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Q9WUT3

- KS6A2_MOUSE

UniProt

Q9WUT3 - KS6A2_MOUSE

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Protein
Ribosomal protein S6 kinase alpha-2
Gene
Rps6ka2, Mapkapk1c, Rsk3
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 transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells By similarity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-570 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-377, allowing binding of PDPK1, which in turn phosphorylates Ser-218 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATP By similarity
Active sitei184 – 1841Proton acceptor By similarity
Binding sitei444 – 4441ATP By similarity
Active sitei532 – 5321Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 739ATP By similarity
Nucleotide bindingi421 – 4299ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. protein binding Source: MGI
  4. protein kinase activity Source: MGI
  5. protein serine/threonine kinase activity Source: MGI
  6. protein serine/threonine/tyrosine kinase activity Source: MGI
  7. ribosomal protein S6 kinase activity Source: MGI

GO - Biological processi

  1. brain renin-angiotensin system Source: MGI
  2. cardiac muscle cell apoptotic process Source: MGI
  3. cellular response to carbohydrate stimulus Source: MGI
  4. heart contraction Source: MGI
  5. heart development Source: MGI
  6. intracellular signal transduction Source: InterPro
  7. negative regulation of cell cycle Source: UniProtKB
  8. negative regulation of cell proliferation Source: UniProtKB
  9. negative regulation of meiosis Source: MGI
  10. oocyte maturation Source: MGI
  11. peptidyl-serine phosphorylation Source: MGI
  12. positive regulation of apoptotic process Source: UniProtKB
  13. positive regulation of gene expression Source: MGI
  14. protein phosphorylation Source: MGI
  15. regulation of protein processing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-2 (EC:2.7.11.1)
Short name:
S6K-alpha-2
Alternative name(s):
90 kDa ribosomal protein S6 kinase 2
Short name:
p90-RSK 2
Short name:
p90RSK2
MAP kinase-activated protein kinase 1c
Short name:
MAPK-activated protein kinase 1c
Short name:
MAPKAP kinase 1c
Short name:
MAPKAPK-1c
Protein-tyrosine kinase Mpk-9
Ribosomal S6 kinase 3
Short name:
RSK-3
pp90RSK3
Gene namesi
Name:Rps6ka2
Synonyms:Mapkapk1c, Rsk3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1342290. Rps6ka2.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Ribosomal protein S6 kinase alpha-2
PRO_0000086202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181Phosphoserine; by PDPK1 By similarity
Modified residuei377 – 3771Phosphoserine; alternate1 Publication
Modified residuei377 – 3771Phosphoserine; by autocatalysis; alternate By similarity
Cross-linki630 – 630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Post-translational modificationi

Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 By similarity.
N-terminal myristoylation results in an activated kinase in the absence of added growth factors By similarity.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9WUT3.
PaxDbiQ9WUT3.
PRIDEiQ9WUT3.

PTM databases

PhosphoSiteiQ9WUT3.

Expressioni

Gene expression databases

ArrayExpressiQ9WUT3.
BgeeiQ9WUT3.
CleanExiMM_RPS6KA2.
GenevestigatoriQ9WUT3.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation By similarity.

Protein-protein interaction databases

IntActiQ9WUT3. 4 interactions.
MINTiMINT-1486826.

Structurei

3D structure databases

ProteinModelPortaliQ9WUT3.
SMRiQ9WUT3. Positions 20-704.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 318260Protein kinase 1
Add
BLAST
Domaini319 – 38870AGC-kinase C-terminal
Add
BLAST
Domaini415 – 672258Protein kinase 2
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00730000110260.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
KOiK04373.
OMAiWIVNREY.
OrthoDBiEOG7B8S38.
PhylomeDBiQ9WUT3.
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_dom.
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.

Q9WUT3-1 [UniParc]FASTAAdd to Basket

« Hide

MELSMKKFTV RRFFSVYLRK KSRSKSSSLS RLEEEGIVKE IDISNHVKEG    50
FEKADPSQFE LLKVLGQGSY GKVFLVRKVT GSDAGQLYAM KVLKKATLKV 100
RDRVRSKMER DILAEVNHPF IVKLHYAFQT EGKLYLILDF LRGGDLFTRL 150
SKEVMFTEED VKFYLAELAL ALDHLHGLGI IYRDLKPENI LLDEEGHIKI 200
TDFGLSKEAT DHDKRAYSFC GTIEYMAPEV VNRRGHTQSA DWWSFGVLMF 250
EMLTGSLPFQ GKDRKETMAL ILKAKLGMPQ FLSAEAQSLL RALFKRNPCN 300
RLGAGVDGVE EIKRHPFFVT IDWNKLYRKE IKPPFKPAVG RPEDTFHFDP 350
EFTARTPTDS PGVPPSANAH HLFRGFSFVA SSLVQEPSQQ DVPKAPIHPI 400
VQQLHGNNIH FTDGYEIKED IGVGSYSVCK RCVHKATDAE YAVKIIDKSK 450
RDPSEEIEIL LRYGQHPNII TLKDVYDDGK YVYLVMELMR GGELLDRILR 500
QRCFSEREAS DVLYTIARTM DYLHSQGVVH RDLKPSNILY MDESGNPESI 550
RICDFGFAKQ LRAENGLLMT PCYTANFVAP EVLKRQGYDA ACDVWSLGIL 600
LYTMLAGFTP FANGPDDTPE EILARIGSGK YALSGGNWDS ISDAAKDVVS 650
KMLHVDPQQR LTAVQVLKHP WIVNREYLSQ NQLSRQDVHL VKGAMAATYF 700
ALNRTPQAPR LEPVLSSSLA QRRGMKRLTS TRL 733
Length:733
Mass (Da):83,157
Last modified:November 1, 1999 - v1
Checksum:i49C1390316CFCE91
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721K → E in BAB31901. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131021 mRNA. Translation: CAB44492.1.
AK019881 mRNA. Translation: BAB31901.1.
BC043064 mRNA. Translation: AAH43064.1.
BC051079 mRNA. Translation: AAH51079.1.
BC056946 mRNA. Translation: AAH56946.1.
X57237 mRNA. Translation: CAA40513.1.
CCDSiCCDS28376.1.
RefSeqiNP_035429.1. NM_011299.4.
UniGeneiMm.268383.

Genome annotation databases

EnsembliENSMUST00000024575; ENSMUSP00000024575; ENSMUSG00000023809.
GeneIDi20112.
KEGGimmu:20112.
UCSCiuc008aih.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131021 mRNA. Translation: CAB44492.1 .
AK019881 mRNA. Translation: BAB31901.1 .
BC043064 mRNA. Translation: AAH43064.1 .
BC051079 mRNA. Translation: AAH51079.1 .
BC056946 mRNA. Translation: AAH56946.1 .
X57237 mRNA. Translation: CAA40513.1 .
CCDSi CCDS28376.1.
RefSeqi NP_035429.1. NM_011299.4.
UniGenei Mm.268383.

3D structure databases

ProteinModelPortali Q9WUT3.
SMRi Q9WUT3. Positions 20-704.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9WUT3. 4 interactions.
MINTi MINT-1486826.

PTM databases

PhosphoSitei Q9WUT3.

Proteomic databases

MaxQBi Q9WUT3.
PaxDbi Q9WUT3.
PRIDEi Q9WUT3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024575 ; ENSMUSP00000024575 ; ENSMUSG00000023809 .
GeneIDi 20112.
KEGGi mmu:20112.
UCSCi uc008aih.2. mouse.

Organism-specific databases

CTDi 6196.
MGIi MGI:1342290. Rps6ka2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00730000110260.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
KOi K04373.
OMAi WIVNREY.
OrthoDBi EOG7B8S38.
PhylomeDBi Q9WUT3.
TreeFami TF313438.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.
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.

Miscellaneous databases

NextBioi 297615.
PROi Q9WUT3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WUT3.
Bgeei Q9WUT3.
CleanExi MM_RPS6KA2.
Genevestigatori Q9WUT3.

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_dom.
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. "The mouse Rsk3 gene maps to the Leh66 elements carrying the T-complex responder Tcr."
    Kispert A., Stoeger R.J., Caparros M., Herrmann B.G.
    Mamm. Genome 10:794-802(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Ovary and Uterus.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Retina.
  4. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
    Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
    Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 534-592.
    Strain: C57BL/6.
    Tissue: Embryonic brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.

Entry informationi

Entry nameiKS6A2_MOUSE
AccessioniPrimary (citable) accession number: Q9WUT3
Secondary accession number(s): Q9D2C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 133 of the entry and version 1 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

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