Protein:RPS6KB1 |
Protein Summary |
 Gene summary |
| Gene name: RPS6KB1 | ASpdb.0 ID: 6198 | Gene | Gene symbol | RPS6KB1 | Gene ID | 6198 |
| Gene name | ribosomal protein S6 kinase B1 |
| Synonyms | PS6K|S6K|S6K-beta-1|S6K1|STK14A|p70 S6KA|p70(S6K)-alpha|p70-S6K|p70-alpha |
| Cytomap | 17q23.1 |
| Type of gene | protein-coding |
| Description | ribosomal protein S6 kinase beta-1ribosomal protein S6 kinase Iribosomal protein S6 kinase, 70kDa, polypeptide 1serine/threonine kinase 14 alphaserine/threonine-protein kinase 14A |
| Modification date | 20240411 |
| UniProtAcc | P23443 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | RPS6KB1 | GO:0004672 | protein kinase activity | 17936702|18952604 |
| Gene | RPS6KB1 | GO:0004674 | protein serine/threonine kinase activity | 1922062|22017876 |
| Gene | RPS6KB1 | GO:0004712 | protein serine/threonine/tyrosine kinase activity | 22797923 |
| Gene | RPS6KB1 | GO:0005654 | nucleoplasm | - |
| Gene | RPS6KB1 | GO:0005739 | mitochondrion | 17936702 |
| Gene | RPS6KB1 | GO:0031667 | response to nutrient levels | 29750193 |
| Gene | RPS6KB1 | GO:0031670 | cellular response to nutrient | 22017876 |
| Gene | RPS6KB1 | GO:0031929 | TOR signaling | 12150926 |
| Gene | RPS6KB1 | GO:0045948 | positive regulation of translational initiation | 1922062 |
| Gene | RPS6KB1 | GO:0071363 | cellular response to growth factor stimulus | 17936702 |
| Gene | RPS6KB1 | GO:1904263 | positive regulation of TORC1 signaling | 22017876 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P23443-1 | P23443-1_4l46_A.pdb | 4L46 | X-ray | 3.01 | A | 80 | 417 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P23443 | RPS6KB1 | P23443-1 | P23443-2 | 525 | 502 | 1 | 23 | Deletion | none | none | 0 | 0 |
| P23443 | RPS6KB1 | P23443-1 | P23443-3 | 525 | 472 | 1 | 53 | Deletion | none | none | 0 | 0 |
| P23443 | RPS6KB1 | P23443-1 | P23443-4 | 525 | 451 | 448 | 525 | Substitution | PVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL | TAMC | 448 | 451 |
| P23443 | RPS6KB1 | P23443-1 | P23443-5 | 525 | 502 | 104 | 126 | Deletion | none | none | 103 | 103 |
| Multiple sequence alignment of our canonical and alternatively spliced RPS6KB1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of RPS6KB1 |
| UniProt-id | ENSG | ENST | ENSP |
| P23443-1 | ENSG00000108443.14 | ENST00000225577.9 | ENSP00000225577.4 |
| P23443-3 | ENSG00000108443.14 | ENST00000393021.7 | ENSP00000376744.3 |
| P23443-4 | ENSG00000108443.14 | ENST00000406116.7 | ENSP00000384335.3 |
| P23443-5 | ENSG00000108443.14 | ENST00000443572.6 | ENSP00000441993.1 |
| UniProt-id | NM ID | NP ID |
| P23443-1 | NM_003161.3 | NP_003152.1 |
| P23443-2 | NM_001272060.1 | NP_001258989.1 |
| P23443-3 | NM_001272044.1 | NP_001258973.1 |
| P23443-4 | NM_001272043.1 | NP_001258972.1 |
| P23443-5 | NM_001272042.1 | NP_001258971.1 |
| Amino acid sequences of our canonical and alternatively spliced RPS6KB1 |
| accession_id | Protein sequence |
| P23443-1 | MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC FELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGEL FMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGH NRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEEL LARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVK |
| P23443-2 | MAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTG ANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVE |
| P23443-3 | MDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAE RNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVK LTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDL LKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTY VAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNS |
| P23443-4 | MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC FELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGEL FMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGH NRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEEL LARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSTAM |
| P23443-5 | MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPEC FELLRVLGKGGYGKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEIS MALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPF TGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFD SKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVE |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| RPS6KB1 (go to UniProt):P23443 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P23443 | Domain | 91 | 352 | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 | Type=Deletion;Start=104;End=126 |
| P23443 | Region | 1 | 54 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=23 |
| P23443 | Region | 1 | 54 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=53 |
| P23443 | Region | 424 | 525 | Note=Autoinhibitory domain | Type=Substitution;Start=448;End=525 |
| P23443 | Motif | 28 | 32 | Note=TOS motif | Type=Deletion;Start=1;End=53 |
| P23443 | Compositional bias | 8 | 26 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=23 |
| P23443 | Compositional bias | 8 | 26 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=53 |
| P23443 | Compositional bias | 27 | 48 | Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=53 |
Gene Isoform Structures and Expression Levels for RPS6KB1 |
| Gene structures of our canonical and alternative spliced genes of RPS6KB1 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P23443-1 |
| 3D view using mol* of P23443-2 |
| 3D view using mol* of P23443-3 |
| 3D view using mol* of P23443-4 |
| 3D view using mol* of P23443-5 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P23443-1 |
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| pLDDT distribution across the protein length of P23443-2 |
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| pLDDT distribution across the protein length of P23443-3 |
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| pLDDT distribution across the protein length of P23443-4 |
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| pLDDT distribution across the protein length of P23443-5 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P23443-1 |
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| Ramachandran plot of P23443-2 |
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| Ramachandran plot of P23443-4 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P23443-1 | 1.031 | 305 | 1.062 | 1204.616 | 0.635 | 0.716 | 0.859 | 0.559 | 0.944 | 0.592 | 1.145 | 21,22,23,24,25,26,27,28,97,98,100,101,102,103,105, 121,123,125,130,136,139,140,143,147,156,172,173,17 4,175,177,178,179,180,181,182,183,184,185,186,188, 218,220,222,223,225,226,235,236,237,238,239,254,25 5,256,257,258,259,289,290,291,294,295,298,301,369, 380,381,382,383,385,386,517 |
| P23443-2 | 1.07 | 194 | 1.085 | 361.522 | 0.429 | 0.798 | 1.105 | 1.025 | 1.024 | 1.001 | 0.751 | 79,113,116,192,194,195,196,197,216,218,220,221,222 ,223,224,225,226,227,228,229,230,231,232,233,236,2 37,238,240,241,242,244,246,247,248,249,251,252,254 ,255 |
| P23443-3 | 1.066 | 233 | 1.037 | 632.149 | 0.467 | 0.797 | 0.999 | 0.766 | 1.17 | 0.655 | 1.198 | 44,45,46,47,48,49,50,51,52,68,70,72,77,83,86,87,90 ,94,103,119,120,121,122,125,126,128,129,165,167,16 8,169,170,172,182,183,184,185,186,203,206,232,328, 329,330,332,333,464,466,467,468,469,470,471 |
| P23443-4 | 1.04 | 460 | 1.063 | 1322.265 | 0.503 | 0.744 | 0.933 | 0.652 | 0.993 | 0.657 | 0.958 | 23,24,25,26,27,28,29,30,31,32,97,98,99,100,101,102 ,103,105,121,123,125,129,130,132,133,135,136,139,1 40,143,147,156,172,173,174,175,179,181,182,184,185 ,188,218,220,221,222,223,225,235,236,237,238,239,2 51,252,253,254,255,256,257,258,260,265,267,285,289 ,297,298,299,302,382,383,385,386,389 |
| P23443-5 | 1.038 | 375 | 1.072 | 976.521 | 0.56 | 0.721 | 0.887 | 0.691 | 0.924 | 0.748 | 1.048 | 91,94,95,96,97,98,99,100,101,102,103,104,105,106,1 07,108,109,112,113,116,117,120,124,133,136,137,143 ,144,145,147,148,149,150,151,152,153,195,197,200,2 02,204,205,210,212,213,214,215,216,340,347,350,352 ,353,354,356,359,366,369,370,371,372,373,374,375,3 95,496,497,499,500,501,502 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P23443-1_P23443-1_4l46_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P23443-1_4l46_A_P23443-2.pdb |
| 3D view using mol* of P23443-1_4l46_A_P23443-3.pdb |
| 3D view using mol* of P23443-1_4l46_A_P23443-4.pdb |
| 3D view using mol* of P23443-1_4l46_A_P23443-5.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P23443-1_P23443-2.pdb |
| 3D view using mol* of P23443-1_P23443-3.pdb |
| 3D view using mol* of P23443-1_P23443-4.pdb |
| 3D view using mol* of P23443-1_P23443-5.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P23443-1_vs_P23443-2.png |
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| ./stats/secondary_structure/figure/P23443-1_vs_P23443-3.png |
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| ./stats/secondary_structure/figure/P23443-1_vs_P23443-4.png |
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| ./stats/secondary_structure/figure/P23443-1_vs_P23443-5.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P23443-1_vs_P23443-2.png |
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| ./stats/relative_asa/P23443-1_vs_P23443-3.png |
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| ./stats/relative_asa/P23443-1_vs_P23443-4.png |
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| ./stats/relative_asa/P23443-1_vs_P23443-5.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to RPS6KB1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to RPS6KB1 |
| Previous studies relating to the alternative splicing of RPS6KB1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| RPS6KB1 | 17310252 | The gene encoding the splicing factor SF2/ASF is a proto-oncogene. | Alternative splicing modulates the expression of many oncogene and tumor-suppressor isoforms. We have tested whether some alternative splicing factors are involved in cancer. We found that the splicing factor SF2/ASF is upregulated in various human tumors, in part due to amplification of its gene, SFRS1. Moreover, slight overexpression of SF2/ASF is sufficient to transform immortal rodent fibroblasts, which form sarcomas in nude mice. We further show that SF2/ASF controls alternative splicing of the tumor suppressor BIN1 and the kinases MNK2 and S6K1. The resulting BIN1 isoforms lack tumor-suppressor activity; an isoform of MNK2 promotes MAP kinase-independent eIF4E phosphorylation; and an unusual oncogenic isoform of S6K1 recapitulates the transforming activity of SF2/ASF. Knockdown of either SF2/ASF or isoform-2 of S6K1 is sufficient to reverse transformation caused by the overexpression of SF2/ASF in vitro and in vivo. Thus, SF2/ASF can act as an oncoprotein and is a potential target for cancer therapy. | D002471 | Cell Transformation, Neoplastic |
| RPS6KB1 | 17310252 | The gene encoding the splicing factor SF2/ASF is a proto-oncogene. | Alternative splicing modulates the expression of many oncogene and tumor-suppressor isoforms. We have tested whether some alternative splicing factors are involved in cancer. We found that the splicing factor SF2/ASF is upregulated in various human tumors, in part due to amplification of its gene, SFRS1. Moreover, slight overexpression of SF2/ASF is sufficient to transform immortal rodent fibroblasts, which form sarcomas in nude mice. We further show that SF2/ASF controls alternative splicing of the tumor suppressor BIN1 and the kinases MNK2 and S6K1. The resulting BIN1 isoforms lack tumor-suppressor activity; an isoform of MNK2 promotes MAP kinase-independent eIF4E phosphorylation; and an unusual oncogenic isoform of S6K1 recapitulates the transforming activity of SF2/ASF. Knockdown of either SF2/ASF or isoform-2 of S6K1 is sufficient to reverse transformation caused by the overexpression of SF2/ASF in vitro and in vivo. Thus, SF2/ASF can act as an oncoprotein and is a potential target for cancer therapy. | D009369 | Neoplasms |
Clinically important variants in RPS6KB1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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