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Q8BSK8

- KS6B1_MOUSE

UniProt

Q8BSK8 - KS6B1_MOUSE

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Protein

Ribosomal protein S6 kinase beta-1

Gene
Rps6kb1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that acts downstream of mTOR 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. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR By similarity.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform Alpha I and isoform Alpha II are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231ATP By similarity
Active sitei218 – 2181Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 1059ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. peptide binding Source: Ensembl
  3. protein binding Source: IntAct
  4. protein kinase activity Source: MGI
  5. protein serine/threonine/tyrosine kinase activity Source: MGI
  6. ribosomal protein S6 kinase activity Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. apoptotic process Source: UniProtKB-KW
  3. cell migration Source: Ensembl
  4. cellular response to growth factor stimulus Source: UniProtKB
  5. cellular response to hormone stimulus Source: Ensembl
  6. G1/S transition of mitotic cell cycle Source: Ensembl
  7. germ cell development Source: MGI
  8. long-term memory Source: Ensembl
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  11. negative regulation of insulin receptor signaling pathway Source: Ensembl
  12. positive regulation of mitotic cell cycle Source: Ensembl
  13. positive regulation of skeletal muscle tissue growth Source: Ensembl
  14. positive regulation of smooth muscle cell migration Source: Ensembl
  15. positive regulation of smooth muscle cell proliferation Source: Ensembl
  16. positive regulation of translational initiation Source: Ensembl
  17. protein kinase B signaling Source: MGI
  18. protein phosphorylation Source: MGI
  19. regulation of glucose import Source: Ensembl
  20. response to drug Source: Ensembl
  21. response to electrical stimulus involved in regulation of muscle adaptation Source: Ensembl
  22. response to ethanol Source: Ensembl
  23. response to glucagon Source: Ensembl
  24. response to glucocorticoid Source: Ensembl
  25. response to glucose Source: Ensembl
  26. response to heat Source: Ensembl
  27. response to insulin Source: Ensembl
  28. response to leucine Source: Ensembl
  29. response to lipopolysaccharide Source: Ensembl
  30. response to mechanical stimulus Source: Ensembl
  31. response to nutrient Source: Ensembl
  32. response to testosterone Source: Ensembl
  33. response to toxic substance Source: Ensembl
  34. response to tumor necrosis factor Source: Ensembl
  35. response to wounding Source: Ensembl
  36. skeletal muscle atrophy Source: Ensembl
  37. skeletal muscle contraction Source: Ensembl
  38. TOR signaling Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase beta-1 (EC:2.7.11.1)
Short name:
S6K-beta-1
Short name:
S6K1
Alternative name(s):
70 kDa ribosomal protein S6 kinase 1
Short name:
P70S6K1
Short name:
p70-S6K 1
Ribosomal protein S6 kinase I
Short name:
S6K
p70 ribosomal S6 kinase alpha
Short name:
p70 S6 kinase alpha
Short name:
p70 S6K-alpha
Short name:
p70 S6KA
Gene namesi
Name:Rps6kb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1270849. Rps6kb1.

Subcellular locationi

Cytoplasm By similarity. Cell junctionsynapsesynaptosome By similarity. Mitochondrion outer membrane. Mitochondrion By similarity
Note: Colocalizes with URI1 at mitochondrion By similarity.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell surface Source: Ensembl
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: UniProtKB
  5. neuron projection Source: UniProtKB-SubCell
  6. nucleus Source: Ensembl
  7. perinuclear region of cytoplasm Source: Ensembl
  8. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Impairment of body growth. Lethal in combination with Rps6kb2 deficiency.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525Ribosomal protein S6 kinase beta-1PRO_0000024344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521Phosphothreonine; by PDPK1 By similarity
Modified residuei394 – 3941Phosphoserine By similarity
Modified residuei412 – 4121Phosphothreonine; by MTOR, NEK6 and NEK7 By similarity
Modified residuei434 – 4341Phosphoserine By similarity
Modified residuei441 – 4411Phosphoserine By similarity
Modified residuei444 – 4441Phosphothreonine By similarity
Modified residuei447 – 4471Phosphoserine By similarity
Modified residuei452 – 4521Phosphoserine By similarity
Modified residuei516 – 5161N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism. Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BSK8.
PaxDbiQ8BSK8.
PRIDEiQ8BSK8.

PTM databases

PhosphoSiteiQ8BSK8.

Expressioni

Gene expression databases

ArrayExpressiQ8BSK8.
BgeeiQ8BSK8.
CleanExiMM_RPS6KB1.
GenevestigatoriQ8BSK8.

Interactioni

Subunit structurei

Interacts with PPP1R9A/neurabin-1 By similarity. Interacts with RPTOR. Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with POLDIP3 and TRAF4 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
Mdm2P238042EBI-646423,EBI-641788

Protein-protein interaction databases

BioGridi215408. 10 interactions.
IntActiQ8BSK8. 5 interactions.
MINTiMINT-5092082.

Structurei

3D structure databases

ProteinModelPortaliQ8BSK8.
SMRiQ8BSK8. Positions 81-417.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 352262Protein kinaseAdd
BLAST
Domaini353 – 42371AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni424 – 525102Autoinhibitory domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi28 – 325TOS motif

Domaini

The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop By similarity.
The TOS (TOR signaling) motif is essential for activation by mTORC1 By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000114960.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ5SWG1.
KOiK04688.
OMAiANRMPAR.
OrthoDBiEOG7B8S38.
TreeFamiTF313438.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016238. Ribosomal_S6_kinase.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Alpha I (identifier: Q8BSK8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRRRRRRDGF YLAPDFRHRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL    50
NESMDHGGVG PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG 100
GYGKVFQVRK VTGANTGKIF AMKVLKKAMI VRNAKDTAHT KAERNILEEV 150
KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL FMQLEREGIF MEDTACFYLA 200
EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC KESIHDGTVT 250
HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK 300
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP 350
FFRHINWEEL LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL 400
SESANQVFLG FTYVAPSVLE SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK 450
FSPGDFWGRG ASASTANPQT PVEYPMETSG IEQMDVTVSG EASAPLPIRQ 500
PNSGPYKKQA FPMISKRPEH LRMNL 525
Length:525
Mass (Da):59,146
Last modified:July 27, 2011 - v2
Checksum:i5B3C09F6BB365EE2
GO
Isoform Alpha II (identifier: Q8BSK8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Show »
Length:502
Mass (Da):56,157
Checksum:i5AE6CF3FCAAE8B83
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform Alpha II. VSP_018840Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601G → E in BAC28000. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032724 mRNA. Translation: BAC28000.1.
AL604063 Genomic DNA. Translation: CAI25799.1.
CH466556 Genomic DNA. Translation: EDL15788.1.
BC038491 mRNA. Translation: AAH38491.1.
CCDSiCCDS48875.1. [Q8BSK8-1]
RefSeqiNP_001107806.1. NM_001114334.1. [Q8BSK8-1]
UniGeneiMm.394280.
Mm.446624.
Mm.479484.

Genome annotation databases

EnsembliENSMUST00000154617; ENSMUSP00000119715; ENSMUSG00000020516. [Q8BSK8-1]
GeneIDi72508.
KEGGimmu:72508.
UCSCiuc007ksn.2. mouse. [Q8BSK8-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032724 mRNA. Translation: BAC28000.1 .
AL604063 Genomic DNA. Translation: CAI25799.1 .
CH466556 Genomic DNA. Translation: EDL15788.1 .
BC038491 mRNA. Translation: AAH38491.1 .
CCDSi CCDS48875.1. [Q8BSK8-1 ]
RefSeqi NP_001107806.1. NM_001114334.1. [Q8BSK8-1 ]
UniGenei Mm.394280.
Mm.446624.
Mm.479484.

3D structure databases

ProteinModelPortali Q8BSK8.
SMRi Q8BSK8. Positions 81-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 215408. 10 interactions.
IntActi Q8BSK8. 5 interactions.
MINTi MINT-5092082.

Chemistry

ChEMBLi CHEMBL5429.

PTM databases

PhosphoSitei Q8BSK8.

Proteomic databases

MaxQBi Q8BSK8.
PaxDbi Q8BSK8.
PRIDEi Q8BSK8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000154617 ; ENSMUSP00000119715 ; ENSMUSG00000020516 . [Q8BSK8-1 ]
GeneIDi 72508.
KEGGi mmu:72508.
UCSCi uc007ksn.2. mouse. [Q8BSK8-1 ]

Organism-specific databases

CTDi 6198.
MGIi MGI:1270849. Rps6kb1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000114960.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q5SWG1.
KOi K04688.
OMAi ANRMPAR.
OrthoDBi EOG7B8S38.
TreeFami TF313438.

Miscellaneous databases

NextBioi 336366.
PROi Q8BSK8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BSK8.
Bgeei Q8BSK8.
CleanExi MM_RPS6KB1.
Genevestigatori Q8BSK8.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016238. Ribosomal_S6_kinase.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
    Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
    EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF EEF2K.
  6. "p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD."
    Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD, FUNCTION IN APOPTOSIS REGULATION, SUBCELLULAR LOCATION.
  7. "S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway."
    Pende M., Um S.H., Mieulet V., Sticker M., Goss V.L., Mestan J., Mueller M., Fumagalli S., Kozma S.C., Thomas G.
    Mol. Cell. Biol. 24:3112-3124(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "S6K directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-(alpha) signaling through IKK2."
    Zhang J., Gao Z., Yin J., Quon M.J., Ye J.
    J. Biol. Chem. 283:35375-35382(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.

Entry informationi

Entry nameiKS6B1_MOUSE
AccessioniPrimary (citable) accession number: Q8BSK8
Secondary accession number(s): Q5SWG1, Q8CHX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi