical activity followed by a period of rest. Thyrotoxic periodic paralysis can occur in association with any cause of hyperthyroidism, but is most commonly associated with Graves disease. Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1S subfamily. Note: This description may include information from UniProtKB.
Protein type: Channel, calcium; Membrane protein, multi-pass; Membrane protein, integral
Chromosomal Location of Human Ortholog: 1q32
Cellular Component: cytoplasm; I band; plasma membrane; T-tubule; voltage-gated calcium channel complex
Molecular Function: high voltage-gated calcium channel activity; protein binding; voltage-gated calcium channel activity
Biological Process: calcium ion transport; muscle contraction
Disease: Hypokalemic Periodic Paralysis, Type 1; Malignant Hyperthermia, Susceptibility To, 5; Thyrotoxic Periodic Paralysis, Susceptibility To, 1
Reference #:  Q13698 (UniProtKB)
Alt. Names/Synonyms: CAC1S; CACH1; CACN1; CACNA1S; CACNL1A3; calcium channel, L type, alpha 1 polypeptide, isoform 3 (skeletal muscle, hypokalemic periodic paralysis); Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle; calcium channel, voltage-dependent, L type, alpha 1S subunit; Cav1.1; CCHL1A3; dihydropyridine receptor; dihydropyridine-sensitive L-type calcium channel alpha-1 subunit; HOKPP; hypoPP; MHS5; TTPP1; Voltage-dependent L-type calcium channel subunit alpha-1S; Voltage-gated calcium channel subunit alpha Cav1.1
Gene Symbols: CACNA1S
Molecular weight: 212,350 Da
Basal Isoelectric point: 6.17  Predict pI for various phosphorylation states
Select Structure to View Below

CACNA1S

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T225‑p FKGKMHKtCYFIGtD
0 1 T231‑p KtCYFIGtDIVAtVE
0 1 T236‑p IGtDIVAtVENEEPS
0 5 K343‑ac EFTKEREkAkSRGTF
0 1 K345‑ac TKEREkAkSRGTFQk
0 1 K352‑ac kSRGTFQkLREKQQL
0 1 S387‑p DFREGKLsLDEGGsD
0 2 S393‑p LsLDEGGsDTEsLyE
0 1 T395 LDEGGsDTEsLyEIA
0 2 S397‑p EGGsDTEsLyEIAGL
0 1 Y399‑p GsDTEsLyEIAGLNK
2 0 S687 EKKRRKMSKGLPDKS
0 2 K719 EGIPTTAKLKIDEFE
0 1 K719 EGIPTTAKLKIDEFE
0 1 K769 AELQLKEKAVPIPEA
0 1 T799‑p CHRIVNAtWFtNFIL
0 1 T802‑p IVNAtWFtNFILLFI
0 1 Y971‑p TEEECRGyyyVyKDG
0 2 Y972‑p EEECRGyyyVyKDGD
0 2 Y973‑p EECRGyyyVyKDGDP
0 1 Y975‑p CRGyyyVyKDGDPMQ
0 1 Y1035‑p AEDVGPIyNNRVEMA
0 1 Y1524‑p EVTVGKFyATFLIQE
0 1 K1550 YYGYRPKKDIVQIQA
0 1 T1573‑p AAPEICRtVsGDLAA
1 4 S1575‑p PEICRtVsGDLAAEE
1 3 A1579 RtVsGDLAAEEELER
1 1 S1617 NFLERTNSLPPVMAN
0 1 L1711 LGQPCRVLGPHSkPC
0 1 K1716‑ac RVLGPHSkPCVEMLk
0 1 M1721 HSkPCVEMLkGLLTQ
0 1 K1723‑ac kPCVEMLkGLLTQRA
0 1 T1810 DANFIMATGQALADA
  mouse

 
T225 FKGKMHKTCYFIGTD
T231 KTCYFIGTDIVATVE
T236 IGTDIVATVENEKPS
K343‑ac EFTKEREkAKSRGTF
K345 TKEREkAKSRGTFQK
K352 KSRGTFQKLREKQQL
S387 DLREGKLSLDEGGsD
S393‑p LSLDEGGsDtEsLYE
T395‑p LDEGGsDtEsLYEIE
S397‑p EGGsDtEsLYEIEGL
Y399 GsDtEsLYEIEGLNK
S687 ERKRRKMSKGLPDKS
K719‑ac EGIPTTAkLKIDEFE
K719‑ub EGIPTTAkLKIDEFE
K769‑ub AELQLKEkAVPIPEA
T799 CHRIVNATWFTNFIL
T802 IVNATWFTNFILLFI
Y971 TEEECRGYyyIYKDG
Y972‑p EEECRGYyyIYKDGD
Y973‑p EECRGYyyIYKDGDP
Y975 CRGYyyIYKDGDPTQ
Y1035 EEDTGPVYNNRVEMA
Y1524 EVTVGKFYATFLIQE
K1550‑ub YYGYRPKkDTVQIQA
A1573 AAPEIHRAIsGDPtA
S1575‑p PEIHRAIsGDPtAEE
T1579‑p RAIsGDPtAEEELER
S1617 NFLERTNSLPPVMAN
S1711‑p LSQPCSGsGPHSRSH
R1716 SGsGPHSRSHVDkLK
K1721‑ac HSRSHVDkLKRPMTQ
K1723 RSHVDkLKRPMTQRG
T1813‑p DANFVMAtGQALADA
  rat

 
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K6‑ac __VPTTAkLKIDEFE
K6 __VPTTAKLKIDEFE
K56 AELQLKEKAVPIPEA
T86 CHRIVNATWFTNFIL
T89 IVNATWFTNFILLFI
Y258 TEEECRGYYYIYKDG
Y259 EEECRGYYYIYKDGD
Y260 EECRGYYYIYKDGDP
Y262 CRGYYYIYKDGDPTQ
Y322 EEDTGPVYNNRVEMA
Y811 EVTVGKFYATFLIQE
K837 YYGYRPKKDTVQIQA
A860 AAPEIHRAIsGDLtA
S862‑p PEIHRAIsGDLtAEE
T866‑p RAIsGDLtAEEELER
S904‑p NFLERTNsLPPVMAN
S998 FSQPCSVSGVNSRSH
R1003 SVSGVNSRSHVDKLE
K1008 NSRSHVDKLERQMSQ
E1010 RSHVDKLERQMSQRR
T1100 DANFVMATGQALADA
  rabbit

 
T225 FKGKMHKTCYYIGTD
T231 KTCYYIGTDIVATVE
T236 IGTDIVATVENEKPS
K343 EFTKEREKAKSRGTF
K345 TKEREKAKSRGTFQK
K352 KSRGTFQKLREKQQL
S387 DLREGKLSLEEGGSD
S393 LSLEEGGSDTESLYE
T395 LEEGGSDTESLYEIE
S397 EGGSDTESLYEIEGL
Y399 GSDTESLYEIEGLNK
S687‑p ERKRRKMsRGLPDKT
K719 EGIPTTAKLKVDEFE
K719 EGIPTTAKLKVDEFE
K769 AELQLKEKAVPIPEA
T799 CHRIVNATWFTNFIL
T802 IVNATWFTNFILLFI
Y971 TEEECRGYYYVYKDG
Y972 EEECRGYYYVYKDGD
Y973 EECRGYYYVYKDGDP
Y975 CRGYYYVYKDGDPTQ
Y1035 EEDMGPVYNNRVEMA
Y1524 EVTVGKFYATFLIQE
K1550 YYGYRPKKDTVQIQA
T1573 AAPEIRRTIsGDLtA
S1575‑p PEIRRTIsGDLtAEE
T1579‑p RTIsGDLtAEEELER
S1617‑p TFLERTNsLPPVMAN
L1711 LSHSHRALGPHSKPC
K1716 RALGPHSKPCAGKLN
K1721 HSKPCAGKLNGQLVQ
N1723 KPCAGKLNGQLVQPG
T1810 DAGFVTATSQALADA
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