圆心角为120&的扇形，其弧长为2／3π，则它的面积为（
）弧所对弦长是（
）此弧和弦所成弓形的面积（
我要解题过程，解题思路
圆心角为120&的扇形，其弧长为2／3π，则它的面积为（ ）弧所对弦长是（ ）此弧和弦所成弓形的面积（ ）
设圆心角为120°扇形的半径为r，那么其所在圆的圆周长为2πr
所以弧长为(2πr)*(120°/360°)=(2/3)πr
所以，(2/3)πr=(2/3)π
那么，它的面积=(1/3)*πr^2=π/3
过圆心作弦的垂线，垂足就是弦的中点，在直角三角形中顶角为120°/2=60°
所以，它所对的直角边为r*sin60°=1*(√3/2)=√3/2
那么，弦长=2*(√3/2)=√3
则等腰三角形的面积=(1/2)*[√3*(1/2)]=√3/4
所以弓形的面积=(π/3)-(√3/4)
解：设扇形的半径是r，则150πr/180 =20π
解得：r=24．
扇形的面积是：1/2 ×20π×24=240π．
故答案是：24和240π．
己知扇形的圆心角为120度,半径为3,则扇形的面积
3x3x3.14x120/360=9.42
设圆锥母线为L,则： 3π=1/3（πL^2),得L=3.
设圆锥底面半径为R，则：1/3(2πL)=2πR,得R=1.
圆锥的底面积：πR^2=π
定义：弧长等于圆半径长的弧所对的圆心角为1弧度。
弧度是角的量度单位。它是由国际单位制导出的单位。
弧度制，顾名思义，就是用弧的长度来度量角的大小的方法。由于圆...
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这个不是我熟悉的地区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:You are using a version of browser that may not display all the features of this website. Please consider upgrading . Phosphatidylinositol 4-kinase type 2-alphaPI4K2AHomo sapiens (Human)-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveliFunctioniMembrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION."Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor.", , , , ,
[] [] []Cited for: FUNCTION, SUBCELLULAR LOCATION."Relationship between phosphatidylinositol 4-phosphate synthesis, membrane organization, and lateral diffusion of PI4KIIalpha at the trans-Golgi network.", , , , ,
[] [] []Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION."Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch.", , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, FUNCTION."The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.Catalytic activityiATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION."Relationship between phosphatidylinositol 4-phosphate synthesis, membrane organization, and lateral diffusion of PI4KIIalpha at the trans-Golgi network.", , , , ,
[] [] []Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION."The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.SitesFeature keyPosition(s)DescriptionActionsGraphical viewLengthBinding siteiATPManual assertion based on experiment ini"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1Binding siteiATPManual assertion based on experiment ini"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1RegionsFeature keyPosition(s)DescriptionActionsGraphical viewLengthNucleotide bindingiATPManual assertion based on experiment ini"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.7Nucleotide bindingiATPManual assertion based on experiment ini"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.4GO - Molecular functioniInferred from direct assayiInferred from direct assayiInferred from direct assayiNon-traceable author statementiGO - Biological processiInferred from direct assayiInferred from direct assayiKeywordsiMolecular function, Ligand, Enzyme and pathway databasesBioCyci Reactomei Synthesis of PIPs at the plasma membrane.
Synthesis of PIPs at the Golgi membrane.
Synthesis of PIPs at the early endosome membrane. SIGNORi Names & TaxonomyiProtein namesiRecommended name:Phosphatidylinositol 4-kinase type 2-alpha (EC:Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION."Relationship between phosphatidylinositol 4-phosphate synthesis, membrane organization, and lateral diffusion of PI4KIIalpha at the trans-Golgi network.", , , , ,
[] [] []Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION."The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.)Alternative name(s):Phosphatidylinositol 4-kinase type II-alphaGene namesiName:OrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 10 Organism-specific databasesEuPathDBi HGNCi PI4K2A. Subcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: "Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor.", , , , ,
[] [] []Cited for: FUNCTION, SUBCELLULAR LOCATION."Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch.", , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, FUNCTION.Golgi apparatus Manual assertion based on experiment ini"Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor.", , , , ,
[] [] []Cited for: FUNCTION, SUBCELLULAR LOCATION."Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178.;
Manual assertion based on experiment ini"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178.Plasma membrane Manual assertion inferred from sequence similarity toi Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION."Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor.", , , , ,
[] [] []Cited for: FUNCTION, SUBCELLULAR LOCATION.Mitochondrion Manual assertion inferred from sequence similarity toiOther locations Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION. Manual assertion inferred from sequence similarity toi Manual assertion inferred from sequence similarity toi Manual assertion based on experiment ini"Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor.", , , , ,
[] [] []Cited for: FUNCTION, SUBCELLULAR LOCATION. Manual assertion based on experiment ini"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.;
Manual assertion based on experiment ini"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.Note: Localized in neuronal cell body. Transported from neuronal cell body to neuron projections in a BLOC-1- and AP-3-complexes-dependent manner. Enriched in neurite tips and neuron projections in a BLOC-1- and AP-3-complexes-dependent manner (By similarity). Found in subdomains of the plasma membrane termed non-caveolar membrane rafts.Manual assertion inferred from sequence similarity toiKeywords - Cellular componenti, , , , , , , , , Pathology & BiotechiMutagenesisOrganism-specific databasesDisGeNETi OpenTargetsi PharmGKBi Chemistry databasesChEMBLi GuidetoPHARMACOLOGYi Polymorphism and mutation databasesBioMutai DMDMi PTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthChainiPRO_Phosphatidylinositol 4-kinase type 2-alpha 479Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthModified residueiN-acetylmethionineManual assertion inferred from combination of experimental and computational evidencei"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", , , , , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.", , , , , , , , , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."N-terminome analysis of the human mitochondrial proteome.", , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", , , , , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", , , , , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", , , , , , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1LipidationiS-palmitoyl cysteineManual assertion inferred by curator fromi"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1LipidationiS-palmitoyl cysteineManual assertion inferred by curator fromi"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1LipidationiS-palmitoyl cysteineManual assertion inferred by curator fromi"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1LipidationiS-palmitoyl cysteineManual assertion inferred by curator fromi"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.1Modified residueiPhosphoserineManual assertion inferred from sequence similarity toi1Post-translational modificationiPalmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization.Manual assertion based on experiment ini"Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner.", , , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178.Ubiquitinated by ITCH; this does not lead to proteasomal degradation.Manual assertion based on experiment ini"Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch.", , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, FUNCTION.Keywords - PTMi, , , , Proteomic databasesEPDi MaxQBi PaxDbi PeptideAtlasi PRIDEi PTM databasesiPTMneti PhosphoSitePlusi SwissPalmi ExpressioniTissue specificityiWidely expressed. Highest expression is observed in kidney, brain, heart, skeletal muscle, and placenta and lowest expression is observed in colon, thymus, and small intestine.Manual assertion based on experiment ini"Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family.", , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION.Gene expression databasesBgeei CleanExi Genevisiblei HS. Organism-specific databasesHPAi
InteractioniSubunit structureiAssociates with the BLOC-1 and the AP-3 the BLOC-1 complex is required for optimal binding of PI4K2A to the AP-3 complex. Interacts with BLOC1S5 and DTNBP1 (PubMed:). Interacts with FOS; this interaction may enhance phosphatidylinositol phosphorylation activity (By similarity). Interacts with ITCH (PubMed:).Manual assertion inferred from sequence similarity toiManual assertion based on experiment ini"The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse.", , , , , , , , , ,
[] [] []Cited for: INTERACTION WITH BLOC1S5 AND DTNBP1."Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch.", , , , , ,
[] [] []Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, FUNCTION.Binary interactionsiWithEntry#Exp.IntActNotesITCH5GO - Molecular functioniInferred from direct assayiProtein-protein interaction databasesBioGridi 23 interactors.CORUMi IntActi 7 interactors.STRINGi Chemistry databasesBindingDBi StructureiSecondary structure1479Legend: HelixTurnBeta strandPDB Structure known for this areaFeature keyPosition(s)DescriptionActionsGraphical viewLengthHelixiManual assertion inferred from combination of experimental and computational evidencei16HelixiManual assertion inferred from combination of experimental and computational evidencei5HelixiManual assertion inferred from combination of experimental and computational evidencei15Beta strandiManual assertion inferred from combination of experimental and computational evidencei6Beta strandiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei7HelixiManual assertion inferred from combination of experimental and computational evidencei3TurniManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5HelixiManual assertion inferred from combination of experimental and computational evidencei15Beta strandiManual assertion inferred from combination of experimental and computational evidencei6HelixiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei10HelixiManual assertion inferred from combination of experimental and computational evidencei21Beta strandiManual assertion inferred from combination of experimental and computational evidencei6Beta strandiManual assertion inferred from combination of experimental and computational evidencei6TurniManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei11HelixiManual assertion inferred from combination of experimental and computational evidencei15HelixiManual assertion inferred from combination of experimental and computational evidencei23HelixiManual assertion inferred from combination of experimental and computational evidencei53D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray3.20A/B[]X-ray2.95A/B[]X-ray2.77A[]X-ray2.58A[]X-ray2.80A[]X-ray2.28A[]ProteinModelPortali SMRi ModBaseiMobiDBiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDomainiPI3K/PI4K 306RegionFeature keyPosition(s)DescriptionActionsGraphical viewLengthRegioniImportant for substrate bindingManual assertion inferred by curator fromi"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.3RegioniImportant for interaction with membranesManual assertion inferred by curator fromi"The crystal structure of the phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF
IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445."Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368. 14RegioniImportant for interaction with membranesManual assertion inferred by curator fromi"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.9RegioniImportant for interaction with membranesManual assertion inferred by curator fromi"Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha.", , , , , , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF
IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.10Compositional biasFeature keyPosition(s)DescriptionActionsGraphical viewLengthCompositional biasiPoly-Ala4Compositional biasiAla-rich 33Sequence similaritiesiBelongs to the . .Phylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Family and domain databasesInterProi PI3/4_kinase_cat_dom. Pfami PI3_PI4_kinase. 1 hit. SequenceiSequence statusi: Complete.Q9BTU6-1 []
50MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG
100SPGHDRERQP LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE
150RNEFPEDPEF EAVVRQAELA IERCIFPERI YQGSSGSYFV KDPQGRIIAV
200FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG RDCLVLNQGY LSEAGASLVD
250QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK VPKVGQRFNR
300IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
350DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA
400FPLKHPDSWR AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED
450LYELFKKDPG FDRGQFHKQI AVMRGQILNL TQALKDNKSP LHLVQMPPVI
470 VETARSHQRS SSESYTQSFQ SRKPFFSWW
47954,022June 1, 2001 - v1Checksum:i9C9F4CE23F197BBDBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterSequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: . Genomic DNA. Translation: . Genomic DNA. Translation: . Genomic DNA. Translation: . mRNA. Translation: . mRNA. Translation: .CCDSi PIRi RefSeqi UniGenei Genome annotation databasesEnsembli; ; . GeneIDi KEGGi UCSCi human. Similar proteinsi mRNA. Translation: . mRNA. Translation: . Genomic DNA. Translation: . Genomic DNA. Translation: . Genomic DNA. Translation: . mRNA. Translation: . mRNA. Translation: .CCDSi PIRi RefSeqi UniGenei 3D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray3.20A/B[]X-ray2.95A/B[]X-ray2.77A[]X-ray2.58A[]X-ray2.80A[]X-ray2.28A[]ProteinModelPortali SMRi ModBaseiMobiDBiProtein-protein interaction databasesBioGridi 23 interactors.CORUMi IntActi 7 interactors.STRINGi Chemistry databasesBindingDBi ChEMBLi GuidetoPHARMACOLOGYi PTM databasesiPTMneti PhosphoSitePlusi SwissPalmi Polymorphism and mutation databasesBioMutai DMDMi Proteomic databasesEPDi MaxQBi PaxDbi PeptideAtlasi PRIDEi Protocols and materials databasesDNASUi Structural Biology KnowledgebaseGenome annotation databasesEnsembli; ; . GeneIDi KEGGi UCSCi human. Organism-specific databasesCTDi DisGeNETi EuPathDBi GeneCardsi HGNCi PI4K2A. HPAi
MIMi gene. neXtProti OpenTargetsi PharmGKBi GenAtlasiPhylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Enzyme and pathway databasesBioCyci Reactomei Synthesis of PIPs at the plasma membrane.
Synthesis of PIPs at the Golgi membrane.
Synthesis of PIPs at the early endosome membrane. SIGNORi Miscellaneous databasesChiTaRSi human. GeneWikii GenomeRNAii PROi SOURCEiGene expression databasesBgeei CleanExi Genevisiblei HS. Family and domain databasesInterProi PI3/4_kinase_cat_dom. Pfami PI3_PI4_kinase. 1 hit. ProtoNetiMiscellaneousiKeywords - Technical termi, , Documents
Human chromosome 10: entries, gene names and cross-references to MIM
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Index of Protein Data Bank (PDB) cross-references
Index of protein domains and families