为什么条件p,q对应的集合A,B.若A包含于B,则p是q的充分条件.我觉得应该是必要条件啊、比如p:A={1} p:B={1,2} A包含于B.p不能推出q 为什么又是充分条件么?难道是我举的例子有问题么?
幻世萌clle
你打成条件p,p了p:A={1} q:B={1,2} .因为p中只有一个元素1,而且1属于集合B.则p能推出q.反之q中元素2不属于A,则q不能推出p.所以p是q的充分不必要条件,或者称q是p的必要不充分条件
“因为p中只有一个元素1，而且1属于集合B。则p能推出q"
q: B={1，2}
p不是只能推出q的一个子集{1}么 怎么能推出整个B呢？
我说的推出意思是：
1属于p，那么能推出1也属于q。则p能推出q（或者这样理解，如果一个元素在范围小的里面，那么一定在范围大的里面）
反之2属于q，但是2不属于p。则q不能推出p（在大的范围里面，不一定在小的范围里面）
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其他类似问题
A包含于B，那么A就推得出B ，A 就是B 的充分条件A就推得出B ，A 就是B 的充分条件
扫描下载二维码下列各题中,p是q的什么条件?(1)p:a+b=0,q:a*2+b*2=0;(2)p:四边形的对角线相等,q:下列各题中,p是q的什么条件?（1）p:a+b=0,q:a*2+b*2=0;(2)p:四边形的对角线相等,q:四边形是矩形；（3）p:x=1或x=2,q:x-1=√x-1;（4）p:m＜-1,q；x*2-x-m=0无实数根例2.求证：实系数一元二次方程x*2+px+q=0有两个异号根的充要条件是q＜0
(1).∵p<=q,∴p是q的必要条件(2).∵p<=q,∴p是q的必要条件(3).∵pq,∴p是q的充要条件(4).∵p=>q,∴p是q的充分条件例2.证明：①充分性：设x1,x2为一元二次方程x²+px+q=0的两根则由韦达定理可知：x1x2=q∵两根异号,∴x1x2<0,即q<0充分性成立.②必要性：设x1,x2为一元二次方程x²+px+q=0的两根则由韦达定理可知：x1x2=q<0即x1x2<0,∴x1,x2异号必要性成立.综上所述：实系数一元二次方程x*2+px+q=0有两个异号根的充要条件是q＜0
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其他类似问题
1. a+b=0不能呢得到a*2+b*2=0，但a*2+b*2=0能得到a=0，b=0，所以a+b=0，因此p是q的必要条件2. 矩形的对角线相等，但对角线相等的四边形必须是平行四边形是才是矩形，因此p是q的必要条件3 p:x=1或x=2是q:x-1=√x-1的解，充分必要条件4.p:m＜-1，q：x*2-x-m=0无实数根，delta小于0求得m<-1/4，充分条件...
扫描下载二维码Protein knowledgebaseSequence archiveHelp pages, FAQs, UniProtKB manual, documents, news archive and Biocuration projects.Sequence clustersProtein sets from fully sequenced genomesAnnotation systemsSystems used to automatically annotate proteins with high accuracy:Supporting dataSelect one of the options below to target your search:Voltage-dependent P/Q-type calcium channel subunit alpha-1ACacna1aMus musculus (Mouse)-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveliFunctioniVoltage-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-1A gives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).SitesFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsSitei1Calcium ion selectivity and permeabilitySitei1Calcium ion selectivity and permeabilitySitei1Calcium ion selectivity and permeabilitySitei1Binds to omega-Aga-IVASitei1Calcium ion selectivity and permeabilityRegionsFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsCalcium bindingi12GO - Molecular functioniGO - Biological processiKeywords - Molecular functioni, , Keywords - Biological processi, , Keywords - Ligandi, Enzyme and pathway databases
Reactomei Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
Regulation of insulin secretion. Names & TaxonomyiProtein namesiRecommended name:Voltage-dependent P/Q-type calcium channel subunit alpha-1AAlternative name(s):Brain calcium channel IShort name: BICalcium channel, L type, alpha-1 polypeptide isoform 4Voltage-gated calcium channel subunit alpha Cav2.1Gene namesiName:Cacna1aSynonyms:Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1aOrganismiTaxonomic identifieri
[]Taxonomic lineagei &
Proteomesi Componenti: Chromosome 8 Organism-specific databases
MGIi Cacna1a. Subcellular locationi; TopologyFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsTopological domaini100CytoplasmicTransmembranei19H Name=S1 of repeat ITopological domaini19ExtracellularTransmembranei18H Name=S2 of repeat ITopological domaini12CytoplasmicTransmembranei16H Name=S3 of repeat ITopological domaini8ExtracellularTransmembranei19H Name=S4 of repeat ITopological domaini19CytoplasmicTransmembranei20H Name=S5 of repeat ITopological domaini87ExtracellularTransmembranei25H Name=S6 of repeat ITopological domaini127CytoplasmicTransmembranei20H Name=S1 of repeat IITopological domaini14ExtracellularTransmembranei20H Name=S2 of repeat IITopological domaini8CytoplasmicTransmembranei19H Name=S3 of repeat IITopological domaini10ExtracellularTransmembranei19H Name=S4 of repeat IITopological domaini19CytoplasmicTransmembranei20H Name=S5 of repeat IITopological domaini53ExtracellularTransmembranei25H Name=S6 of repeat IITopological domaini474CytoplasmicTransmembranei24H Name=S1 of repeat IIITopological domaini17ExtracellularTransmembranei20H Name=S2 of repeat IIITopological domaini7CytoplasmicTransmembranei24H Name=S3 of repeat IIITopological domaini11ExtracellularTransmembranei18H Name=S4 of repeat IIITopological domaini19CytoplasmicTransmembranei20H Name=S5 of repeat IIITopological domaini87ExtracellularTransmembranei25H Name=S6 of repeat IIITopological domaini56CytoplasmicTransmembranei19H Name=S1 of repeat IVTopological domaini14ExtracellularTransmembranei22H Name=S2 of repeat IVTopological domaini7CytoplasmicTransmembranei20H Name=S3 of repeat IVTopological domaini7ExtracellularTransmembranei19H Name=S4 of repeat IVTopological domaini19CytoplasmicTransmembranei20H Name=S5 of repeat IVTopological domaini72ExtracellularTransmembranei26H Name=S6 of repeat IVTopological domaini605CytoplasmicGO - Cellular componentiKeywords - Cellular componentiPathology & BiotechiInvolvement in diseaseiDefects in Cacna1a are the cause of a delayed-onset, recessive neurological disorder seen in tottering (tg) mutants, resulting in ataxia, motor seizures and behavioral absence seizures resembling petit mal epilepsy (or absence epilepsy) in humans. There are two more alleles, leaner (tg(lA)), that is characterized by severe ataxia and frequent death past weaning, b and rolling Nagoya (tg(rol)), that presents an intermediary phenotype, the ataxia being somewhat more severe that with tg, but without motors seizures. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants.Keywords - DiseaseiPTM / ProcessingiMolecule processingFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsChaini2368Voltage-dependent P/Q-type calcium channel subunit alpha-1APRO_Amino acid modificationsFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsGlycosylationi1N-linked (GlcNAc...)Modified residuei1Phosphothreonine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"Comprehensive identification of phosphorylation sites in postsynaptic density preparations.", , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Glycosylationi1N-linked (GlcNAc...)Modified residuei1Phosphothreonine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1PhosphoserineModified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1PhosphoserineModified residuei1PhosphoserineModified residuei1Phosphoserine"A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Modified residuei1PhosphoserineKeywords - PTMi, , Proteomic databases
PeptideAtlasi
PRIDEi PTM databases
PhosphoSitei ExpressioniTissue specificityiB mainly found in the cerebellum, olfactory bulb, cerebral cortex, hippocampus, and inferior colliculus. In the hippocampus, expression occurs in pyramidal and granule neurons, as well as in interneurons. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells.Gene expression databases
ExpressionAtlasi baseline and differential.
Genevisiblei MM. InteractioniSubunit structureiVoltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with CABP1 (By similarity).GO - Molecular functioniProtein-protein interaction databases
BioGridi 4 interactions.
IntActi 1 interaction.
STRINGi Structurei3D structure databases
ProteinModelPortali
SMRi Positions
MobiDBiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsRepeati301IRepeati245IIRepeati284IIIRepeati264IVRegionFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsRegioni18Binding to the beta subunitCompositional biasFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsCompositional biasi6Poly-GluCompositional biasi4Poly-GluDomainiEach 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.Sequence similaritiesiBelongs to the . . []Keywords - Domaini, , Phylogenomic databases
eggNOGi Eukaryota.
InParanoidi
PhylomeDBi
TreeFami Family and domain databases
Gene3Di 4 hits.
InterProi CACNA1A.
Channel_four-helix_dom.
Ion_trans_dom.
VDCC_a1su_IQ.
VDCCAlpha1.
PANTHERi PTHR10037:SF59. 3 hits.
Pfami Ca_chan_IQ. 1 hit.
GPHH. 1 hit.
Ion_trans. 4 hits.
PRINTSi CACHANNEL.
PQVDCCALPHA1.
SMARTi Ca_chan_IQ. 1 hit.
[]SequenceiSequence statusi: Complete.P97445-1 []
50MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY
100KQSMAQRART MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP
150PFEYMILATI IANCIVLALE QHLPDDDKTP MSERLDDTEP YFIGIFCFEA
200GIKIVALGFA FHKGSYLRNG WNVMDFVVVL TGILATVGTE FDLRTLRAVR
250VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL IFAIIGLEFY
300MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
350TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS
400FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK
450AEEVILAEDE TDVEQRHPFD GALRRATLKK SKTDLLNPEE AEDQLADIAS
500VGSPFARASI KSAKLENSTF FHKKERRMRF YIRRMVKTQA FYWTVLSLVA
550LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM YGLGTRPYFH
600SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
650SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP
700TNFDTFPAAI MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT
750LFGNYTLLNV FLAIAVDNLA NAQELTKDEQ EEEEAANQKL ALQKAKEVAE
800VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR TSEMRKQNLL ASREALYGDA
850AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR APEALRPTAR
900PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
950DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA
1000TRPARAADGE GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP
1050NLSTTRPIQQ DLGRQDLPLA EDLDNMKNNK LATGEPASPH DSLGHSGLPP
1100SPAKIGNSTN PGPALATNPQ NAASRRTPNN PGNPSNPGPP KTPENSLIVT
1150NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN ANPDPLPKKE
1200EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
1250ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL
1300GLVLHQGAYF RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR
1350VLRPLKTIKR LPKLKAVFDC VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF
1400KGKFFHCTDE SKEFERDCRG KYLLYEKNEV KARDREWKKY EFHYDNVLWA
1450LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI FYVVYFVVFP
1500FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
1550QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR
1600VFNIVFTSLF SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE
1650FGNNFINLSF LRLFRAARLI KLLRQGYTIR ILLWTFVQSF KALPYVCLLI
1700AMLFFIYAII GMQVFGNIGI DGEDEDSDED EFQITEHNNF RTFFQALMLL
1750FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF YFVSFIFLCS
1800FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
1850KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA
1900LIRTALDIKI AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST
1950DLTVGKIYAA MMIMEYYRQS KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE
2000GGPSQNALPS TQLDPGGGLM AHEGGMKESP SWVTQRAQEM FQKTGTWSPE
2050RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT RAASMPRLPA
2100ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
2150QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD
2200RGRPKDRKHR PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS
2250PSEGREHTTH RQGSSSVSGS PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS
2300YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA PRWPAHAPEG PRPRGADYTE
2350PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY YAGHGAPRPR
2360 TARRGAHDAY SESEDDWC
2,368267,647February 6, 2007 - v2Checksum:iE7B573BA005E5CB1BLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterExperimental InfoFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsSequence conflicti1S & P in
(PubMed:).Sequence conflicti1L & F in
(PubMed:).Sequence conflicti1P & L in
(PubMed:).Sequence conflicti1E & D in
() Sequence conflicti1N & D in
(PubMed:).Sequence conflicti1L & F in
(PubMed:).Sequence conflicti1L & F in
(PubMed:).Sequence conflicti1P & PH in
() Natural variantFeature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActionsNatural varianti1P & L in tg. "Absence epilepsy in tottering mutant mice is associated with calcium channel defects.", , , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF , VARIANT TG LEU-649. Sequence databases
Select the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: .
UniGenei Genome annotation databases
Ensembli; ; .
UCSCi mouse. Cross-referencesiSequence databases
Select the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: .
UniGenei 3D structure databases
ProteinModelPortali
SMRi Positions
MobiDBiProtein-protein interaction databases
BioGridi 4 interactions.
IntActi 1 interaction.
STRINGi PTM databases
PhosphoSitei Proteomic databases
PeptideAtlasi
PRIDEi Protocols and materials databases
Structural Biology KnowledgebaseGenome annotation databases
Ensembli; ; .
UCSCi mouse. Organism-specific databases
MGIi Cacna1a. Phylogenomic databases
eggNOGi Eukaryota.
InParanoidi
PhylomeDBi
TreeFami Enzyme and pathway databases
Reactomei Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
Regulation of insulin secretion. Miscellaneous databases
ChiTaRSi mouse.
SOURCEiGene expression databases
ExpressionAtlasi baseline and differential.
Genevisiblei MM. Family and domain databases
Gene3Di 4 hits.
InterProi CACNA1A.
Channel_four-helix_dom.
Ion_trans_dom.
VDCC_a1su_IQ.
VDCCAlpha1.
PANTHERi PTHR10037:SF59. 3 hits.
Pfami Ca_chan_IQ. 1 hit.
GPHH. 1 hit.
Ion_trans. 4 hits.
PRINTSi CACHANNEL.
PQVDCCALPHA1.
SMARTi Ca_chan_IQ. 1 hit.
ProtoNetiPublicationsi"Molecular identity of P-type calcium current in Purkinje neurons.", , Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: . Tissue: . "Absence epilepsy in tottering mutant mice is associated with calcium channel defects.", , , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF , VARIANT TG LEU-649. Strain: . "Comprehensive identification of phosphorylation sites in postsynaptic density preparations.", , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: . "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.", , , , , , , , , , , ,
[] [] []Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: . "A tissue-specific atlas of mouse protein phosphorylation and expression.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453; SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: . + MiscellaneousiKeywords - Technical termi, Documents
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
Index of protein domains and families
Similar proteinsiLinks to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
