在2.4GHz频段无线速率最高可达300Mbps，在5GHz频段采用全新一代11AC技术，
通过提升频宽，提高频率调制效率，无线速率最高可达867Mbps，可以轻松支持高清（1080P）电影
播放、在线视频、3D游戏等高网速应用。
注：TL-WDR6300可向下兼容11a、11n技术，可以兼容市面上主流的2.4GHz和5GHz设备，以及集成11ac无线网卡的新Wi-Fi设备，如MacBook、iPhone 6、iPhone 6 Plus、三星Galaxy S6等。
TL-WDR6300外置2根2.4GHz单频天线和2根5GHz单频天线，通过更为科学的整体布局，在有限的壳体空间内，使同频
天线之间获得更大的隔离度，有效降低同频干扰，获得更优异的传输性能。同时，通过精密和专业的天线内部结构设计，
可获得更高的天线增益，无线信号更强，覆盖更广。
不合理的天线布局
科学合理的天线布局
好路由、好宽带，要配好网线
无论交换机和路由器的性能多好、宽带线路速率多高，一旦布线质量不过关，整个网络性能
都会功亏一篑。市面充斥了大量品质低下、以次充好的布线产品，普通消费者很难辨别。
TP-LINK综合布线企业标准，全面高于国际标准和国家标准，品质值得信赖。
*京东、淘宝、官方商城、线下经销商均有售
点击查看TP-LINK综合布线全系列产品
＊ 以上介绍所引用数据为产品在特定设备特定实验环境下的表现，基于现场实际环境或设备的不同可能会有所差异，提及的技术对比均为科学原理解释，不涉及其他目的。
IEEE802.11ac
IEEE802.11n
IEEE802.11g
IEEE802.11b
IEEE802.11a
IEEE802.3u
2.4GHz频段：300Mbps
5GHz频段：867Mbps
4个10/100M自适应LAN口，支持自动翻转（Auto MDI/MDIX）
1个10/100M自适应WAN口，支持自动翻转（Auto MDI/MDIX）
4根外置不可拆卸全向天线
230mm*144mm*37mm
信号强度调节
AC1200双频无线路由器 TL-WDR6300
电源适配器
工作温度：0℃~40℃
存储温度：-40℃~70℃
工作湿度：10%~90%不凝结
存储湿度：5%~90%不凝结加载中，请稍后...
TP-LINK TL-WDR5600Sina Visitor System纤薄身板，大显不凡
科技产品，不是用于炫耀复杂的技术本身，而是用于简化生活，从而享受生活。
TP-LINK打破常规，用高性能的板阵天线系统，取代林立的天线。
从而将不凡的无线性能，隐藏于纤薄简约的外型之下。
一体化阵列天线系统
解决信号难题更简单
TP-LINK一体化板阵天线系统，集优质单元天线、科学天线组合、信号净噪技术
和高效调度算法于一身，不仅经过实验室严格科学测试，更在大量复杂环境下
实地调校，让用户无论身处何种应用场景，都能体验优质的Wi-Fi信号。
了解阵列天线
双频，双倍的酣畅淋漓
TP-LINK小黑板2.4GHz、5GHz双频并发，无线速率高达1167Mbps。
其中，5GHz频段采用新一代11AC技术，无线速率高达867Mbps，
双倍于普通单频路由的无线速率，带来双倍的高速无线体验。
双频同时工作，互不干扰，可接入的终端
设备数量，也是普通单频路由的两倍。
家里的每一台手机、Pad、电脑都可以轻
松享受高清电影、在线视频、3D游戏等高
网速应用。
支持访客网络
家庭网络安全有保障
支持访客网络，将主人网络和客人网络分离，既方便客
人来访的时候上网，也保障家庭网络安全。
网速控制、上网时间控制等多样功能
提供设备管理功能，可对连接到路由器的每一台设备的上网速度进行控制，
避免个别用户使用BT、迅雷等软件占用过多带宽。同时能够设置允许上网时间段，
有效管理设备的上网时间，更加方便家长对于孩子上网时间进行管控。
手机APP，管理随时随地
通过TP-LINK手机APP，轻松掌控家中网络和设备，状态
一目了然，在线升级、远程管理以及安装体验新版路由应
用等。路由管理，随时随地。
一体化阵列天线系统，信号难题一扫而空
TP-LINK一体化阵列天线系统，科学设计，创新方阵、环阵、翼阵、板阵四种不同阵列，同时满足高规格性
能和艺术造型两方面需求。不仅经过实验室严格科学测试，更在大量复杂环境下实地调校，让用户无论身处
何种应用场景，都能体验优质的Wi-Fi信号。
每一根天线，都对信号至关重要
阵列是单元的科学组合，优秀的单元是强大阵列必不可
少的基础。TP-LINK一体化阵列天线系统，采用拥有原创
专利的优质单元天线，每一根单元天线，在各自工作频
段（2.4G、5G Band1、5G Band4），无论是增益还是方
向性都表现出色。
阵列，不是简单随意的摆放
TP-LINK一体化阵列天线系统，由多个单元天线组合而成，每一根天线的空间位置、指向角度
、距离关系、排列顺序，都严格遵循科学原理。不但通过实验室严格测试，更在大量复杂环
境下实地调校，由上万种不同可能组合中，优选最佳阵列，绝不是找个空闲位置随意摆放那
样简单。以科学的组合避免天线之间的相互内耗，释放阵列天线的威力。
去除和隔离信号中噪音
强劲、灵敏、高效
无论是用于发射的功率放大器（PA），还是用于接收的低噪音放大器（LNA），在放
大信号的同时也会放大噪音，对无线性能来说是一把双刃剑。TP-LINK一体化阵列天
线系统，除精心调校每一路PA和LNA之外，额外引入一般通信基站设备才会使用的高
级介质滤波器，使信号在进入放大电路前去除噪音。天线间隔离条的使用阻断了不同
天线信号间的相互干扰，使信号更加纯净。
调度算法，一体化天线系统的灵魂
发达的四肢，需要聪明的大脑来指挥才能发挥威力，TP-LINK一体化阵列天线系
统的灵魂，正是其调度算法。升级版TP-LINK天线系统控制软件，着力于调度
算法的效率优化。就好比超级都市的交通指挥控制中心一样，高效的调度指挥，
往往比宽阔的道路更为重要。
好路由、好宽带，要配好网线
无论交换机和路由器的性能多好、宽带线路速率多高，一旦布线质量不过关，整个网络性能
都会功亏一篑。市面充斥了大量品质低下、以次充好的布线产品，普通消费者很难辨别。
TP-LINK综合布线企业标准，全面高于国际标准和国家标准，品质值得信赖。
*京东、淘宝、官方商城、线下经销商均有售
点击查看TP-LINK综合布线全系列产品
＊ 以上介绍所引用数据为产品在特定设备特定实验环境下的表现，基于现场实际环境或设备的不同可能会有所差异，提及的技术对比均为科学原理解释，不涉及其他目的。
IEEE802.11ac
IEEE802.11n
IEEE802.11g
IEEE802.11b
IEEE802.11a
IEEE802.3u
2.4GHz频段：300Mbps
5GHz频段：867Mbps
4个10/100M自适应LAN口，支持自动翻转（Auto MDI/MDIX）
1个10/100M自适应WAN口，支持自动翻转（Auto MDI/MDIX）
内置两根双频天线
267mm*147mm*50mm
信号强度调节
AC1200双频无线路由器 TL-WDR5630
电源适配器
工作温度：0℃~40℃
存储温度：-40℃~70℃
工作湿度：10%~90%不凝结
存储湿度：5%~90%不凝结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 .
From June 20, 2018 all traffic will be automatically redirected to HTTPS.
Serine/threonine-protein kinase RIO1RIOK1Homo sapiens (Human)-Annotation score: -Experimental evidence at protein leveliFunctioniInvolved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor (PubMed:). The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit (By similarity). Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity). The catalytic activity regulates its dynamic association with the 40S subunit (By similarity). In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation (PubMed:).Manual assertion inferred from sequence similarity toiManual assertion based on experiment ini"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.", , , , , ,
[] [] []Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRMT5 AND NCL, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77 AND RIOK1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION."The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-324.Catalytic activityiATP + a protein = ADP + a phosphoprotein.Manual assertion based on experiment ini"The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-324.CofactoriManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.SitesFeature keyPosition(s)DescriptionActionsGraphical viewLengthBinding siteiATPManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1Binding siteiATP; via carbonyl oxygenManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1Binding siteiATP; via amide nitrogenManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1Active siteiProton acceptorManual assertion inferred by curator fromi"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.Manual assertion based on experiment ini"The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-324.1Metal bindingiMagnesiumManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1Active sitei4-aspartylphosphate intermediateManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1Metal bindingiMagnesiumManual assertion inferred from combination of experimental and computational evidenceiManual assertion based on experiment ini"Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes.", , , ,
[] [] []Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF
IN COMPLEX WITH ADP, COFACTOR.1GO - Molecular functioniGO - Biological processiInferred from mutant phenotypeiInferred from mutant phenotypeiInferred from mutant phenotypeiKeywordsiMolecular function, , , Biological processLigand, , , Enzyme and pathway databasesReactomei Major pathway of rRNA processing in the nucleolus and cytosolNames & TaxonomyiProtein namesiRecommended name:Serine/threonine-protein kinase RIO1 (EC:Manual assertion based on experiment ini"The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-324., EC:)Alternative name(s):RIO kinase 1Gene namesiName:Manual assertion inferred from database entriesiSynonyms:RIO1OrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 6 Organism-specific databasesEuPathDBiHGNCi RIOK1MIMi geneneXtProtiSubcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: "RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.", , , , , ,
[] [] []Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRMT5 AND NCL, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77 AND RIOK1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.Keywords - Cellular componentiPathology & BiotechiMutagenesisOrganism-specific databasesDisGeNETiOpenTargetsiPharmGKBiChemistry databasesChEMBLiGuidetoPHARMACOLOGYiPolymorphism and mutation databasesBioMutaiDMDMiPTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthChainiPRO_Serine/threonine-protein kinase RIO1 568Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthModified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Modified residueiPhosphoserineManual assertion inferred from combination of experimental and computational evidencei"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.", , , , , , ,
[] [] []Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-22, 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-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].1Keywords - PTMiProteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEiProteomicsDBiPTM databasesiPTMnetiPhosphoSitePlusiExpressioniGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSOrganism-specific databasesHPAiInteractioniSubunit structureiAssociates with the precursor of the 40S ribosome subunit. Interacts (via its N-terminus) with PRMT5 (via its N-terminus) (PubMed:, PubMed:). Interacts with WDR77 (PubMed:). Found in a PRMT5 complex composed of PRMT5, WDR77 and RIOK1 (PubMed:). Interacts (via its C-terminus) with NCL; this interaction targets NCL for PRTM5 methylation (PubMed:).Manual assertion based on experiment ini"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.", , , , , ,
[] [] []Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PRMT5 AND NCL, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77 AND RIOK1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION."The kinase activity of human Rio1 is required for final steps of cytoplasmic maturation of 40S subunits.", , , , , ,
[] [] []Cited for: FUNCTION, INTERACTION WITH PRMT5 AND WDR77, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-324.Binary interactionsiWithEntry#Exp.IntActNotesPRMT54Protein-protein interaction databasesBioGridi, 55 interactorsIntActi, 11 interactorsMINTiSTRINGiChemistry databasesBindingDBiStructureiSecondary structure1568Legend: HelixTurnBeta strandPDB Structure known for this areaFeature keyPosition(s)DescriptionActionsGraphical viewLengthHelixiManual 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 evidencei9Beta strandiManual assertion inferred from combination of experimental and computational evidencei7HelixiManual assertion inferred from combination of experimental and computational evidencei14Beta strandiManual assertion inferred from combination of experimental and computational evidencei5Beta strandiManual 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 evidencei20HelixiManual assertion inferred from combination of experimental and computational evidencei3Beta strandiManual assertion inferred from combination of experimental and computational evidencei4Beta strandiManual 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 evidencei9HelixiManual assertion inferred from combination of experimental and computational evidencei14HelixiManual assertion inferred from combination of experimental and computational evidencei183D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.70A[]ProteinModelPortaliSMRiModBaseiMobiDBiFamily & DomainsiDomains and RepeatsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDomainiProtein kinase 300Sequence similaritiesiBelongs to the . .Phylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOGENOMiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiFamily and domain databasesInterProi Kinase-like_dom_sf RIO_kinase RIO_kinase_CS Ser/Thr_kinase_Rio1PIRSFi Ser/Thr_PK_RIO1, 1 hitSMARTi RIO, 1 hitSUPFAMi SSF56112, 1 hitPROSITEi RIO1, 1 hitSequenceiSequence statusi: Complete.Q9BRS2-1 []
50MDYRRLLMSR VVPGQFDDAD SSDSENRDLK TVKEKDDILF EDLQDNVNEN
100GEGEIEDEEE EGYDDDDDDW DWDEGVGKLA KGYVWNGGSN PQANRQTSDS
150SSAKMSTPAD KVLRKFENKI NLDKLNVTDS VINKVTEKSR QKEADMYRIK
200DKADRATVEQ VLDPRTRMIL FKMLTRGIIT EINGCISTGK EANVYHASTA
250NGESRAIKIY KTSILVFKDR DKYVSGEFRF RHGYCKGNPR KMVKTWAEKE
300MRNLIRLNTA EIPCPEPIML RSHVLVMSFI GKDDMPAPLL KNVQLSESKA
350RELYLQVIQY MRRMYQDARL VHADLSEFNM LYHGGGVYII DVSQSVEHDH
400PHALEFLRKD CANVNDFFMR HSVAVMTVRE LFEFVTDPSI THENMDAYLS
450KAMEIASQRT KEERSSQDHV DEEVFKRAYI PRTLNEVKNY ERDMDIIMKL
500KEEDMAMNAQ QDNILYQTVT GLKKDLSGVQ KVPALLENQV EERTCSDSED
550IGSSECSDTD SEEQGDHARP KKHTTDPDID KKERKKMVKE AQREKRKNKI
560 PKHVKKRKEK TAKTKKGK
56865,583March 1, 2004 - v2Checksum:i5730BFCBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterNatural variantFeature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_061777. Corresponds to variant .1Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi mRNA Translation:
mRNA Translation:
Genomic DNA Translation:
mRNA Translation:
mRNA Translation: CCDSiRefSeqi, UniGeneiGenome annotation databasesEnsembli; ; GeneIDiKEGGiUCSCi humanKeywords - Coding sequence diversityiSimilar proteinsi674574571571571674574571571571 mRNA Translation:
mRNA Translation:
Genomic DNA Translation:
mRNA Translation:
mRNA Translation: CCDSiRefSeqi, UniGenei3D structure databasesSelect the link destinations:PDBeiRCSB PDBiPDBjiPDB entryMethodResolution (?)ChainPositionsPDBsumX-ray2.70A[]ProteinModelPortaliSMRiModBaseiMobiDBiProtein-protein interaction databasesBioGridi, 55 interactorsIntActi, 11 interactorsMINTiSTRINGiChemistry databasesBindingDBiChEMBLiGuidetoPHARMACOLOGYiPTM databasesiPTMnetiPhosphoSitePlusiPolymorphism and mutation databasesBioMutaiDMDMiProteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEiProteomicsDBiProtocols and materials databasesDNASUiStructural Biology KnowledgebaseGenome annotation databasesEnsembli; ; GeneIDiKEGGiUCSCi humanOrganism-specific databasesCTDiDisGeNETiEuPathDBiGeneCardsiHGNCi RIOK1HPAiMIMi geneneXtProtiOpenTargetsiPharmGKBiGenAtlasiPhylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOGENOMiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiEnzyme and pathway databasesReactomei Major pathway of rRNA processing in the nucleolus and cytosolMiscellaneous databasesChiTaRSi humanGenomeRNAiiPROiSOURCEiGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSFamily and domain databasesInterProi Kinase-like_dom_sf RIO_kinase RIO_kinase_CS Ser/Thr_kinase_Rio1PIRSFi Ser/Thr_PK_RIO1, 1 hitSMARTi RIO, 1 hitSUPFAMi SSF56112, 1 hitPROSITEi RIO1, 1 hitProtoNetiMiscellaneousiKeywords - Technical termi, , , DocumentsHuman chromosome 6: 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
with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.