EKS-HOS-00160
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00160
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
AGC/RSK368.61.0E-10991352262
StatusReviewed
Ensembl ProteinENSP00000384335
UniProt AccessionP23443;
Protein NameRibosomal protein S6 kinase beta-1
Protein Synonyms/Alias S6K-beta-1; S6K1; 70 kDa ribosomal protein S6 kinase 1; P70S6K1; p70-S6K 1; Ribosomal protein S6 kinase I; Serine/threonine-protein kinase 14A; p70 ribosomal S6 kinase alpha; p70 S6 kinase alpha; p70 S6K-alpha; p70 S6KA;
Gene NameRPS6KB1
Gene Synonyms/Alias RPS6KB1; STK14A;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000108443ENSP00000225577ENST00000225577
ENSG00000108443ENSP00000464805ENST00000592726
ENSG00000108443ENSP00000384335ENST00000406116
ENSG00000108443ENSP00000441993ENST00000443572
ENSG00000108443ENSP00000468058ENST00000472940
ENSG00000108443ENSP00000466562ENST00000489824
ENSG00000108443ENSP00000376744ENST00000393021
OrganismHomo sapiens
Functional DescriptionSerine/threonine-protein kinase that acts downstream ofmTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the preinitiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at 'Thr-412', which is proposed to be a negative feedback mechanism for the RPS6KB1 anti- apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1- 2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin.
Protein Length451
Protein Sequence
(FASTA)
MRRRRRRDGF YPAPDFRDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG 60
PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF 120
AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL 180
FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC 240
KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK 300
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL 360
LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE 420
SVKEKFSFEP KIRSPRRFIG SPRTPVSTAM C 451
Nucleotide Sequence
(FASTA)
ATGAGGCGAC GAAGGAGGCG GGACGGCTTT TACCCAGCCC CGGACTTCCG AGACAGGGAA 60
GCTGAGGACA TGGCAGGAGT GTTTGACATA GACCTGGACC AGCCAGAGGA CGCGGGCTCT 120
GAGGATGAGC TGGAGGAGGG GGGTCAGTTA AATGAAAGCA TGGACCATGG GGGAGTTGGA 180
CCATATGAAC TTGGCATGGA ACATTGTGAG AAATTTGAAA TCTCAGAAAC TAGTGTGAAC 240
AGAGGGCCAG AAAAAATCAG ACCAGAATGT TTTGAGCTAC TTCGGGTACT TGGTAAAGGG 300
GGCTATGGAA AGGTTTTTCA AGTACGAAAA GTAACAGGAG CAAATACTGG GAAAATATTT 360
GCCATGAAGG TGCTTAAAAA GGCAATGATA GTAAGAAATG CTAAAGATAC AGCTCATACA 420
AAAGCAGAAC GGAATATTCT GGAGGAAGTA AAGCATCCCT TCATCGTGGA TTTAATTTAT 480
GCCTTTCAGA CTGGTGGAAA ACTCTACCTC ATCCTTGAGT ATCTCAGTGG AGGAGAACTA 540
TTTATGCAGT TAGAAAGAGA GGGAATATTT ATGGAAGACA CTGCCTGCTT TTACTTGGCA 600
GAAATCTCCA TGGCTTTGGG GCATTTACAT CAAAAGGGGA TCATCTACAG AGACCTGAAG 660
CCGGAGAATA TCATGCTTAA TCACCAAGGT CATGTGAAAC TAACAGACTT TGGACTATGC 720
AAAGAATCTA TTCATGATGG AACAGTCACA CACACATTTT GTGGAACAAT AGAATACATG 780
GCCCCTGAAA TCTTGATGAG AAGTGGCCAC AATCGTGCTG TGGATTGGTG GAGTTTGGGA 840
GCATTAATGT ATGACATGCT GACTGGAGCA CCCCCATTCA CTGGGGAGAA TAGAAAGAAA 900
ACAATTGACA AAATCCTCAA ATGTAAACTC AATTTGCCTC CCTACCTCAC ACAAGAAGCC 960
AGAGATCTGC TTAAAAAGCT GCTGAAAAGA AATGCTGCTT CTCGTCTGGG AGCTGGTCCT 1020
GGGGACGCTG GAGAAGTTCA AGCTCATCCA TTCTTTAGAC ACATTAACTG GGAAGAACTT 1080
CTGGCTCGAA AGGTGGAGCC CCCCTTTAAA CCTCTGTTGC AATCTGAAGA GGATGTAAGT 1140
CAGTTTGATT CCAAGTTTAC ACGTCAGACA CCTGTCGACA GCCCAGATGA CTCAACTCTC 1200
AGTGAAAGTG CCAATCAGGT CTTTCTGGGT TTTACATATG TGGCTCCATC TGTACTTGAA 1260
AGTGTGAAAG AAAAGTTTTC CTTTGAACCA AAAATCCGAT CACCTCGAAG ATTTATTGGC 1320
AGCCCACGAA CACCTGTCAG TACTGCTATG TGCTAA 1356
Domain Profile
S: 1     fellkvlgkGaygkvflvrkvekkdtgklyavKvlkkaelvk..kkkertkeereiLeev  58
         fell+vlgkG+ygkvf+vrkv++ +tgk++a+Kvlkka +v+  k++++tk+er+iLeev
Q: 91    FELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRnaKDTAHTKAERNILEEV  150
         89***********************************9999999****************
S: 59    ehpfivklheafqdekklylvlellkGgeLlerlkkkklfseeeasfilaelvlaleylH  118
         +hpfiv+l +afq+  klyl+le+l+GgeL+++l+++++f+e++a+f+lae+++al +lH
Q: 151   KHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLH  210
         ************************************************************
S: 119   skgvvyrDLkpeNilldeeghvkltDfglakekiaeneekaysfcgTleyvaPevlkrkg  178
         +kg++yrDLkpeNi+l+++ghvkltDfgl+ke+i ++++ +++fcgT+ey+aPe+l+r+g
Q: 211   QKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESI-HDGTVTHTFCGTIEYMAPEILMRSG  269
         *********************************9.9999999******************
S: 179   ydeavDlwslGvllyemLtGktPftgeerketlarilkgkfslklpaweelseeakdlvk  238
         +++avD+wslG+l+y+mLtG++Pftge+rk+t+++ilk+k  l+lp +  l++ea+dl+k
Q: 270   HNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCK--LNLPPY--LTQEARDLLK  325
         ****************************************..9*****..**********
S: 239   klLkkdpakRlga...taeeikehkfl  262
         klLk++ a+Rlga   +a e+++h+f+
Q: 326   KLLKRNAASRLGAgpgDAGEVQAHPFF  352
         *************9*9*********97
Domain Sequence
(FASTA)
FELLRVLGKG GYGKVFQVRK VTGANTGKIF AMKVLKKAMI VRNAKDTAHT KAERNILEEV 60
KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL FMQLEREGIF MEDTACFYLA EISMALGHLH 120
QKGIIYRDLK PENIMLNHQG HVKLTDFGLC KESIHDGTVT HTFCGTIEYM APEILMRSGH 180
NRAVDWWSLG ALMYDMLTGA PPFTGENRKK TIDKILKCKL NLPPYLTQEA RDLLKKLLKR 240
NAASRLGAGP GDAGEVQAHP FF 262
Keyword3D-structure; Acetylation; Alternative initiation; Apoptosis; ATP-binding; Cell cycle; Cell junction; Complete proteome; Cytoplasm; Kinase; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase; Translation regulation.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Choloepus hoffmanni"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sorex araneus"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tursiops truncatus"; ?>Vicugna pacos"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>Schizosaccharomyces pombe"; ?>
EKS-AIM-00147
EKS-ANC-00148
EKS-BOT-00154
EKS-CAE-00124
EKS-CAJ-00159
EKS-CAF-00162
EKS-CAP-00155
EKS-CHH-00022
EKS-DAR-00441
EKS-DRM-00075
EKS-EQC-00153
EKS-FEC-00145
EKS-GAG-00132
EKS-GAA-00182
EKS-ICT-00151
EKS-LAC-00164
EKS-LOA-00154
EKS-MAM-00153
EKS-MEG-00122
EKS-MOD-00155
EKS-MUM-00159
EKS-MUP-00159
EKS-MYL-00163
EKS-NOL-00148
EKS-ORN-00191
EKS-ORA-00134
EKS-ORL-00179
EKS-OTG-00160
EKS-PAT-00145
EKS-PES-00137
EKS-POA-00151
EKS-RAN-00152
EKS-SAH-00149
EKS-SOA-00029
EKS-SUS-00135
EKS-TAG-00183
EKS-TAR-00200
EKS-TEN-00193
EKS-TUT-00147
EKS-VIP-00075
EKS-XET-00143
EKS-XIM-00186
EKS-SCP-00040
Gene Ontology
GO:0030054; C:cell junction
GO:0009986; C:cell surface
GO:0005737; C:cytoplasm
GO:0005829; C:cytosol
GO:0005741; C:mitochondrial outer membrane
GO:0005739; C:mitochondrion
GO:0043005; C:neuron projection
GO:0005634; C:nucleus
GO:0048471; C:perinuclear region of cytoplasm
GO:0045202; C:synapse
GO:0005524; F:ATP binding
GO:0042277; F:peptide binding
GO:0004672; F:protein kinase activity
GO:0004711; F:ribosomal protein S6 kinase activity
GO:0007568; P:aging
GO:0006915; P:apoptotic process
GO:0016477; P:cell migration
GO:0071363; P:cellular response to growth factor stimulus
GO:0000082; P:G1/S transition of mitotic cell cycle
GO:0007281; P:germ cell development
GO:0008286; P:insulin receptor signaling pathway
GO:0007616; P:long-term memory
GO:0043066; P:negative regulation of apoptotic process
GO:0046627; P:negative regulation of insulin receptor signaling pathway
GO:0048015; P:phosphatidylinositol-mediated signaling
GO:0045931; P:positive regulation of mitotic cell cycle
GO:0048633; P:positive regulation of skeletal muscle tissue growth
GO:0014911; P:positive regulation of smooth muscle cell migration
GO:0048661; P:positive regulation of smooth muscle cell proliferation
GO:0045948; P:positive regulation of translational initiation
GO:0043491; P:protein kinase B signaling cascade
GO:0046324; P:regulation of glucose import
GO:0042493; P:response to drug
GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation
GO:0045471; P:response to ethanol
GO:0033762; P:response to glucagon stimulus
GO:0051384; P:response to glucocorticoid stimulus
GO:0009749; P:response to glucose stimulus
GO:0009408; P:response to heat
GO:0043201; P:response to leucine
GO:0032496; P:response to lipopolysaccharide
GO:0009612; P:response to mechanical stimulus
GO:0007584; P:response to nutrient
GO:0033574; P:response to testosterone stimulus
GO:0009636; P:response to toxin
GO:0034612; P:response to tumor necrosis factor
GO:0009611; P:response to wounding
GO:0014732; P:skeletal muscle atrophy
GO:0003009; P:skeletal muscle contraction
GO:0031929; P:TOR signaling cascade
KEGG
hsa:6198;
InterPros
IPR000961; AGC-kinase_C.
IPR011009; Kinase-like_dom.
IPR017892; Pkinase_C.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR016238; Ribosomal_S6_kinase.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
SMARTs
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
Prosites
PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013