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Protein

Voltage-dependent L-type calcium channel subunit alpha-1S

Gene

CACNA1S

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca2+ release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.By similarity

Enzyme regulationi

Channel activity is blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). It is however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi292CalciumBy similarity1
Metal bindingi614CalciumBy similarity1
Metal bindingi1014CalciumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi1410 – 1421By similarityAdd BLAST12

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB-KW
  • high voltage-gated calcium channel activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • cardiac conduction Source: Reactome
  • cellular response to caffeine Source: UniProtKB
  • membrane depolarization during action potential Source: GO_Central
  • muscle contraction Source: UniProtKB

Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-419037. NCAM1 interactions.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5576893. Phase 2 - plateau phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1S
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle
Voltage-gated calcium channel subunit alpha Cav1.1
Gene namesi
Name:CACNA1S
Synonyms:CACH1, CACN1, CACNL1A32 Publications
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000081248.10.
HGNCiHGNC:1397. CACNA1S.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 51CytoplasmicCuratedAdd BLAST51
Transmembranei52 – 70Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini71 – 85ExtracellularCuratedAdd BLAST15
Transmembranei86 – 106Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini107 – 115CytoplasmicCurated9
Transmembranei116 – 136Helical; Name=S3 of repeat IBy similarityAdd BLAST21
Topological domaini137 – 160ExtracellularCuratedAdd BLAST24
Transmembranei161 – 179Helical; Name=S4 of repeat IBy similarityAdd BLAST19
Topological domaini180 – 196CytoplasmicCuratedAdd BLAST17
Transmembranei197 – 218Helical; Name=S5 of repeat IBy similarityAdd BLAST22
Topological domaini219 – 279ExtracellularCuratedAdd BLAST61
Intramembranei280 – 301Pore-formingBy similarityAdd BLAST22
Topological domaini302 – 309ExtracellularCurated8
Transmembranei310 – 330Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini331 – 432CytoplasmicCuratedAdd BLAST102
Transmembranei433 – 451Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini452 – 462ExtracellularCuratedAdd BLAST11
Transmembranei463 – 483Helical; Name=S2 of repeat IIBy similarityAdd BLAST21
Topological domaini484 – 494CytoplasmicCuratedAdd BLAST11
Transmembranei495 – 514Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini515 – 523ExtracellularCurated9
Transmembranei524 – 542Helical; Name=S4 of repeat IIBy similarityAdd BLAST19
Topological domaini543 – 561CytoplasmicCuratedAdd BLAST19
Transmembranei562 – 581Helical; Name=S5 of repeat IIBy similarityAdd BLAST20
Topological domaini582 – 601ExtracellularCuratedAdd BLAST20
Intramembranei602 – 623Pore-formingBy similarityAdd BLAST22
Topological domaini624 – 633ExtracellularCurated10
Transmembranei634 – 653Helical; Name=S6 of repeat IIBy similarityAdd BLAST20
Topological domaini654 – 799CytoplasmicCuratedAdd BLAST146
Transmembranei800 – 818Helical; Name=S1 of repeat IIIBy similarityAdd BLAST19
Topological domaini819 – 830ExtracellularCuratedAdd BLAST12
Transmembranei831 – 850Helical; Name=S2 of repeat IIIBy similarityAdd BLAST20
Topological domaini851 – 866CytoplasmicCuratedAdd BLAST16
Transmembranei867 – 885Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini886 – 892ExtracellularCurated7
Transmembranei893 – 911Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini912 – 930CytoplasmicCuratedAdd BLAST19
Transmembranei931 – 950Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini951 – 1000ExtracellularCuratedAdd BLAST50
Intramembranei1001 – 1021Pore-formingBy similarityAdd BLAST21
Topological domaini1022 – 1038ExtracellularCuratedAdd BLAST17
Transmembranei1039 – 1060Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1061 – 1118CytoplasmicCuratedAdd BLAST58
Transmembranei1119 – 1140Helical; Name=S1 of repeat IVBy similarityAdd BLAST22
Topological domaini1141 – 1148ExtracellularCurated8
Transmembranei1149 – 1170Helical; Name=S2 of repeat IVBy similarityAdd BLAST22
Topological domaini1171 – 1180CytoplasmicCurated10
Transmembranei1181 – 1200Helical; Name=S3 of repeat IVBy similarityAdd BLAST20
Topological domaini1201 – 1231ExtracellularCuratedAdd BLAST31
Transmembranei1232 – 1250Helical; Name=S4 of repeat IVBy similarityAdd BLAST19
Topological domaini1251 – 1268CytoplasmicCuratedAdd BLAST18
Transmembranei1269 – 1289Helical; Name=S5 of repeat IVBy similarityAdd BLAST21
Topological domaini1290 – 1311ExtracellularCuratedAdd BLAST22
Intramembranei1312 – 1330Pore-formingBy similarityAdd BLAST19
Topological domaini1331 – 1356ExtracellularCuratedAdd BLAST26
Transmembranei1357 – 1381Helical; Name=S6 of repeat IVBy similarityAdd BLAST25
Topological domaini1382 – 1873CytoplasmicCuratedAdd BLAST492

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Periodic paralysis hypokalemic 1 (HOKPP1)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder manifested by episodic flaccid generalized muscle weakness associated with falls of serum potassium levels.
See also OMIM:170400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054953528R → G in HOKPP1. 1 PublicationCorresponds to variant dbSNP:rs80338778Ensembl.1
Natural variantiVAR_001499528R → H in HOKPP1. 3 PublicationsCorresponds to variant dbSNP:rs80338777Ensembl.1
Natural variantiVAR_054954900R → S in HOKPP1. 1 Publication1
Natural variantiVAR_0015011239R → G in HOKPP1. 3 PublicationsCorresponds to variant dbSNP:rs28930069Ensembl.1
Natural variantiVAR_0015021239R → H in HOKPP1. 4 PublicationsCorresponds to variant dbSNP:rs28930068Ensembl.1
Malignant hyperthermia 5 (MHS5)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disorder that is potentially lethal in susceptible individuals on exposure to commonly used inhalational anesthetics and depolarizing muscle relaxants.
See also OMIM:601887
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0015001086R → H in MHS5. 1 PublicationCorresponds to variant dbSNP:rs1800559Ensembl.1
Thyrotoxic periodic paralysis 1 (TTPP1)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:188580

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi779.
GeneReviewsiCACNA1S.
MalaCardsiCACNA1S.
MIMi170400. phenotype.
188580. phenotype.
601887. phenotype.
OpenTargetsiENSG00000081248.
Orphaneti681. Hypokalemic periodic paralysis.
423. Malignant hyperthermia.
397755. Periodic paralysis with transient compartment-like syndrome.
79102. Thyrotoxic periodic paralysis.
PharmGKBiPA85.

Chemistry databases

ChEMBLiCHEMBL3805.
DrugBankiDB00381. Amlodipine.
DB00568. Cinnarizine.
DB04920. Clevidipine.
DB04855. Dronedarone.
DB00898. Ethanol.
DB01023. Felodipine.
DB00270. Isradipine.
DB00653. Magnesium Sulfate.
DB01388. Mibefradil.
DB01115. Nifedipine.
DB06712. Nilvadipine.
DB00393. Nimodipine.
DB00401. Nisoldipine.
DB01054. Nitrendipine.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi528.

Polymorphism and mutation databases

BioMutaiCACNA1S.
DMDMi209572767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539431 – 1873Voltage-dependent L-type calcium channel subunit alpha-1SAdd BLAST1873

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi226 ↔ 254By similarity
Disulfide bondi245 ↔ 261By similarity
Glycosylationi257N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei393PhosphoserineBy similarity1
Modified residuei397PhosphoserineBy similarity1
Modified residuei687Phosphoserine; by PKABy similarity1
Disulfide bondi957 ↔ 968By similarity
Glycosylationi1141N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1338 ↔ 1352By similarity
Modified residuei1392Phosphoserine; by PKASequence analysis1
Modified residuei1575PhosphoserineBy similarity1
Modified residuei1617PhosphoserineBy similarity1

Post-translational modificationi

The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690.By similarity
Both the minor and major forms are phosphorylated in vitro by PKA. Phosphorylation by PKA activates the calcium channel.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ13698.
PeptideAtlasiQ13698.
PRIDEiQ13698.

PTM databases

iPTMnetiQ13698.
PhosphoSitePlusiQ13698.

Expressioni

Tissue specificityi

Skeletal muscle specific.

Gene expression databases

BgeeiENSG00000081248.
CleanExiHS_CACNA1S.
ExpressionAtlasiQ13698. baseline and differential.
GenevisibleiQ13698. HS.

Organism-specific databases

HPAiCAB009507.
HPA048892.
HPA056815.

Interactioni

Subunit structurei

Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2 (By similarity). CACNA1S channel activity is modulated by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1). Interacts with DYSF and JSRP1 (By similarity). Interacts with RYR1 (By similarity). Interacts with CALM (PubMed:19473981).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PDZD3Q86UT53EBI-5329490,EBI-8744528

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107233. 4 interactors.
IntActiQ13698. 6 interactors.
MINTiMINT-7899448.
STRINGi9606.ENSP00000355192.

Chemistry databases

BindingDBiQ13698.

Structurei

Secondary structure

11873
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1523 – 1536Combined sources14
Helixi1538 – 1541Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VAYX-ray1.94B1522-1542[»]
DisProtiDP01103.
ProteinModelPortaliQ13698.
SMRiQ13698.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13698.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati38 – 337ICuratedAdd BLAST300
Repeati418 – 664IICuratedAdd BLAST247
Repeati786 – 1068IIICuratedAdd BLAST283
Repeati1105 – 1384IVCuratedAdd BLAST280

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni357 – 374Binding to the beta subunitBy similarityAdd BLAST18
Regioni988 – 1077Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1337 – 1403Dihydropyridine bindingBy similarityAdd BLAST67
Regioni1349 – 1391Phenylalkylamine bindingBy similarityAdd BLAST43
Regioni1522 – 1542Interaction with calmodulin1 PublicationAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi290 – 293Selectivity filter of repeat IBy similarity4
Motifi612 – 615Selectivity filter of repeat IIBy similarity4
Motifi1012 – 1015Selectivity filter of repeat IIIBy similarity4
Motifi1321 – 1324Selectivity filter of repeat IVBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi562 – 568Poly-Leu7

Domaini

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.By similarity
The loop between repeats II and III interacts with the ryanodine receptor, and is therefore important for calcium release from the endoplasmic reticulum necessary for muscle contraction.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231529.
HOVERGENiHBG050763.
InParanoidiQ13698.
KOiK04857.
OMAiACSYGKL.
OrthoDBiEOG091G0TKO.
PhylomeDBiQ13698.
TreeFamiTF312805.

Family and domain databases

InterProiView protein in InterPro
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005450. VDCC_L_a1ssu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
PANTHERiPTHR10037:SF190. PTHR10037:SF190. 1 hit.
PfamiView protein in Pfam
PF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
PRINTSiPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01634. LVDCCALPHA1S.
SMARTiView protein in SMART
SM01062. Ca_chan_IQ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q13698-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLENPL RKACISIVEW
60 70 80 90 100
KPFETIILLT IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLIVFSIE
110 120 130 140 150
AAMKIIAYGF LFHQDAYLRS GWNVLDFTIV FLGVFTVILE QVNVIQSHTA
160 170 180 190 200
PMSSKGAGLD VKALRAFRVL RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA
210 220 230 240 250
LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE EPSPCARTGS
260 270 280 290 300
GRRCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
310 320 330 340 350
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF
360 370 380 390 400
QKLREKQQLD EDLRGYMSWI TQGEVMDVED FREGKLSLDE GGSDTESLYE
410 420 430 440 450
IAGLNKIIQF IRHWRQWNRI FRWKCHDIVK SKVFYWLVIL IVALNTLSIA
460 470 480 490 500
SEHHNQPLWL TRLQDIANRV LLSLFTTEML MKMYGLGLRQ YFMSIFNRFD
510 520 530 540 550
CFVVCSGILE ILLVESGAMT PLGISVLRCI RLLRIFKITK YWTSLSNLVA
560 570 580 590 600
SLLNSIRSIA SLLLLLFLFI VIFALLGMQL FGGRYDFEDT EVRRSNFDNF
610 620 630 640 650
PQALISVFQV LTGEDWTSMM YNGIMAYGGP SYPGMLVCIY FIILFVCGNY
660 670 680 690 700
ILLNVFLAIA VDNLAEAESL TSAQKAKAEE KKRRKMSKGL PDKSEEEKST
710 720 730 740 750
MAKKLEQKPK GEGIPTTAKL KIDEFESNVN EVKDPYPSAD FPGDDEEDEP
760 770 780 790 800
EIPLSPRPRP LAELQLKEKA VPIPEASSFF IFSPTNKIRV LCHRIVNATW
810 820 830 840 850
FTNFILLFIL LSSAALAAED PIRADSMRNQ ILKHFDIGFT SVFTVEIVLK
860 870 880 890 900
MTTYGAFLHK GSFCRNYFNM LDLLVVAVSL ISMGLESSAI SVVKILRVLR
910 920 930 940 950
VLRPLRAINR AKGLKHVVQC MFVAISTIGN IVLVTTLLQF MFACIGVQLF
960 970 980 990 1000
KGKFFRCTDL SKMTEEECRG YYYVYKDGDP MQIELRHREW VHSDFHFDNV
1010 1020 1030 1040 1050
LSAMMSLFTV STFEGWPQLL YKAIDSNAED VGPIYNNRVE MAIFFIIYII
1060 1070 1080 1090 1100
LIAFFMMNIF VGFVIVTFQE QGETEYKNCE LDKNQRQCVQ YALKARPLRC
1110 1120 1130 1140 1150
YIPKNPYQYQ VWYIVTSSYF EYLMFALIML NTICLGMQHY NQSEQMNHIS
1160 1170 1180 1190 1200
DILNVAFTII FTLEMILKLM AFKARGYFGD PWNVFDFLIV IGSIIDVILS
1210 1220 1230 1240 1250
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA
1260 1270 1280 1290 1300
EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI
1310 1320 1330 1340 1350
NRNNNFQTFP QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY
1360 1370 1380 1390 1400
TCGTNFAYYY FISFYMLCAF LVINLFVAVI MDNFDYLTRD WSILGPHHLD
1410 1420 1430 1440 1450
EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP HRVACKRLVG
1460 1470 1480 1490 1500
MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
1510 1520 1530 1540 1550
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK
1560 1570 1580 1590 1600
DIVQIQAGLR TIEEEAAPEI CRTVSGDLAA EEELERAMVE AAMEEGIFRR
1610 1620 1630 1640 1650
TGGLFGQVDN FLERTNSLPP VMANQRPLQF AEIEMEEMES PVFLEDFPQD
1660 1670 1680 1690 1700
PRTNPLARAN TNNANANVAY GNSNHSNSHV FSSVHYEREF PEETETPATR
1710 1720 1730 1740 1750
GRALGQPCRV LGPHSKPCVE MLKGLLTQRA MPRGQAPPAP CQCPRVESSM
1760 1770 1780 1790 1800
PEDRKSSTPG SLHEETPHSR STRENTSRCS APATALLIQK ALVRGGLGTL
1810 1820 1830 1840 1850
AADANFIMAT GQALADACQM EPEEVEIMAT ELLKGREAPE GMASSLGCLN
1860 1870
LGSSLGSLDQ HQGSQETLIP PRL
Length:1,873
Mass (Da):212,350
Last modified:October 14, 2008 - v4
Checksum:i7B7446727E578913
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26R → S in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti265W → C in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti265W → C in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti574A → R in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti574A → R in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti627 – 628YG → SS in AAA51902 (PubMed:7713519).Curated2
Sequence conflicti628G → R in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti916 – 919Missing in AAB37235 (PubMed:8838325).Curated4
Sequence conflicti918 – 919VQ → AR in AAA51902 (PubMed:7713519).Curated2
Sequence conflicti1180D → N in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti1180D → N in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1294 – 1295LV → FE in AAA20531 (PubMed:8004673).Curated2
Sequence conflicti1318R → RHA in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1472R → G in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1510I → M in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1532H → D in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1671G → A in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti1671G → A in AAB37235 (PubMed:8838325).Curated1
Sequence conflicti1710V → S in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti1815A → G in AAA51902 (PubMed:7713519).Curated1
Sequence conflicti1815A → G in AAB37235 (PubMed:8838325).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04697069A → G. Corresponds to variant dbSNP:rs12406479Ensembl.1
Natural variantiVAR_001498458L → H2 PublicationsCorresponds to variant dbSNP:rs12742169Ensembl.1
Natural variantiVAR_054953528R → G in HOKPP1. 1 PublicationCorresponds to variant dbSNP:rs80338778Ensembl.1
Natural variantiVAR_001499528R → H in HOKPP1. 3 PublicationsCorresponds to variant dbSNP:rs80338777Ensembl.1
Natural variantiVAR_054954900R → S in HOKPP1. 1 Publication1
Natural variantiVAR_0015001086R → H in MHS5. 1 PublicationCorresponds to variant dbSNP:rs1800559Ensembl.1
Natural variantiVAR_0015011239R → G in HOKPP1. 3 PublicationsCorresponds to variant dbSNP:rs28930069Ensembl.1
Natural variantiVAR_0015021239R → H in HOKPP1. 4 PublicationsCorresponds to variant dbSNP:rs28930068Ensembl.1
Natural variantiVAR_0015031539R → C1 PublicationCorresponds to variant dbSNP:rs3850625Ensembl.1
Natural variantiVAR_0469711658R → H. Corresponds to variant dbSNP:rs13374149Ensembl.1
Natural variantiVAR_0469721800L → S1 PublicationCorresponds to variant dbSNP:rs12139527Ensembl.1
Natural variantiVAR_0469731840E → D2 PublicationsCorresponds to variant dbSNP:rs1042379Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33798 mRNA. Translation: AAA51902.1.
U30707
, U30666, U30667, U30668, U30669, U30670, U30671, U30672, U30673, U30674, U30675, U30676, U30677, U30678, U30679, U30680, U30681, U30682, U30683, U30684, U30685, U30686, U30687, U30688, U30689, U30690, U30691, U30692, U30693, U30694, U30695, U30696, U30697, U30698, U30699, U30700, U30701, U30702, U30703, U30704, U30705, U30706 Genomic DNA. Translation: AAB37235.1.
AL358473 Genomic DNA. No translation available.
AL139159 Genomic DNA. No translation available.
BC133671 mRNA. Translation: AAI33672.1.
M87486 Genomic DNA. No translation available.
M87487 Genomic DNA. No translation available.
M87488 Genomic DNA. No translation available.
U09784 mRNA. Translation: AAA20531.1.
Z50091 Genomic DNA. No translation available.
Z50092 Genomic DNA. No translation available.
Z50093 Genomic DNA. No translation available.
CCDSiCCDS1407.1.
PIRiA55645.
I38611.
RefSeqiNP_000060.2. NM_000069.2.
UniGeneiHs.1294.

Genome annotation databases

EnsembliENST00000362061; ENSP00000355192; ENSG00000081248.
GeneIDi779.
KEGGihsa:779.
UCSCiuc001gvv.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCAC1S_HUMAN
AccessioniPrimary (citable) accession number: Q13698
Secondary accession number(s): A4IF51
, B1ALM2, Q12896, Q13934
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: November 22, 2017
This is version 187 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families