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Q9Z1M4 (KS6B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal protein S6 kinase beta-2

Short name=S6K-beta-2
Short name=S6K2
EC=2.7.11.1
Alternative name(s):
70 kDa ribosomal protein S6 kinase 2
p70 ribosomal S6 kinase beta
Short name=p70 S6 kinase beta
Short name=p70 S6K-beta
Short name=p70 S6KB
Gene names
Name:Rps6kb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates specifically ribosomal protein S6.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Post-translational modification

Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Ribosomal protein S6 kinase beta-2
PRO_0000086215

Regions

Domain67 – 328262Protein kinase
Domain329 – 39971AGC-kinase C-terminal
Nucleotide binding73 – 819ATP By similarity
Motif474 – 4807Nuclear localization signal By similarity
Compositional bias411 – 48575Pro-rich

Sites

Active site1941Proton acceptor By similarity
Binding site991ATP By similarity

Amino acid modifications

Modified residue151Phosphoserine By similarity
Modified residue4201Phosphothreonine Ref.3
Modified residue4231Phosphoserine Ref.3
Modified residue4761Phosphoserine; by PKC By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z1M4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 396929ADAB0F6CB6

FASTA48553,538
        10         20         30         40         50         60 
MAAVFDLDLE TEEGSEGEGE PEFSPADVCP LGELRAAGLE TVGHYEEVEL TESSVNLGPE 

        70         80         90        100        110        120 
RIGPHCFELL SVLGKGGYGK VFQVRKVQGT NLGKIYAMKV LRKAKIVCSA KDTAHTRAER 

       130        140        150        160        170        180 
NILESVKHPF IVELAYAFQT GGKLYLILEC LSGGELFTHL EREGIFLEDT ACFYLAEITL 

       190        200        210        220        230        240 
ALGHLHSHGI IYRDLKPENI MLSSQGHIKL TDFGLCKESI HEGAITHTFC GTIEYMAPEI 

       250        260        270        280        290        300 
LVRTGHNRAV DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIKGKLVLPP YLTPDARDLA 

       310        320        330        340        350        360 
KKFLKRNPTQ RIGGGLGDAA DVQRHPFFRH INWDDLLARR VDPPFRPSLQ SEEDVSQFDA 

       370        380        390        400        410        420 
RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE GFSFQPKLRS PRRLNSSPRT 

       430        440        450        460        470        480 
PISPLKFSPF EGFRPSPGPP EPMEPSLPPL LPSPPSPPPT STAPLPIRPP SGTKKSKKGR 


GRSGR 

« Hide

References

« Hide 'large scale' references
[1]"Disruption of the p70(s6k)/p85(s6k) gene reveals a small mouse phenotype and a new functional S6 kinase."
Shima H., Pende M., Chen Y., Fumagalli S., Thomas G., Kozma S.C.
EMBO J. 17:6649-6659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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: Placenta.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007938 mRNA. Translation: CAA07774.1.
AK014412 mRNA. Translation: BAB29335.1.
CCDSCCDS29419.1.
RefSeqNP_067460.1. NM_021485.2.
UniGeneMm.271937.

3D structure databases

ProteinModelPortalQ9Z1M4.
SMRQ9Z1M4. Positions 58-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000025749.

PTM databases

PhosphoSiteQ9Z1M4.

Proteomic databases

PaxDbQ9Z1M4.
PRIDEQ9Z1M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025749; ENSMUSP00000025749; ENSMUSG00000024830.
ENSMUST00000181245; ENSMUSP00000137802; ENSMUSG00000097721.
GeneID58988.
KEGGmmu:58988.
UCSCuc008fzb.1. mouse.

Organism-specific databases

CTD6199.
MGIMGI:1927343. Rps6kb2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114960.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ9Z1M4.
KOK04688.
OMAHYEEIEI.
OrthoDBEOG7B8S38.
PhylomeDBQ9Z1M4.
TreeFamTF313438.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressQ9Z1M4.
BgeeQ9Z1M4.
GenevestigatorQ9Z1M4.

Family and domain databases

InterProIPR000961. 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]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

NextBio314486.
PROQ9Z1M4.
SOURCESearch...

Entry information

Entry nameKS6B2_MOUSE
AccessionPrimary (citable) accession number: Q9Z1M4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot