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UniProtKB/Swiss-Prot entry Q15418


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

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Entry information
Entry name KS6A1_HUMAN
Primary accession number Q15418
Secondary accession numbers Q5SVM5 Q5SVM8 Q5SVM9 Q96C05 Q9BQK2
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on April 16, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 96)
Name and origin of the protein
Protein name Ribosomal protein S6 kinase alpha-1
Synonyms S6K-alpha 1
EC 2.7.11.1
90 kDa ribosomal protein S6 kinase 1
p90-RSK 1
pp90RSK1
p90S6K
Ribosomal S6 kinase 1
RSK-1
MAP kinase-activated protein kinase 1a
MAPKAPK1A
Gene name
Name: RPS6KA1
Synonyms: RSK1
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 VARIANT THR-335.
PubMed=8141249 [NCBI, ExPASy, EBI, Israel, Japan]
Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.;
"Human rsk isoforms: cloning and characterization of tissue-specific expression.";
Am. J. Physiol. 266:C351-C359(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION.
DOI=10.1093/emboj/17.15.4426; PubMed=9687510 [NCBI, ExPASy, EBI, Israel, Japan]
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
EMBO J. 17:4426-4441(1998).
[5]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.
DOI=10.1074/jbc.273.3.1496; PubMed=9430688 [NCBI, ExPASy, EBI, Israel, Japan]
Dalby K.N., Morrice N., Caudwell F.B., Avruch J., Cohen P.;
"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.";
J. Biol. Chem. 273:1496-1505(1998).
[6]
INTERACTION WITH MAPK1 OR MAPK3.
DOI=10.1128/MCB.23.14.4796-4804.2003; PubMed=12832467 [NCBI, ExPASy, EBI, Israel, Japan]
Roux P.P., Richards S.A., Blenis J.;
"Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.";
Mol. Cell. Biol. 23:4796-4804(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359 AND SER-363, 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-225; THR-359; SER-363; SER-369 AND SER-380, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369; SER-380 AND THR-573, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369; SER-380 AND THR-573, 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).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
VARIANT [LARGE SCALE ANALYSIS] THR-335.
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
L07597; AAC82497.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109743; CAC36348.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627313; CAI14647.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627313; CAI14648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL627313; CAI14649.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014966; AAH14966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00017305; -.
PIR I51901; I51901.
RefSeq NP_001006666.1; -.
NP_002944.2; -.
UniGene Hs.149957
3D structure databases
PDB
2Z7Q; X-ray; 2.00 A; A=33-353.[ExPASy / RCSB / EBI]
2Z7R; X-ray; 2.00 A; A=33-353.[ExPASy / RCSB / EBI]
2Z7S; X-ray; 2.10 A; A=33-353.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2Z7Q; -.
2Z7R; -.
2Z7S; -.
ModBase Q15418.
Protein-protein interaction databases
IntAct Q15418; 1.
PTM databases
PhosphoSite Q15418; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Pathway_Interaction_DB fgf_pathway; FGF signaling pathway.
mapktrkpathway; Trk receptor signaling mediated by the MAPK pathway.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC01P026728; -.
H-InvDB HIX0022890; -.
HGNC HGNC:10430; RPS6KA1.
GenAtlas RPS6KA1.
HPA CAB003852; -.
HPA007981; -.
MIM 601684; gene. [NCBI / EBI]
PharmGKB PA34845; -.
Gene expression databases
ArrayExpress Q15418; -.
Bgee Q15418; -.
CleanEx HS_RPS6KA1; -.
GermOnline ENSG00000117676; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from experiment from Reactome).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007243; Biological process: protein kinase cascade (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000961; AGC-kinase_C.
IPR017892; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR016239; Ribosomal_S6_kinase_II.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 2.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000606; Ribsml_S6_kin_2; 1.
ProDom PD000001; Prot_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00133; S_TK_X; 1.
SM00220; S_TKc; 2.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 2.
PS50011; PROTEIN_KINASE_DOM; 2.
PS00108; PROTEIN_KINASE_ST; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q15418; -.
Genome annotation databases
Ensembl ENSG00000117676; Homo sapiens. [Contig view]
GeneID 6195; -.
KEGG hsa:6195; -.
Phylogenomic databases
HOVERGEN Q15418; -.
Other
BindingDB Q15418; -.
NextBio 24057; -.
SOURCE RPS6KA1; Homo sapiens.
ProtoNet Q15418.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Repeat; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   735  735     Ribosomal protein S6 kinase alpha-1. PRO_0000086198
DOMAIN   62   321  260     Protein kinase 1. 
DOMAIN   322   391  70     AGC-kinase C-terminal. 
DOMAIN   418   675  258     Protein kinase 2. 
NP_BIND   68    76  9     ATP (By similarity). 
NP_BIND   424   432  9     ATP (By similarity). 
ACT_SITE   187   187        Proton acceptor (By similarity). 
ACT_SITE   535   535        Proton acceptor (By similarity). 
BINDING   94    94        ATP (By similarity). 
BINDING   447   447        ATP (By similarity). 
MOD_RES   221   221        Phosphoserine. 
MOD_RES   225   225        Phosphothreonine. 
MOD_RES   348   348        Phosphothreonine. 
MOD_RES   359   359        Phosphothreonine. 
MOD_RES   363   363        Phosphoserine. 
MOD_RES   369   369        Phosphoserine. 
MOD_RES   380   380        Phosphoserine; by autocatalysis. 
MOD_RES   573   573        Phosphothreonine. 
MOD_RES   732   732        Phosphoserine. 
VARIANT   335   335  1     K -> T (in dbSNP:rs2229712 [NCBI]). VAR_021864 [3D]
HELIX   59    61  3      
STRAND   62    71  10      
STRAND   74    81  8      
STRAND   83    86  4      
STRAND   90    96  7      
STRAND   127   133  7      
STRAND   136   141  6      
HELIX   149   156  8      
HELIX   161   180  20      
HELIX   190   192  3      
STRAND   193   195  3      
STRAND   197   199  3      
STRAND   201   203  3      
HELIX   226   228  3      
HELIX   231   234  4      
HELIX   241   257  17      
HELIX   267   276  10      
HELIX   287   296  10      
TURN   301   303  3      
STRAND   307   310  4      
HELIX   312   316  5      
HELIX   319   321  3      
HELIX   326   330  5      
Sequence information
Length: 735 AA [This is the length of the unprocessed precursor] Molecular weight: 82723 Da [This is the MW of the unprocessed precursor] CRC64: 765731A4442A53DF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV KAGSEKADPS 

        70         80         90        100        110        120 
HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT LKVRDRVRTK MERDILADVN 

       130        140        150        160        170        180 
HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS 

       190        200        210        220        230        240 
LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS 

       250        260        270        280        290        300 
HSADWWSYGV LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN 

       310        320        330        340        350        360 
PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY FDTEFTSRTP 

       370        380        390        400        410        420 
KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL HSVVQQLHGK NLVFSDGYVV 

       430        440        450        460        470        480 
KETIGVGSYS ECKRCVHKAT NMEYAVKVID KSKRDPSEEI EILLRYGQHP NIITLKDVYD 

       490        500        510        520        530        540 
DGKHVYLVTE LMRGGELLDK ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN 

       550        560        570        580        590        600 
ILYVDESGNP ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL 

       610        620        630        640        650        660 
GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD LVSKMLHVDP 

       670        680        690        700        710        720 
HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA TYSALNSSKP TPQLKPIESS 

       730 
ILAQRRVRKL PSTTL 

Q15418 in FASTA format

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