| Tag | Content |
|---|
| EKPD ID | EKS-RAN-00152 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| AGC/RSK | 368.1 | 3.7E-110 | 91 | 352 | 262 |
|
| Status | Reviewed |
| Ensembl Protein | ENSRNOP00000005226 |
| UniProt Accession | P67999; P21425; |
| Protein Name | Ribosomal 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; p70 ribosomal S6 kinase alpha; p70 S6 kinase alpha; p70 S6K-alpha; p70 S6KA; |
| Gene Name | Rps6kb1 |
| Gene Synonyms/Alias | Rps6kb1; |
| Ensembl Information | |
| Organism | Rattus norvegicus |
| Functional Description | Serine/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 RMP leading to dissociation of a RMP: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 (By similarity). |
| Protein Length | 525 |
Protein Sequence
(FASTA) | | MRRRRRRDGF YPAPDFRHRE 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 SPRTPVSPVK FSPGDFWGRG ASASTANPQT PVEYPMETSG 480 | | IEQMDVTTSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL 525 |
|
Nucleotide Sequence
(FASTA) | | ATGAGGCGAC GACGGAGGCG GGACGGCTTT TACCCAGCGC CTGACTTCCG ACACAGGGAA 60 | | GCTGAGGACA TGGCAGGAGT GTTTGACATA GACCTGGACC AGCCAGAGGA TGCAGGCTCT 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 GAAGATATTT 360 | | GCCATGAAGG TGCTTAAAAA GGCAATGATA GTAAGAAATG CTAAAGATAC AGCTCATACA 420 | | AAAGCAGAGC GGAATATTCT GGAGGAAGTA AAGCATCCCT TCATTGTGGA TTTAATTTAT 480 | | GCCTTTCAGA CCGGTGGAAA ACTCTACCTC ATCCTTGAGT ATCTCAGTGG AGGAGAACTA 540 | | TTTATGCAGT TAGAAAGAGA GGGGATATTC ATGGAAGATA CAGCTTGCTT TTACTTGGCT 600 | | GAAATCTCCA TGGCTTTGGG GCATTTACAT CAAAAAGGGA TCATCTACAG AGACCTGAAG 660 | | CCGGAGAACA TCATGCTTAA TCACCAAGGT CACGTGAAGC TGACAGACTT TGGACTATGC 720 | | AAAGAATCTA TTCATGATGG AACAGTCACG CACACATTTT GTGGAACAAT AGAATACATG 780 | | GCCCCTGAAA TCTTGATGAG AAGCGGCCAC AACCGTGCTG TGGATTGGTG GAGTTTGGGA 840 | | GCATTAATGT ATGACATGCT GACTGGAGCA CCTCCATTCA CTGGGGAGAA TAGAAAGAAA 900 | | ACAATTGACA AAATCCTCAA ATGTAAACTT AATTTGCCTC CCTACCTCAC ACAAGAAGCT 960 | | CGAGATCTGC TTAAAAAGCT GCTGAAAAGA AATGCTGCTT CTCGTCTTGG AGCTGGCCCT 1020 | | GGGGATGCTG GAGAAGTCCA AGCGCATCCA TTTTTTAGAC ACATTAACTG GGAAGAGCTT 1080 | | TTGGCTCGGA AGGTGGAGCC CCCCTTTAAG CCTCTGTTGC AATCTGAAGA GGATGTGAGT 1140 | | CAGTTTGATT CAAAGTTTAC TCGTCAGACA CCTGTTGACA GCCCCGATGA CTCAACTCTC 1200 | | AGTGAAAGTG CCAACCAGGT CTTTCTGGGT TTTACATATG TGGCTCCATC TGTACTTGAA 1260 | | AGTGTGAAAG AAAAGTTTTC TTTTGAACCA AAAATCCGAT CGCCTCGAAG ATTTATTGGT 1320 | | AGCCCACGAA CGCCTGTCAG CCCAGTCAAA TTCTCTCCTG GGGATTTCTG GGGACGAGGT 1380 | | GCTTCAGCCA GCACAGCAAA TCCTCAGACA CCTGTGGAAT ACCCAATGGA AACAAGTGGA 1440 | | ATAGAGCAGA TGGATGTGAC AACGAGCGGG GAAGCTTCAG CGCCACTTCC AATCCGACAG 1500 | | CCCAACTCTG GGCCATACAA AAAACAAGCT TTTCCTATGA TCTCCAAACG GCCAGAGCAC 1560 | | CTGCGTATGA ATCTATGA 1578 |
|
| 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 |
|
| Keyword | Acetylation; Alternative initiation; Apoptosis; ATP-binding; Cell cycle; Cell junction; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase; Translation regulation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
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| Pfam | |
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| Prints | |
| Created Date | 20-Feb-2013 |