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UniProtKB/Swiss-Prot entry Q9UK32


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

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Entry information
Entry name KS6A6_HUMAN
Primary accession number Q9UK32
Secondary accession numbers Q6FHX2 Q8WX28 Q9H4S6
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 76)
Name and origin of the protein
Protein name Ribosomal protein S6 kinase alpha-6
Synonyms S6K-alpha 6
EC 2.7.11.1
90 kDa ribosomal protein S6 kinase 6
p90-RSK 6
Ribosomal S6 kinase 4
RSK-4
pp90RSK4
Gene name
Name: RPS6KA6
Synonyms: RSK4
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].
DOI=10.1006/geno.1999.6004; PubMed=10644430 [NCBI, ExPASy, EBI, Israel, Japan]
Yntema H.G., van den Helm B., Kissing J., van Duijnhoven G., Poppelaars F., Chelly J., Moraine C., Fryns J.-P., Hamel B.C.J., Heilbronner H., Pander H.-J., Brunner H.G., Ropers H.-H., Cremers F.P.M., van Bokhoven H.;
"A novel ribosomal S6-kinase (RSK4; RPS6KA6) is commonly deleted in patients with complex X-linked mental retardation.";
Genomics 62:332-343(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, 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).
[5]
VARIANTS [LARGE SCALE ANALYSIS] CYS-140; THR-258 AND ASN-692.
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
AF184965; AAF13190.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536566; CAG38803.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389887; CAC16111.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL354653; CAC16111.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL354653; CAD13486.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL389887; CAD13486.2; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00007123; -.
RefSeq NP_055311.1; -.
UniGene Hs.368153
3D structure databases
HSSP P49137; 1KWP. [HSSP ENTRY / PDB]
ModBase Q9UK32.
Protein-protein interaction databases
IntAct Q9UK32; 2.
PTM databases
PhosphoSite Q9UK32; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Organism-specific databases
GeneCards GC0XM083125; -.
HGNC HGNC:10435; RPS6KA6.
GenAtlas RPS6KA6.
HPA HPA002852; -.
HPA003904; -.
MIM 300303; gene. [NCBI / EBI]
PharmGKB PA34850; -.
Gene expression databases
ArrayExpress Q9UK32; -.
Bgee Q9UK32; -.
CleanEx HS_RPS6KA6; -.
GermOnline ENSG00000072133; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from HPA).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from HPA).
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:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0007417; Biological process: central nervous system development (traceable author statement from ProtInc).
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 Q9UK32; -.
Genome annotation databases
Ensembl ENSG00000072133; Homo sapiens. [Contig view]
GeneID 27330; -.
KEGG hsa:27330; -.
Phylogenomic databases
HOGENOM Q9UK32; -.
HOVERGEN Q9UK32; -.
OMA Q9UK32; TPITSAN.
Other
NextBio 50372; -.
SOURCE RPS6KA6; Homo sapiens.
ProtoNet Q9UK32.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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   745  745     Ribosomal protein S6 kinase alpha-6. PRO_0000086209
DOMAIN   73   330  258     Protein kinase 1. 
DOMAIN   331   400  70     AGC-kinase C-terminal. 
DOMAIN   426   683  258     Protein kinase 2. 
NP_BIND   79    87  9     ATP (By similarity). 
NP_BIND   432   440  9     ATP (By similarity). 
ACT_SITE   198   198        Proton acceptor (By similarity). 
ACT_SITE   543   543        Proton acceptor (By similarity). 
BINDING   105   105        ATP (By similarity). 
BINDING   455   455        ATP (By similarity). 
MOD_RES   232   232        Phosphoserine. 
MOD_RES   368   368        Phosphothreonine (By similarity). 
MOD_RES   372   372        Phosphoserine (By similarity). 
MOD_RES   389   389        Phosphoserine (By similarity). 
MOD_RES   581   581        Phosphothreonine (By similarity). 
MOD_RES   742   742        Phosphoserine (By similarity). 
VARIANT   140   140  1     Y -> C (in a lung large cell carcinoma sample; somatic mutation). VAR_040637 [3D]
VARIANT   258   258  1     S -> T (in a lung adenocarcinoma sample; somatic mutation). VAR_040638 [3D]
VARIANT   692   692  1     D -> N (in dbSNP:rs6616890 [NCBI]). VAR_030670 
CONFLICT   116   116        D -> G (in Ref. 2; CAG38803). 
CONFLICT   295   295        F -> L (in Ref. 2; CAG38803). 
CONFLICT   341   341        R -> G (in Ref. 2; CAG38803). 
Sequence information
Length: 745 AA [This is the length of the unprocessed precursor] Molecular weight: 83872 Da [This is the MW of the unprocessed precursor] CRC64: 5EC5AB2FA1C19DE8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLPFAPQDEP WDREMEVFSG GGASSGEVNG LKMVDEPMEE GEADSCHDEG VVKEIPITHH 

        70         80         90        100        110        120 
VKEGYEKADP AQFELLKVLG QGSFGKVFLV RKKTGPDAGQ LYAMKVLKKA SLKVRDRVRT 

       130        140        150        160        170        180 
KMERDILVEV NHPFIVKLHY AFQTEGKLYL ILDFLRGGDV FTRLSKEVLF TEEDVKFYLA 

       190        200        210        220        230        240 
ELALALDHLH QLGIVYRDLK PENILLDEIG HIKLTDFGLS KESVDQEKKA YSFCGTVEYM 

       250        260        270        280        290        300 
APEVVNRRGH SQSADWWSYG VLMFEMLTGT LPFQGKDRNE TMNMILKAKL GMPQFLSAEA 

       310        320        330        340        350        360 
QSLLRMLFKR NPANRLGSEG VEEIKRHLFF ANIDWDKLYK REVQPPFKPA SGKPDDTFCF 

       370        380        390        400        410        420 
DPEFTAKTPK DSPGLPASAN AHQLFKGFSF VATSIAEEYK ITPITSANVL PIVQINGNAA 

       430        440        450        460        470        480 
QFGEVYELKE DIGVGSYSVC KRCIHATTNM EFAVKIIDKS KRDPSEEIEI LMRYGQHPNI 

       490        500        510        520        530        540 
ITLKDVFDDG RYVYLVTDLM KGGELLDRIL KQKCFSEREA SDILYVISKT VDYLHCQGVV 

       550        560        570        580        590        600 
HRDLKPSNIL YMDESASADS IRICDFGFAK QLRGENGLLL TPCYTANFVA PEVLMQQGYD 

       610        620        630        640        650        660 
AACDIWSLGV LFYTMLAGYT PFANGPNDTP EEILLRIGNG KFSLSGGNWD NISDGAKDLL 

       670        680        690        700        710        720 
SHMLHMDPHQ RYTAEQILKH SWITHRDQLP NDQPKRNDVS HVVKGAMVAT YSALTHKTFQ 

       730        740 
PVLEPVAASS LAQRRSMKKR TSTGL 

Q9UK32 in FASTA format

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