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UniProtKB/Swiss-Prot entry P23443


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KS6B1_HUMAN
Primary accession number P23443
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on October 11, 2004 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Ribosomal protein S6 kinase beta-1
Synonyms EC 2.7.11.1
Ribosomal protein S6 kinase I
S6K1
S6K
70 kDa ribosomal protein S6 kinase 1
p70 S6 kinase alpha
p70(S6K)-alpha
p70-S6K
P70S6K
p70-alpha
Gene name
Name: RPS6KB1
Synonyms: STK14A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION.
PubMed=1922062 [NCBI, ExPASy, EBI, Israel, Japan]
Grove J., Bonerjee P., Balasubramanyam A., Coffer P., Price D.J., Avruch J., Woodgett J.R.;
"Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino termini.";
Mol. Cell. Biol. 11:5541-5550(1991).
[2]
TISSUE SPECIFICITY.
DOI=10.1074/jbc.273.46.30061; PubMed=9804755 [NCBI, ExPASy, EBI, Israel, Japan]
Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D., Yonezawa K.;
"Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region.";
J. Biol. Chem. 273:30061-30064(1998).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; THR-444 AND SER-447, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; THR-444 AND SER-447, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
VARIANT [LARGE SCALE ANALYSIS] GLU-289.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[7]
VARIANTS [LARGE SCALE ANALYSIS] ILE-225; CYS-272; CYS-276 AND ALA-398.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M60724; AAA36410.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60725; AAA36411.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216132; -.
IPI00759649; -.
PIR A41687; A41687.
RefSeq NP_003152.1; -.
UniGene Hs.463642
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
ModBase P23443.
PTM databases
PhosphoSite P23443; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Pathway_Interaction_DB a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
igf1_pathway; IGF1 pathway.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il4_2pathway; IL4-mediated signaling events.
insulin_pathway; Insulin Pathway.
avb3_integrin_pathway; Integrins in angiogenesis.
mtor_4pathway; mTOR signaling pathway.
telomerasepathway; Regulation of Telomerase.
rxr_vdr_pathway; RXR and RAR hetrodimerization with other nuclear receptor.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
kitpathway; Signaling events mediated by Stem cell factor receptor (c-Kit).
tgfbrpathway; TGF-beta receptor signaling.
Reactome REACT_498; Signaling by Insulin receptor.
Organism-specific databases
GeneCards GC17P055325; -.
H-InvDB HIX0014049; -.
HGNC HGNC:10436; RPS6KB1.
GenAtlas RPS6KB1.
HPA CAB003838; -.
CAB018346; -.
MIM 608938; gene. [NCBI / EBI]
PharmGKB PA34851; -.
Gene expression databases
ArrayExpress P23443; -.
Bgee P23443; -.
CleanEx HS_RPS6KB1; -.
GermOnline ENSG00000108443; Homo sapiens.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0045202; Cellular component: synapse (inferred from electronic annotation from UniProtKB-SubCell).
GO:0019717; Cellular component: synaptosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000961; AGC-kinase_C.
IPR017892; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR016238; Ribosomal_S6_kinase.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000605; Ribsml_S6_kin_1; 1.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P23443; -.
Genome annotation databases
Ensembl ENSG00000108443; Homo sapiens. [Contig view]
GeneID 6198; -.
KEGG hsa:6198; -.
Phylogenomic databases
HOGENOM P23443; -.
HOVERGEN P23443; -.
OMA P23443; DELEEGX.
Other
NextBio 24073; -.
SOURCE RPS6KB1; Homo sapiens.
ProtoNet P23443.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; ATP-binding; Cell junction; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Synapse; Synaptosome; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   525  525     Ribosomal protein S6 kinase beta-1. PRO_0000024342
DOMAIN   91   352  262     Protein kinase. 
DOMAIN   353   423  71     AGC-kinase C-terminal. 
NP_BIND   97   105  9     ATP (By similarity). 
ACT_SITE   218   218        Proton acceptor (By similarity). 
BINDING   123   123        ATP (By similarity). 
MOD_RES   441   441        Phosphoserine. 
MOD_RES   444   444        Phosphothreonine. 
MOD_RES   447   447        Phosphoserine. 
VAR_SEQ   1    23        Missing (in isoform Alpha II). VSP_018839
VARIANT   225   225  1     M -> I. VAR_040639 
VARIANT   272   272  1     R -> C. VAR_040640 
VARIANT   276   276  1     W -> C. VAR_040641 
VARIANT   289   289  1     G -> E (in a colorectal cancer sample; somatic mutation). VAR_035628 
VARIANT   398   398  1     S -> A. VAR_040642 
Sequence information
Length: 525 AA [This is the length of the unprocessed precursor] Molecular weight: 59140 Da [This is the MW of the unprocessed precursor] CRC64: 2C3BA13CCDAF4AB3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRRRRRRDGF YPAPDFRDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG 

        70         80         90        100        110        120 
PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF 

       130        140        150        160        170        180 
AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL 

       190        200        210        220        230        240 
FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC 

       250        260        270        280        290        300 
KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK 

       310        320        330        340        350        360 
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL 

       370        380        390        400        410        420 
LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE 

       430        440        450        460        470        480 
SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK FSPGDFWGRG ASASTANPQT PVEYPMETSG 

       490        500        510        520 
IEQMDVTMSG EASAPLPIRQ PNSGPYKKQA FPMISKRPEH LRMNL 

P23443 in FASTA format

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