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Protein

Ribosomal protein S6 kinase alpha-5

Gene

Rps6ka5

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

Functioni

Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by phosphorylation at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-211, Ser-375 and Ser-380 by the activated C-terminal kinase domain. The active N-terminal kinase domain finally phosphorylates downstream substrates, as well as Ser-814, Ser-816 and Ser-822 in its own C-terminal region.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801ATPPROSITE-ProRule annotation
Active sitei176 – 1761Proton acceptorBy similarity
Binding sitei454 – 4541ATPPROSITE-ProRule annotation
Active sitei608 – 6081Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi54 – 629ATPPROSITE-ProRule annotation
Nucleotide bindingi431 – 44010ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: InterPro
  3. protein kinase activity Source: MGI
  4. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. histone H2A-S1 phosphorylation Source: UniProtKB
  2. histone H3-S10 phosphorylation Source: UniProtKB
  3. histone H3-S28 phosphorylation Source: UniProtKB
  4. histone phosphorylation Source: MGI
  5. inflammatory response Source: UniProtKB-KW
  6. interleukin-1-mediated signaling pathway Source: MGI
  7. intracellular signal transduction Source: UniProtKB
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of histone acetylation Source: MGI
  10. positive regulation of histone phosphorylation Source: MGI
  11. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. protein phosphorylation Source: UniProtKB
  14. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_277525. CREB phosphorylation.
REACT_323000. ERK/MAPK targets.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_353475. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-5 (EC:2.7.11.1)
Short name:
S6K-alpha-5
Alternative name(s):
90 kDa ribosomal protein S6 kinase 5
Nuclear mitogen- and stress-activated protein kinase 1
RSK-like protein kinase
Short name:
RLSK
Gene namesi
Name:Rps6ka5
Synonyms:Msk1
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1920336. Rps6ka5.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: MGI
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 863863Ribosomal protein S6 kinase alpha-5PRO_0000086208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111Phosphoserine; by autocatalysisBy similarity
Modified residuei359 – 3591Phosphoserine; by MAPK1, MAPK3 and MAPK14By similarity
Modified residuei375 – 3751Phosphoserine; by autocatalysisBy similarity
Modified residuei380 – 3801Phosphoserine; by autocatalysisBy similarity
Modified residuei645 – 6451Phosphothreonine; by MAPK1, MAPK3 and MAPK14By similarity
Modified residuei711 – 7111PhosphoserineBy similarity
Modified residuei721 – 7211PhosphoserineBy similarity
Modified residuei755 – 7551PhosphoserineBy similarity
Modified residuei759 – 7591PhosphoserineBy similarity
Modified residuei764 – 7641Phosphothreonine; by MAPK1, MAPK3 and MAPK14By similarity
Modified residuei814 – 8141Phosphoserine; by autocatalysisBy similarity
Modified residuei816 – 8161Phosphoserine; by autocatalysisBy similarity
Modified residuei822 – 8221Phosphoserine; by autocatalysisBy similarity
Modified residuei823 – 8231PhosphoserineBy similarity

Post-translational modificationi

Ser-375 and Thr-645 phosphorylation is required for kinase activity. Ser-375 and Ser-211 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-814, Ser-816 and Ser-822 by the N-terminal kinase domain (By similarity).By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8C050.
PaxDbiQ8C050.
PRIDEiQ8C050.

PTM databases

PhosphoSiteiQ8C050.

Expressioni

Gene expression databases

BgeeiQ8C050.
CleanExiMM_RPS6KA5.
GenevestigatoriQ8C050.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA5 associates with and phosphorylates the NF-kappa-B p65 subunit RELA. Interacts with CREBBP and EP300 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RaraP114162EBI-8391218,EBI-346736

Protein-protein interaction databases

BioGridi215759. 6 interactions.
IntActiQ8C050. 2 interactions.
MINTiMINT-4116279.
STRINGi10090.ENSMUSP00000042987.

Structurei

3D structure databases

ProteinModelPortaliQ8C050.
SMRiQ8C050. Positions 23-380, 414-793.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 317270Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini318 – 38669AGC-kinase C-terminalAdd
BLAST
Domaini428 – 675248Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 2 protein kinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ8C050.
KOiK04445.
OMAiFQSHDKS.
OrthoDBiEOG76HQ0Z.
PhylomeDBiQ8C050.
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.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 3 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 3 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2Curated (identifier: Q8C050-1) [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

        10         20         30         40         50
MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL
60 70 80 90 100
LKVLGTGAYG KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE
110 120 130 140 150
RQVLEHIRQS PFLVTLHYAF QTETKLHLIL DYINGGELFT HLSQRERFTE
160 170 180 190 200
HEVQIYVGEI VLALEHLHKL GIIYRDIKLE NILLDSNGHV VLTDFGLSKE
210 220 230 240 250
FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL GVLMYELLTG
260 270 280 290 300
ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR
310 320 330 340 350
LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE
360 370 380 390 400
FTEMDPTYSP AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD
410 420 430 440 450
RPGVTNVARS AMMKDSPFYQ HYDLDLKDKP LGEGSFSICR KCVHKKTNQA
460 470 480 490 500
FAVKIISKRM EANTQKEITA LKLCEGHPNI VKLHEVFHDQ VAASAQPPGQ
510 520 530 540 550
VVLCSLLLLA LLFNRSLTRK PVTWTWLVHS TSQLPPLPPP MPEIVLFILL
560 570 580 590 600
SDNGQLHTFL VMELLNGGEL FERIKRKKHF SETEASYIMR KLVSAVSHMH
610 620 630 640 650
DVGVVHRDLK PENLLFTDEN DNLEIKVIDF GFARLKPPDN QPLKTPCFTL
660 670 680 690 700
HYAAPELLTH NGYDESCDLW SLGVILYTML SGQVPFQSHD RSLTCTSAVE
710 720 730 740 750
IMKKIKKGDF SFEGEAWKNV SQEAKDLIQG LLTVDPNKRL KMSGLRYNEW
760 770 780 790 800
LQDGSQLSSN PLMTPDILGS SGAAVHTCVK ATFHAFNKYK REGFCLQNVD
810 820 830 840 850
KAPLAKRRKM KRTSTSTETR SSSSESSRSS SSQSHGKTTP TKTLQPSNPT
860
EGSNPDTLFQ FSD
Length:863
Mass (Da):96,583
Last modified:October 23, 2003 - v2
Checksum:i7A3C76D4036EA3EA
GO
Isoform 1Curated (identifier: Q8C050-2) [UniParc]FASTAAdd to basket

Also known as: 5Curated

The sequence of this isoform differs from the canonical sequence as follows:
     490-554: Missing.

Show »
Length:798
Mass (Da):89,515
Checksum:i57AB12399BEF7B0E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 1514EGEGG…AGTSG → GGRAAAAAARAPAE in AAQ24165 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti117 – 1171H → N in BAC27809 (PubMed:16141072).Curated
Sequence conflicti376 – 3761F → Y in BAC27809 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei490 – 55465Missing in isoform 1. 3 PublicationsVSP_050613Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY341873 mRNA. Translation: AAQ24158.1.
AY341881 mRNA. Translation: AAQ24165.1.
AK032316 mRNA. Translation: BAC27809.1.
BC035298 mRNA. Translation: AAH35298.1.
CCDSiCCDS26107.1. [Q8C050-1]
RefSeqiNP_705815.1. NM_153587.2. [Q8C050-1]
XP_006516337.1. XM_006516274.2. [Q8C050-2]
UniGeneiMm.220417.
Mm.392855.

Genome annotation databases

EnsembliENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180. [Q8C050-1]
GeneIDi73086.
KEGGimmu:73086.
UCSCiuc007ost.1. mouse. [Q8C050-1]
uc007osu.1. mouse. [Q8C050-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY341873 mRNA. Translation: AAQ24158.1.
AY341881 mRNA. Translation: AAQ24165.1.
AK032316 mRNA. Translation: BAC27809.1.
BC035298 mRNA. Translation: AAH35298.1.
CCDSiCCDS26107.1. [Q8C050-1]
RefSeqiNP_705815.1. NM_153587.2. [Q8C050-1]
XP_006516337.1. XM_006516274.2. [Q8C050-2]
UniGeneiMm.220417.
Mm.392855.

3D structure databases

ProteinModelPortaliQ8C050.
SMRiQ8C050. Positions 23-380, 414-793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215759. 6 interactions.
IntActiQ8C050. 2 interactions.
MINTiMINT-4116279.
STRINGi10090.ENSMUSP00000042987.

PTM databases

PhosphoSiteiQ8C050.

Proteomic databases

MaxQBiQ8C050.
PaxDbiQ8C050.
PRIDEiQ8C050.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180. [Q8C050-1]
GeneIDi73086.
KEGGimmu:73086.
UCSCiuc007ost.1. mouse. [Q8C050-1]
uc007osu.1. mouse. [Q8C050-2]

Organism-specific databases

CTDi9252.
MGIiMGI:1920336. Rps6ka5.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121860.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ8C050.
KOiK04445.
OMAiFQSHDKS.
OrthoDBiEOG76HQ0Z.
PhylomeDBiQ8C050.
TreeFamiTF313438.

Enzyme and pathway databases

ReactomeiREACT_277525. CREB phosphorylation.
REACT_323000. ERK/MAPK targets.
REACT_339798. NCAM signaling for neurite out-growth.
REACT_353475. Recycling pathway of L1.

Miscellaneous databases

NextBioi337443.
PROiQ8C050.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C050.
CleanExiMM_RPS6KA5.
GenevestigatoriQ8C050.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 3 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 3 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of mouse ribosomal protein S6 kinase, 90kDa, polypeptide 5 (RPS6KA5)."
    Zhou G., Wang J., Xu W.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  4. "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
    Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
    J. Biol. Chem. 276:33213-33219(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  5. "MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells."
    Zhang Y., Liu G., Dong Z.
    J. Biol. Chem. 276:42534-42542(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3.
  6. "MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts."
    Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S.
    Mol. Cell. Biol. 22:2871-2881(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1 AND ATF1.
  7. "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)."
    Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.
    EMBO J. 22:1313-1324(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Mitogen and stress response kinase-1 (MSK1) mediates excitotoxic induced death of hippocampal neurones."
    Hughes J.P., Staton P.C., Wilkinson M.G., Strijbos P.J., Skaper S.D., Arthur J.S., Reith A.D.
    J. Neurochem. 86:25-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL DEATH.
  9. "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
    Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
    J. Cell Sci. 118:2247-2259(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  10. "ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-kappaB transactivation during oxidative stress in skeletal myoblasts."
    Kefaloyianni E., Gaitanaki C., Beis I.
    Cell. Signal. 18:2238-2251(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RELA/NFKB3.
  11. "The kinases MSK1 and MSK2 are required for epidermal growth factor-induced, but not tumor necrosis factor-induced, histone H3 Ser10 phosphorylation."
    Duncan E.A., Anest V., Cogswell P., Baldwin A.S.
    J. Biol. Chem. 281:12521-12525(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  12. "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling."
    Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.
    Nat. Immunol. 9:1028-1036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1; ATF1 AND HISTONE H3.

Entry informationi

Entry nameiKS6A5_MOUSE
AccessioniPrimary (citable) accession number: Q8C050
Secondary accession number(s): Q8CI92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2003
Last sequence update: October 23, 2003
Last modified: March 31, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Enzyme activity requires the presence of both kinase domains.By similarity

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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.