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3秒自动关闭窗口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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Ribosomal protein S6 kinase alpha-1RPS6KA1Homo sapiens (Human)-Annotation score: -Experimental evidence at protein leveliFunctioniSerine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:).Manual assertion inferred from sequence similarity toiManual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732."Rsk1 mediates a MEK-MAP kinase cell survival signal.", , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF BAD."C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival.", , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF CEBPB."Regulation of the ETS transcription factor ER81 by the 90-kDa ribosomal S6 kinase 1 and protein kinase A.",
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF ETV1/ER81, INTERACTION WITH ETV1/ER81."90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH FGFR1, ENZYME REGULATION, SUBCELLULAR LOCATION."Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase.", , , ,
[] [] []Cited for: FUNCTION IN MTOR SIGNALING, INTERACTION WITH TSC2."The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling.", , , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK1."Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation.", , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF NR4A1/NUR77."The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity.", , , , , , , , ,
[] [] []Cited for: FUNCTION IN TRANSLATION REGULATION, FUNCTION IN PHOSPHORYLATION OF EIF4B."RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation.", , , , , , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6."Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation.", , , , , ,
[] [] []Cited for: FUNCTION IN MTOR SIGNALING."Crucial roles of RSK in cell motility by catalysing serine phosphorylation of EphA2.", , , , , , , , , ,
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF EPHA2.Catalytic activityiATP + a protein = ADP + a phosphoprotein.CofactoriEnzyme regulationiUpon extracellular signal or mitogen stimulation, phosphorylated at Thr-573 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-380, allowing binding of PDPK1, which in turn phosphorylates Ser-221 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.Manual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732."90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH FGFR1, ENZYME REGULATION, SUBCELLULAR LOCATION.SitesFeature keyPosition(s)DescriptionActionsGraphical viewLengthBinding siteiATPManual assertion according to rulesi1Active siteiProton acceptor1Binding siteiATPManual assertion according to rulesi1Active siteiProton acceptor1RegionsFeature keyPosition(s)DescriptionActionsGraphical viewLengthNucleotide bindingiATPManual assertion according to rulesi9Nucleotide bindingiATPManual assertion according to rulesi9GO - Molecular functioniInferred from direct assayiInferred from direct assayiInferred from direct assayiGO - Biological processiInferred from mutant phenotypeiInferred from direct assayiTraceable author statementiTraceable author statementiInferred from mutant phenotypeiInferred from mutant phenotypeiTraceable author statementiTraceable author statementiTraceable author statementiKeywordsiMolecular function, , Biological process, Ligand, , , Enzyme and pathway databasesBRENDAi 2681Reactomei ERK/MAPK targets CREB phosphorylation Senescence-Associated Secretory Phenotype (SASP) Recycling pathway of L1 CREB phosphorylation through the activation of Ras RSK activation Gastrin-CREB signalling pathway via PKC and MAPKSABIO-RKiSignaLinkiSIGNORiNames & TaxonomyiProtein namesiRecommended name:Ribosomal protein S6 kinase alpha-1 (EC:)Short name: S6K-alpha-1Alternative name(s):90 kDa ribosomal protein S6 kinase 1Short name: p90-RSK 1Short name: p90RSK1Short name: p90S6KMAP kinase-activated protein kinase 1aShort name: MAPK-activated protein kinase 1aShort name: MAPKAP kinase 1aShort name: MAPKAPK-1aRibosomal S6 kinase 1Short name: RSK-1Gene namesiName:Synonyms:MAPKAPK1A, RSK1OrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 1 Organism-specific databasesEuPathDBiHGNCi RPS6KA1MIMi geneneXtProtiSubcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: Keywords - Cellular componenti, Pathology & BiotechiOrganism-specific databasesDisGeNETiOpenTargetsiPharmGKBiChemistry databasesChEMBLiDrugBanki Purvalanol AGuidetoPHARMACOLOGYiPolymorphism and mutation databasesBioMutaiDMDMiPTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthChainiPRO_Ribosomal protein S6 kinase alpha-1 735Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthModified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiP by PDPK1Manual assertion inferred by curator fromi"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphothreonineManual assertion inferred from combination of experimental and computational evidencei"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, 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 THR-359 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Manual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, 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 THR-359 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, 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-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Manual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiP by autocatalysisManual assertion inferred from combination of experimental and computational evidencei"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.", , , , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."A quantitative atlas of mitotic phosphorylation.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Large-scale proteomics analysis of the human kinome.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, 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-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]."Toward a comprehensive characterization of a human cancer cell phosphoproteome.", , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, 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-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].Manual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Modified residueiPhosphothreonineManual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Modified residueiPhosphoserineManual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.1Post-translational modificationiActivated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.Manual assertion based on experiment ini"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.", , , ,
[] [] []Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.N-terminal myristoylation results in an activated kinase in the absence of added growth factors.Keywords - PTMiProteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEi2D gel databasesUCD-2DPAGEiPTM databasesiPTMnetiPhosphoSitePlusiExpressioniGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSOrganism-specific databasesHPAiInteractioniSubunit structureiForms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation. Interacts with ETV1/ER81 and FGFR1.Manual assertion based on experiment ini"Regulation of the ETS transcription factor ER81 by the 90-kDa ribosomal S6 kinase 1 and protein kinase A.",
[] [] []Cited for: FUNCTION IN PHOSPHORYLATION OF ETV1/ER81, INTERACTION WITH ETV1/ER81."Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.", ,
[] [] []Cited for: INTERACTION WITH MAPK1 OR MAPK3."90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling.", , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH FGFR1, ENZYME REGULATION, SUBCELLULAR LOCATION."Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase.", , , ,
[] [] []Cited for: FUNCTION IN MTOR SIGNALING, INTERACTION WITH TSC2."Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors.", , , , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF
IN COMPLEX WITH INHIBITOR.Binary interactionsiProtein-protein interaction databasesBioGridi, 76 interactorsDIPiELMiIntActi, 33 interactorsMINTiSTRINGiChemistry databasesBindingDBiStructureiSecondary structure1735Legend: HelixTurnBeta strandPDB Structure known for this areaFeature keyPosition(s)DescriptionActionsGraphical viewLengthHelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei10Beta strandiManual assertion inferred from combination of experimental and computational evidencei8Beta strandiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei7Beta strandiManual assertion inferred from combination of experimental and computational evidencei6HelixiManual assertion inferred from combination of experimental and computational evidencei8HelixiManual assertion inferred from combination of experimental and computational evidencei20HelixiManual 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 evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual 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 evidencei17HelixiManual assertion inferred from combination of experimental and computational evidencei10HelixiManual assertion inferred from combination of experimental and computational evidencei10TurniManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei5HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei10Beta strandiManual assertion inferred from combination of experimental and computational evidencei8TurniManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual assertion inferred from combination of experimental and computational evidencei9TurniManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei10Beta strandiManual assertion inferred from combination of experimental and computational evidencei6Beta strandiManual assertion inferred from combination of experimental and computational evidencei9HelixiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei20HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei7HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual 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 evidencei27HelixiManual assertion inferred from combination of experimental and computational evidencei10HelixiManual 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 evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei6HelixiManual assertion inferred from combination of experimental and computational evidencei4HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei16HelixiManual assertion inferred from combination of experimental and computational evidencei3HelixiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual assertion inferred from combination of experimental and computational evidencei33D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.40A/B[]X-ray2.00A[]X-ray2.00A[]X-ray2.10A[]X-ray2.70A/B[]X-ray2.40B[]X-ray2.30B/E[]X-ray2.15A/D[]X-ray2.40C[]X-ray2.13C[]X-ray2.70C[]X-ray2.95C[]X-ray2.30C[]X-ray2.30C[]X-ray2.95C[]X-ray2.20I[]X-ray1.90I[]ProteinModelPortaliSMRiModBaseiMobiDBiMiscellaneous databasesEvolutionaryTraceiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDomainiProtein kinase 1Manual assertion according to rulesi 260DomainiAGC-kinase C-terminal 70DomainiProtein kinase 2Manual assertion according to rulesi 258Sequence similaritiesiBelongs to the . . .Keywords - DomainiPhylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiFamily and domain databasesInterProi AGC-kinase_C Kinase-like_dom_sf Pkinase_C Prot_kinase_dom Protein_kinase_ATP_BS Ribosomal_S6_kinase_II Ser/Thr_kinase_ASPfami Pkinase, 2 hits Pkinase_C, 1 hitPIRSFi Ribsml_S6_kin_2, 1 hitSMARTi S_TK_X, 1 hit S_TKc, 2 hitsSUPFAMi SSF56112, 2 hitsPROSITEi AGC_KINASE_CTER, 1 hit PROTEIN_KINASE_ATP, 2 hits PROTEIN_KINASE_DOM, 2 hits PROTEIN_KINASE_ST, 2 hitsSequences (4)iSequence statusi: Complete.This entry describes 4 isoformsi produced by alternative splicing.
(identifier: Q15418-1)
[]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.
50MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV
100KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT
150LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF
200TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH
250IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV
300LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN
350PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY
400FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL
450HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID
500KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK
550ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP
600ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL
650GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD
700LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA
730 TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL
73582,723April 16, 2002 - v2Checksum:i2A53DFBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutter (identifier: Q15418-2)
[]The sequence of this isoform differs from the canonical sequence as follows:
: MPLAQLKEPW...GEEAGLQPSK → MEQDPKPPRL...GPGSGPQRDS74483,932Checksum:iEBDBBFBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutter (identifier: Q15418-3)
[]The sequence of this isoform differs from the canonical sequence as follows:
: Missing.Note: No experimental confirmation available.64372,698Checksum:iB8362021FCCC17B5BLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutter (identifier: Q15418-4)
[]The sequence of this isoform differs from the canonical sequence as follows:
: MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPS → MQTPADFPRVERDLVPCPR71981,147Checksum:iD47F7EC9609D5ACFBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterExperimental InfoFeature keyPosition(s)DescriptionActionsGraphical viewLengthSequence conflictiA → T in
(PubMed:).1Sequence conflictiS → G in
(PubMed:).1Natural variantFeature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_021864Manual assertion based on experiment ini"Human rsk isoforms: cloning and characterization of tissue-specific expression.", , , , Am. J. Physiol. 266:C351-C359(1994)
[] [] []Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-335."Patterns of somatic mutation in human cancer genomes.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-335.Corresponds to variant .1Alternative sequenceFeature keyPosition(s)DescriptionActionsGraphical viewLengthAlternative sequenceiVSP_041580Missing
in isoform . Manual assertion based on opinion ini"Complete sequencing and characterization of 21,243 full-length human cDNAs.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). 92Alternative sequenceiVSP_041380MPLAQ…LQPSK → MEQDPKPPRLRLWALIPWLP RKQRPRISQTSLPVPGPGSG PQRDS in isoform . Manual assertion based on opinion ini"Complete sequencing and characterization of 21,243 full-length human cDNAs.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). 36Alternative sequenceiVSP_057469MPLAQ…GLQPS → MQTPADFPRVERDLVPCPR in isoform .
35Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
Genomic DNA Translation:
Genomic DNA No translation available. Genomic DNA Translation:
mRNA Translation: CCDSi [] [] []PIRiRefSeqi,
[]UniGeneiGenome annotation databasesEnsembli; ;
[]GeneIDiKEGGiUCSCi human [] humanKeywords - Coding sequence diversityi, Similar proteinsi735735Q15418-3744744744643843Q15418-4594719719719735735876112112Q15418-3744750744744744740740740740740Q15418-3784841808880883 mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
Genomic DNA Translation:
Genomic DNA No translation available. Genomic DNA Translation:
mRNA Translation: CCDSi [] [] []PIRiRefSeqi,
[]UniGenei3D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.40A/B[]X-ray2.00A[]X-ray2.00A[]X-ray2.10A[]X-ray2.70A/B[]X-ray2.40B[]X-ray2.30B/E[]X-ray2.15A/D[]X-ray2.40C[]X-ray2.13C[]X-ray2.70C[]X-ray2.95C[]X-ray2.30C[]X-ray2.30C[]X-ray2.95C[]X-ray2.20I[]X-ray1.90I[]ProteinModelPortaliSMRiModBaseiMobiDBiProtein-protein interaction databasesBioGridi, 76 interactorsDIPiELMiIntActi, 33 interactorsMINTiSTRINGiChemistry databasesBindingDBiChEMBLiDrugBanki Purvalanol AGuidetoPHARMACOLOGYiPTM databasesiPTMnetiPhosphoSitePlusiPolymorphism and mutation databasesBioMutaiDMDMi2D gel databasesUCD-2DPAGEiProteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEiProtocols and materials databasesDNASUiStructural Biology KnowledgebaseGenome annotation databasesEnsembli; ;
[]GeneIDiKEGGiUCSCi human [] humanOrganism-specific databasesCTDiDisGeNETiEuPathDBiGeneCardsiHGNCi RPS6KA1HPAiMIMi geneneXtProtiOpenTargetsiPharmGKBiGenAtlasiPhylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiEnzyme and pathway databasesBRENDAi 2681Reactomei ERK/MAPK targets CREB phosphorylation Senescence-Associated Secretory Phenotype (SASP) Recycling pathway of L1 CREB phosphorylation through the activation of Ras RSK activation Gastrin-CREB signalling pathway via PKC and MAPKSABIO-RKiSignaLinkiSIGNORiMiscellaneous databasesChiTaRSi humanEvolutionaryTraceiGeneWikiiGenomeRNAiiPROiSOURCEiGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSFamily and domain databasesInterProi AGC-kinase_C Kinase-like_dom_sf Pkinase_C Prot_kinase_dom Protein_kinase_ATP_BS Ribosomal_S6_kinase_II Ser/Thr_kinase_ASPfami Pkinase, 2 hits Pkinase_C, 1 hitPIRSFi Ribsml_S6_kin_2, 1 hitSMARTi S_TK_X, 1 hit S_TKc, 2 hitsSUPFAMi SSF56112, 2 hitsPROSITEi AGC_KINASE_CTER, 1 hit PROTEIN_KINASE_ATP, 2 hits PROTEIN_KINASE_DOM, 2 hits PROTEIN_KINASE_ST, 2 hitsProtoNeti Q9BQK2Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998Last sequence update: April 16, 2002Last modified: May 23, 2018This is version 197 of the entry and version 2 of the sequence. Entry statusiReviewed (UniProtKB/Swiss-Prot)Annotation programDisclaimerAny 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.MiscellaneousiKeywords - Technical termi, , DocumentsHuman chromosome 1: entries, gene names and cross-references to MIMList of human entries with polymorphisms or disease mutationsIndex of human polymorphisms and disease mutationsOnline Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-ProtIndex of Protein Data Bank (PDB) cross-referencesHuman and mouse protein kinases: classification and indexIndex of protein domains and familiesWe'd like to inform you that we have updated our
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