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P18654

- KS6A3_MOUSE

UniProt

P18654 - KS6A3_MOUSE

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Protein

Ribosomal protein S6 kinase alpha-3

Gene

Rps6ka3

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 ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001ATPPROSITE-ProRule annotation
Active sitei193 – 1931Proton acceptorBy similarity
Binding sitei451 – 4511ATPPROSITE-ProRule annotation
Active sitei539 – 5391Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 829ATPPROSITE-ProRule annotation
Nucleotide bindingi428 – 4369ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: Ensembl
  3. magnesium ion binding Source: InterPro
  4. protein kinase binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. intracellular signal transduction Source: InterPro
  3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. response to lipopolysaccharide Source: UniProtKB
  5. response to stress Source: UniProtKB-KW
  6. toll-like receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_198245. RSK activation.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_215063. ERK/MAPK targets.
REACT_224314. CREB phosphorylation.
REACT_257923. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-3 (EC:2.7.11.1)
Short name:
S6K-alpha-3
Alternative name(s):
90 kDa ribosomal protein S6 kinase 3
Short name:
p90-RSK 3
Short name:
p90RSK3
MAP kinase-activated protein kinase 1b
Short name:
MAPK-activated protein kinase 1b
Short name:
MAPKAP kinase 1b
Short name:
MAPKAPK-1b
Ribosomal S6 kinase 2
Short name:
RSK-2
pp90RSK2
Gene namesi
Name:Rps6ka3
Synonyms:Mapkapk1b, Rps6ka-rs1, Rsk2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:104557. Rps6ka3.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271S → E: Loss of phosphorylation and activation by PDPK1. 1 Publication
Mutagenesisi386 – 3861S → A: Loss of phosphorylation by PDPK1; loss of activation by PDPK1 and EGF. 2 Publications
Mutagenesisi386 – 3861S → E: Loss of interaction with PDPK1 and phosphorylation at S-227. 2 Publications
Mutagenesisi529 – 5291Y → F: Attenuates activation by MAPK1/ERK1 and MAPK3/ERK2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Ribosomal protein S6 kinase alpha-3PRO_0000086204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine; by PDPK11 Publication
Modified residuei365 – 3651PhosphothreonineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei386 – 3861Phosphoserine; by autocatalysis and MAPKAPK22 Publications
Modified residuei415 – 4151PhosphoserineBy similarity
Modified residuei529 – 5291Phosphotyrosine; by FGFR31 Publication
Modified residuei556 – 5561PhosphoserineBy similarity
Modified residuei715 – 7151PhosphoserineBy similarity

Post-translational modificationi

Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.3 Publications
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP18654.
PaxDbiP18654.
PRIDEiP18654.

PTM databases

PhosphoSiteiP18654.

Expressioni

Tissue specificityi

Intestine, thymus, lung, heart and brain.

Gene expression databases

BgeeiP18654.
CleanExiMM_RPS6KA3.
ExpressionAtlasiP18654. baseline and differential.
GenevestigatoriP18654.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi225783. 6 interactions.
DIPiDIP-31554N.
IntActiP18654. 7 interactions.
MINTiMINT-1486771.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 567Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 758Combined sources
Helixi77 – 793Combined sources
Beta strandi81 – 877Combined sources
Turni91 – 944Combined sources
Beta strandi96 – 11116Combined sources
Helixi121 – 1244Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi142 – 1476Combined sources
Helixi156 – 1627Combined sources
Helixi167 – 18620Combined sources
Helixi196 – 1983Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi207 – 21610Combined sources
Helixi232 – 2343Combined sources
Helixi237 – 2415Combined sources
Helixi248 – 26316Combined sources
Helixi273 – 28210Combined sources
Helixi293 – 30210Combined sources
Helixi307 – 3093Combined sources
Turni315 – 3173Combined sources
Helixi318 – 3225Combined sources
Helixi325 – 3273Combined sources
Helixi332 – 3365Combined sources
Helixi418 – 4214Combined sources
Beta strandi422 – 4309Combined sources
Beta strandi432 – 44110Combined sources
Turni442 – 4443Combined sources
Beta strandi447 – 4548Combined sources
Turni455 – 4573Combined sources
Helixi461 – 47010Combined sources
Beta strandi479 – 4846Combined sources
Beta strandi486 – 4938Combined sources
Helixi501 – 5066Combined sources
Helixi513 – 53220Combined sources
Helixi542 – 5443Combined sources
Beta strandi545 – 5517Combined sources
Helixi554 – 5563Combined sources
Beta strandi557 – 5593Combined sources
Helixi587 – 61327Combined sources
Helixi626 – 63510Combined sources
Turni643 – 6475Combined sources
Helixi650 – 65910Combined sources
Turni664 – 6663Combined sources
Helixi670 – 6734Combined sources
Helixi677 – 6804Combined sources
Helixi682 – 6843Combined sources
Helixi696 – 71015Combined sources
Turni711 – 7133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QR7X-ray2.00A399-740[»]
2QR8X-ray2.00A399-740[»]
3G51X-ray1.80A44-367[»]
3UBDX-ray1.53A45-346[»]
4EL9X-ray1.55A45-346[»]
4GUEX-ray1.80A45-346[»]
ProteinModelPortaliP18654.
SMRiP18654. Positions 51-714.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18654.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 327260Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini328 – 39770AGC-kinase C-terminalAdd
BLAST
Domaini422 – 679258Protein 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.
GeneTreeiENSGT00770000120454.
HOVERGENiHBG108317.
InParanoidiP18654.
KOiK04373.
OMAiHPWIVHC.
PhylomeDBiP18654.
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. 2 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. 2 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]

Sequencei

Sequence statusi: Complete.

P18654-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEGSIKEI
60 70 80 90 100
AITHHVKEGH EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK
110 120 130 140 150
VLKKATLKVR DRVRTKMERD ILVEVNHPFI VKLHYAFQTE GKLYLILDFL
160 170 180 190 200
RGGDLFTRLS KEVMFTEEDV KFYLAELALA LDHLHSLGII YRDLKPENIL
210 220 230 240 250
LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV NRRGHTQSAD
260 270 280 290 300
WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
310 320 330 340 350
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR
360 370 380 390 400
PEDTFYFDPE FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ
410 420 430 440 450
TVGVHSIVQQ LHRNSIQFTD GYEVKEDIGV GSYSVCKRCI HKATNMEFAV
460 470 480 490 500
KIIDKSKRDP TEEIEILLRY GQHPNIITLK DVYDDGKYVY VVTELMKGGE
510 520 530 540 550
LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL KPSNILYVDE
560 570 580 590 600
SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
610 620 630 640 650
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD
660 670 680 690 700
TAKDLVSKML HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK
710 720 730 740
GAMAATYSAL NRNQSPVLEP VGRSTLAQRR GIKKITSTAL
Length:740
Mass (Da):83,694
Last modified:March 25, 2003 - v2
Checksum:i0CD54E5918567007
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY083469 mRNA. Translation: AAM00022.1.
AL808146 Genomic DNA. Translation: CAM25836.1.
CCDSiCCDS30502.1.
PIRiC32571.
S30504.
RefSeqiNP_683747.1. NM_148945.2.
UniGeneiMm.328476.
Mm.392829.

Genome annotation databases

EnsembliENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
GeneIDi110651.
KEGGimmu:110651.
UCSCiuc009usj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY083469 mRNA. Translation: AAM00022.1 .
AL808146 Genomic DNA. Translation: CAM25836.1 .
CCDSi CCDS30502.1.
PIRi C32571.
S30504.
RefSeqi NP_683747.1. NM_148945.2.
UniGenei Mm.328476.
Mm.392829.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QR7 X-ray 2.00 A 399-740 [» ]
2QR8 X-ray 2.00 A 399-740 [» ]
3G51 X-ray 1.80 A 44-367 [» ]
3UBD X-ray 1.53 A 45-346 [» ]
4EL9 X-ray 1.55 A 45-346 [» ]
4GUE X-ray 1.80 A 45-346 [» ]
ProteinModelPortali P18654.
SMRi P18654. Positions 51-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 225783. 6 interactions.
DIPi DIP-31554N.
IntActi P18654. 7 interactions.
MINTi MINT-1486771.

Chemistry

BindingDBi P18654.

PTM databases

PhosphoSitei P18654.

Proteomic databases

MaxQBi P18654.
PaxDbi P18654.
PRIDEi P18654.

Protocols and materials databases

DNASUi 110651.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033671 ; ENSMUSP00000033671 ; ENSMUSG00000031309 .
GeneIDi 110651.
KEGGi mmu:110651.
UCSCi uc009usj.1. mouse.

Organism-specific databases

CTDi 6197.
MGIi MGI:104557. Rps6ka3.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120454.
HOVERGENi HBG108317.
InParanoidi P18654.
KOi K04373.
OMAi HPWIVHC.
PhylomeDBi P18654.
TreeFami TF313438.

Enzyme and pathway databases

Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_198245. RSK activation.
REACT_198246. CREB phosphorylation through the activation of Ras.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_215063. ERK/MAPK targets.
REACT_224314. CREB phosphorylation.
REACT_257923. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSi Rps6ka3. mouse.
EvolutionaryTracei P18654.
NextBioi 364399.
PROi P18654.
SOURCEi Search...

Gene expression databases

Bgeei P18654.
CleanExi MM_RPS6KA3.
ExpressionAtlasi P18654. baseline and differential.
Genevestigatori P18654.

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.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal domain as a protein kinase."
    Chrestensen C.A., Sturgill T.W.
    J. Biol. Chem. 277:27733-27741(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase."
    Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W., Erikson R.L.
    Mol. Cell. Biol. 9:3850-3859(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-740.
  4. "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1."
    Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M.
    J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-227 AND SER-386, MUTAGENESIS OF SER-227 AND SER-386.
  5. "A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1."
    Froedin M., Jensen C.J., Merienne K., Gammeltoft S.
    EMBO J. 19:2924-2934(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-386.
  6. "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization."
    Fujita N., Sato S., Tsuruo T.
    J. Biol. Chem. 278:49254-49260(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
  7. "FGFR3 activates RSK2 to mediate hematopoietic transformation through tyrosine phosphorylation of RSK2 and activation of the MEK/ERK pathway."
    Kang S., Dong S., Gu T.L., Guo A., Cohen M.S., Lonial S., Khoury H.J., Fabbro D., Gilliland D.G., Bergsagel P.L., Taunton J., Polakiewicz R.D., Chen J.
    Cancer Cell 12:201-214(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HEMATOPOIETIC TRANSFORMATION, PHOSPHORYLATION AT TYR-529, MUTAGENESIS OF TYR-529.
  8. "The MAPK-activated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways."
    Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.
    Nat. Immunol. 8:1227-1235(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, PHOSPHORYLATION AT SER-386.
  9. "Structural basis for activation of the autoinhibitory C-terminal kinase domain of p90 RSK2."
    Malakhova M., Tereshko V., Lee S.Y., Yao K., Cho Y.Y., Bode A., Dong Z.
    Nat. Struct. Mol. Biol. 15:112-113(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 399-740.
  10. "Structural diversity of the active N-terminal kinase domain of p90 ribosomal S6 kinase 2."
    Malakhova M., Kurinov I., Liu K., Zheng D., D'Angelo I., Shim J.H., Steinman V., Bode A.M., Dong Z.
    PLoS ONE 4:E8044-E8044(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-367.

Entry informationi

Entry nameiKS6A3_MOUSE
AccessioniPrimary (citable) accession number: P18654
Secondary accession number(s): B1AXN4, Q03140, Q8K3J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 25, 2003
Last modified: November 26, 2014
This is version 151 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3