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Q9UBS0 (KS6B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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
Short name=P70S6K2
Short name=p70-S6K 2
S6 kinase-related kinase
Short name=SRK
Serine/threonine-protein kinase 14B
p70 ribosomal S6 kinase beta
Short name=S6K-beta
Short name=p70 S6 kinase beta
Short name=p70 S6K-beta
Short name=p70 S6KB
Short name=p70-beta
Gene names
Name:RPS6KB2
Synonyms:STK14B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 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. Nucleus Ref.8 Ref.9.

Post-translational modification

Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention. Ref.8 Ref.9

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 caution

The sequence BAA34402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of translational initiation

Inferred from mutant phenotype PubMed 16763566. Source: UniProtKB

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

translation

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide binding

Inferred from electronic annotation. Source: Ensembl

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: ProtInc

ribosomal protein S6 kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Ribosomal protein S6 kinase beta-2
PRO_0000086214

Regions

Domain67 – 328262Protein kinase
Domain329 – 39971AGC-kinase C-terminal
Nucleotide binding73 – 819ATP By similarity
Motif471 – 4777Nuclear localization signal Ref.9
Compositional bias411 – 48272Pro-rich

Sites

Active site1941Proton acceptor By similarity
Binding site991ATP By similarity

Amino acid modifications

Modified residue151Phosphoserine Ref.10
Modified residue4231Phosphoserine By similarity
Modified residue4731Phosphoserine; by PKC Ref.9

Natural variations

Natural variant2671P → L. Ref.13
Corresponds to variant rs55987642 [ dbSNP | Ensembl ].
VAR_040643
Natural variant3681V → M. Ref.13
Corresponds to variant rs55642995 [ dbSNP | Ensembl ].
VAR_040644
Natural variant4201A → V. Ref.1 Ref.2 Ref.3 Ref.7 Ref.13
Corresponds to variant rs13859 [ dbSNP | Ensembl ].
VAR_040645
Natural variant4431T → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.13
VAR_040646

Experimental info

Sequence conflict901Missing in BAA37145. Ref.2
Sequence conflict4091R → C in BAA37145. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UBS0 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 5D33660D24A2C7BE

FASTA48253,455
        10         20         30         40         50         60 
MAAVFDLDLE TEEGSEGEGE PELSPADACP LAELRAAGLE PVGHYEEVEL TETSVNVGPE 

        70         80         90        100        110        120 
RIGPHCFELL RVLGKGGYGK VFQVRKVQGT NLGKIYAMKV LRKAKIVRNA KDTAHTRAER 

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

       190        200        210        220        230        240 
ALGHLHSQGI IYRDLKPENI MLSSQGHIKL TDFGLCKESI HEGAVTHTFC GTIEYMAPEI 

       250        260        270        280        290        300 
LVRSGHNRAV DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIRGKLALPP YLTPDARDLV 

       310        320        330        340        350        360 
KKFLKRNPSQ RIGGGPGDAA DVQRHPFFRH MNWDDLLAWR VDPPFRPCLQ SEEDVSQFDT 

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

       430        440        450        460        470        480 
PVSPLKFSPF EGFRPSPSLP EPTELPLPPL LPPPPPSTTA PLPIRPPSGT KKSKRGRGRP 


GR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region."
Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D., Yonezawa K.
J. Biol. Chem. 273:30061-30064(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[2]"Cloning and characterization of p70 S6Kbeta defines a novel family of p70 S6 kinases."
Saitoh M., ten Dijke P., Miyazono K., Ichijo H.
Biochem. Biophys. Res. Commun. 253:470-476(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[3]"Characterization of S6K2, a novel kinase homologous to S6K1."
Lee-Fruman K.K., Kuo C.J., Lippincott J., Terada N., Blenis J.
Oncogene 18:5108-5114(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[4]"Cloning and characterization of a novel S6 kinase-related kinase, SRK."
Koh H.J., Lee B.N., Choi H.S., Chung J.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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], VARIANT VAL-420.
Tissue: Brain.
[8]"Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin."
Park I.H., Bachmann R., Shirazi H., Chen J.
J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY MTOR, SUBCELLULAR LOCATION.
[9]"Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization."
Valovka T., Verdier F., Cramer R., Zhyvoloup A., Fenton T., Rebholz H., Wang M.L., Gzhegotsky M., Lutsyk A., Matsuka G., Filonenko V., Wang L., Proud C.G., Parker P.J., Gout I.T.
Mol. Cell. Biol. 23:852-863(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-473, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-267; MET-368; VAL-420 AND MET-443.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016869 mRNA. Translation: BAA34402.1. Different initiation.
AB019245 mRNA. Translation: BAA37145.1.
AF076931 mRNA. Translation: AAD46063.1.
AF099739 mRNA. Translation: AAD20990.1.
AP003419 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74621.1.
BC000094 mRNA. Translation: AAH00094.3.
BC136564 mRNA. Translation: AAI36565.1.
PIRJE0377.
RefSeqNP_003943.2. NM_003952.2.
UniGeneHs.534345.

3D structure databases

ProteinModelPortalQ9UBS0.
SMRQ9UBS0. Positions 58-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112113. 16 interactions.
IntActQ9UBS0. 7 interactions.
MINTMINT-207158.
STRING9606.ENSP00000308413.

Chemistry

ChEMBLCHEMBL3111.
GuidetoPHARMACOLOGY1526.

PTM databases

PhosphoSiteQ9UBS0.

Polymorphism databases

DMDM296434560.

Proteomic databases

PaxDbQ9UBS0.
PRIDEQ9UBS0.

Protocols and materials databases

DNASU6199.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312629; ENSP00000308413; ENSG00000175634.
GeneID6199.
KEGGhsa:6199.
UCSCuc001old.3. human.

Organism-specific databases

CTD6199.
GeneCardsGC11P067195.
H-InvDBHIX0009859.
HGNCHGNC:10437. RPS6KB2.
HPACAB019404.
HPA010010.
MIM608939. gene.
neXtProtNX_Q9UBS0.
PharmGKBPA34852.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ9UBS0.
KOK04688.
OMATETSVNP.
PhylomeDBQ9UBS0.
TreeFamTF313438.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ9UBS0.

Gene expression databases

ArrayExpressQ9UBS0.
BgeeQ9UBS0.
CleanExHS_RPS6KB2.
GenevestigatorQ9UBS0.

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

GeneWikiRPS6KB2.
GenomeRNAi6199.
NextBio24077.
PROQ9UBS0.
SOURCESearch...

Entry information

Entry nameKS6B2_HUMAN
AccessionPrimary (citable) accession number: Q9UBS0
Secondary accession number(s): B2RMZ9, O94809, Q9UEC1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM