膨胀机工作原理ZR7-750AT-D这是什么意思?

D_绯色喜欢的音乐 - 歌单 - 网易云音乐
D_绯色喜欢的音乐
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D温燙傷喜欢的音乐
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举报邮箱: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 .
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ATP-dependent RNA helicase DDX24DDX24Homo sapiens (Human)-Annotation score: -Experimental evidence at protein leveliFunctioniATP-dependent RNA helicase.Catalytic activityiATP + H2O = ADP + phosphate.RegionsFeature keyPosition(s)DescriptionActionsGraphical viewLengthNucleotide bindingiATPManual assertion according to rulesi8GO - Molecular functioniInferred from high throughput direct assayiNon-traceable author statementiGO - Biological processiNon-traceable author statementiKeywordsiMolecular function, , Ligand, Names & TaxonomyiProtein namesiRecommended name:ATP-dependent RNA helicase DDX24 (EC:)Alternative name(s):DEAD box protein 24Gene namesiName:OrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 14 Organism-specific databasesEuPathDBi HGNCi DDX24. MIMi gene. neXtProti Subcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: Pathology & BiotechiOrganism-specific databasesOpenTargetsi PharmGKBi Polymorphism and mutation databasesBioMutai DMDMi PTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthChainiPRO_ATP-dependent RNA helicase DDX24 859Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthModified residueiN6-acetyllysineManual assertion inferred from combination of experimental and computational evidencei"Lysine acetylation targets protein complexes and co-regulates major cellular functions.", , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-71, 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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiN6-acetyllysineManual assertion inferred from combination of experimental and computational evidencei"Lysine acetylation targets protein complexes and co-regulates major cellular functions.", , , , , , ,
[] [] []Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-71, 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-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."A probability-based approach for high-throughput protein phosphorylation analysis and site localization.", , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, 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-82; SER-94; SER-287 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", , , , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, 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-82, 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-82 AND SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, 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-82; SER-94; SER-287 AND SER-295, 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-82 AND SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, 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-82; SER-94; SER-287 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, 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-82; SER-94; SER-287 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphothreonineManual assertion inferred from combination of experimental and computational evidencei"A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-94; SER-287; SER-295 AND THR-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Cross-linkiGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Manual assertion inferred from combination of experimental and computational evidencei"Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.", , , , ,
[] [] []Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-370; LYS-624; LYS-808 AND LYS-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Cross-linkiGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Manual assertion inferred from combination of experimental and computational evidencei"Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.", , , , ,
[] [] []Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-370; LYS-624; LYS-808 AND LYS-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Cross-linkiGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Manual assertion inferred from combination of experimental and computational evidencei"Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.", , , , ,
[] [] []Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-370; LYS-624; LYS-808 AND LYS-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Cross-linkiGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Manual assertion inferred from combination of experimental and computational evidencei"Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.", , , , ,
[] [] []Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-370; LYS-624; LYS-808 AND LYS-825, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Keywords - PTMi, , , Proteomic databasesEPDi MaxQBi PaxDbi PeptideAtlasi PRIDEi 2D gel databasesSWISS-2DPAGEi PTM databasesiPTMneti PhosphoSitePlusi ExpressioniTissue specificityiUbiquitous. Most abundant in heart and brain, but with lowest levels in thymus and small intestine.Gene expression databasesBgeei CleanExi ExpressionAtlasi baseline and differential. Genevisiblei HS. Organism-specific databasesHPAi InteractioniBinary interactionsiWithEntry#Exp.IntActNotesMYC2Protein-protein interaction databasesBioGridi 159 interactors.DIPi IntActi 52 interactors.MINTi STRINGi Structurei3D structure databasesProteinModelPortali SMRi ModBaseiMobiDBiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDomainiHelicase ATP-bindingManual assertion according to rulesi 305DomainiHelicase C-terminalManual assertion according to rulesi 146MotifFeature keyPosition(s)DescriptionActionsGraphical viewLengthMotifiQ motif 29MotifiDEAD box4Compositional biasFeature keyPosition(s)DescriptionActionsGraphical viewLengthCompositional biasiPoly-Glu7Compositional biasiPoly-Lys9Compositional biasiPoly-Lys 11Sequence similaritiesiBelongs to the . .Phylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Family and domain databasesCDDi HELICc. 1 hit. InterProi DEAD/DEAH_box_helicase_dom.
Helicase_ATP-bd.
Helicase_C.
P-loop_NTPase.
RNA-helicase_DEAD-box_CS.
RNA_helicase_DEAD_Q_motif. Pfami DEAD. 1 hit.
Helicase_C. 1 hit. SMARTi DEXDc. 1 hit.
HELICc. 1 hit. SUPFAMi SSF52540. 3 hits. PROSITEi DEAD_ATP_HELICASE. 1 hit.
HELICASE_ATP_BIND_1. 1 hit.
HELICASE_CTER. 1 hit.
Q_MOTIF. 1 hit. Sequences (2)iSequence statusi: Complete.This entry describes 2 isoformsi produced by alternative splicing.
(identifier: Q9GZR7-1)
[]This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
50MKLKDTKSRP KQSSCGKFQT KGIKVVGKWK EVKIDPNMFA DGQMDDLVCF
100EELTDYQLVS PAKNPSSLFS KEAPKRKAQA VSEEEEEEEG KSSSPKKKIK
150LKKSKNVATE GTSTQKEFEV KDPELEAQGD DMVCDDPEAG EMTSENLVQT
200APKKKKNKGK KGLEPSQSTA AKVPKKAKTW IPEVHDQKAD VSAWKDLFVP
250RPVLRALSFL GFSAPTPIQA LTLAPAIRDK LDILGAAETG SGKTLAFAIP
300MIHAVLQWQK RNAAPPPSNT EAPPGETRTE AGAETRSPGK AEAESDALPD
350DTVIESEALP SDIAAEARAK TGGTVSDQAL LFGDDDAGEG PSSLIREKPV
400PKQNENEEEN LDKEQTGNLK QELDDKSATC KAYPKRPLLG LVLTPTRELA
450VQVKQHIDAV ARFTGIKTAI LVGGMSTQKQ QRMLNRRPEI VVATPGRLWE
500LIKEKHYHLR NLRQLRCLVV DEADRMVEKG HFAELSQLLE MLNDSQYNPK
550RQTLVFSATL TLVHQAPARI LHKKHTKKMD KTAKLDLLMQ KIGMRGKPKV
600IDLTRNEATV ETLTETKIHC ETDEKDFYLY YFLMQYPGRS LVFANSISCI
650KRLSGLLKVL DIMPLTLHAC MHQKQRLRNL EQFARLEDCV LLATDVAARG
700LDIPKVQHVI HYQVPRTSEI YVHRSGRTAR ATNEGLSLML IGPEDVINFK
750KIYKTLKKDE DIPLFPVQTK YMDVVKERIR LARQIEKSEY RNFQACLHNS
800WIEQAAAALE IELEEDMYKG GKADQQEERR RQKQMKVLKK ELRHLLSQPL
850FTESQKTKYP TQSGKPPLLV SAPSKSESAL SCLSKQKKKK TKKPKEPQPE QPQPSTSAN
85996,332March 1, 2001 - v1Checksum:iB01B1170B2CFA0F7BLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutter (identifier: Q9GZR7-2)
[]The sequence of this isoform differs from the canonical sequence as follows:
: Missing.Note: No experimental confirmation available.>>80490,298Checksum:iDB6589BLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterNatural variantFeature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_052162. Corresponds to variant .1Alternative sequenceFeature keyPosition(s)DescriptionActionsGraphical viewLengthAlternative sequenceiVSP_053881Missing
in isoform . Manual assertion based on opinion ini"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
[] [] []Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 55Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: .CCDSi
[]UniGenei Genome annotation databasesEnsembli; ; .
[]GeneIDi KEGGi UCSCi human.
[]Keywords - Coding sequence diversityi, Similar proteinsi mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: . mRNA. Translation: .CCDSi
[]UniGenei 3D structure databasesProteinModelPortali SMRi ModBaseiMobiDBiProtein-protein interaction databasesBioGridi 159 interactors.DIPi IntActi 52 interactors.MINTi STRINGi PTM databasesiPTMneti PhosphoSitePlusi Polymorphism and mutation databasesBioMutai DMDMi 2D gel databasesSWISS-2DPAGEi Proteomic databasesEPDi MaxQBi PaxDbi PeptideAtlasi PRIDEi Protocols and materials databasesDNASUi Structural Biology KnowledgebaseGenome annotation databasesEnsembli; ; .
[]GeneIDi KEGGi UCSCi human.
[]Organism-specific databasesCTDi EuPathDBi GeneCardsi HGNCi DDX24. HPAi MIMi gene. neXtProti OpenTargetsi PharmGKBi GenAtlasiPhylogenomic databaseseggNOGi Eukaryota.
LUCA. GeneTreei HOGENOMi HOVERGENi InParanoidi KOi OMAi OrthoDBi PhylomeDBi TreeFami Miscellaneous databasesChiTaRSi human. GeneWikii GenomeRNAii PROi SOURCEiGene expression databasesBgeei CleanExi ExpressionAtlasi baseline and differential. Genevisiblei HS. Family and domain databasesCDDi HELICc. 1 hit. InterProi DEAD/DEAH_box_helicase_dom.
Helicase_ATP-bd.
Helicase_C.
P-loop_NTPase.
RNA-helicase_DEAD-box_CS.
RNA_helicase_DEAD_Q_motif. Pfami DEAD. 1 hit.
Helicase_C. 1 hit. SMARTi DEXDc. 1 hit.
HELICc. 1 hit. SUPFAMi SSF52540. 3 hits. PROSITEi DEAD_ATP_HELICASE. 1 hit.
HELICASE_ATP_BIND_1. 1 hit.
HELICASE_CTER. 1 hit.
Q_MOTIF. 1 hit. ProtoNetiMiscellaneousiKeywords - Technical termi,D.LY - 歌单 - 网易云音乐
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同步歌单,随时畅听320k好音乐
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