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O75676 (KS6A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal protein S6 kinase alpha-4

Short name=S6K-alpha-4
EC=2.7.11.1
Alternative name(s):
90 kDa ribosomal protein S6 kinase 4
Nuclear mitogen- and stress-activated protein kinase 2
Ribosomal protein kinase B
Short name=RSKB
Gene names
Name:RPS6KA4
Synonyms:MSK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Ref.1 Ref.6 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1

Cofactor

Magnesium. Ref.1

Enzyme regulation

Activated by phosphorylation at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-196, Ser-360 and Ser-365 by the activated C-terminal kinase domain By similarity. Ref.1

Subunit structure

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA4 associates with and phosphorylates the NF-kappa-B p65 subunit RELA.

Subcellular location

Nucleus Ref.1 Ref.6.

Post-translational modification

Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-737 and Ser-745 by the N-terminal kinase domain By similarity.

Miscellaneous

Enzyme activity requires the presence of both kinase domains By similarity. UniProtKB O75582

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 2 protein kinase domains.

Ontologies

Keywords
   Biological processInflammatory response
Stress response
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

histone H3-S10 phosphorylation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

histone H3-S28 phosphorylation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

histone phosphorylation

Traceable author statement PubMed 20018936. Source: BHF-UCL

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-1-mediated signaling pathway

Inferred from mutant phenotype PubMed 20018936. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of cytokine production

Traceable author statement Ref.8. Source: UniProtKB

positive regulation of CREB transcription factor activity

Traceable author statement Ref.8. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Traceable author statement Ref.8. Source: UniProtKB

positive regulation of histone acetylation

Inferred from mutant phenotype PubMed 20018936. Source: BHF-UCL

positive regulation of histone phosphorylation

Inferred from mutant phenotype PubMed 20018936. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20018936. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.6Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

mitogen-activated protein kinase p38 binding

Inferred from genetic interaction Ref.6. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

ribosomal protein S6 kinase activity

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAPK14Q165393EBI-73933,EBI-73946

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75676-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75676-2)

The sequence of this isoform differs from the canonical sequence as follows:
     401-406: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 772772Ribosomal protein S6 kinase alpha-4
PRO_0000086205

Regions

Domain33 – 301269Protein kinase 1
Domain302 – 37170AGC-kinase C-terminal
Domain411 – 674264Protein kinase 2
Nucleotide binding39 – 479ATP By similarity UniProtKB Q15418
Nucleotide binding417 – 4259ATP By similarity UniProtKB Q15418
Region725 – 77248Required for nuclear targeting and association with MAPK14

Sites

Active site1611Proton acceptor By similarity UniProtKB Q15418
Active site5301Proton acceptor By similarity UniProtKB Q15418
Binding site651ATP By similarity UniProtKB Q15418
Binding site4401ATP By similarity UniProtKB Q15418

Amino acid modifications

Modified residue1961Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
Modified residue3431Phosphoserine; by MAPK1, MAPK3 and MAPK14 Probable UniProtKB Q15418
Modified residue3471Phosphoserine Ref.9 Ref.11
Modified residue3601Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
Modified residue3651Phosphoserine; by autocatalysis By similarity
Modified residue5421Phosphothreonine Ref.11
Modified residue5681Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarity UniProtKB Q15418
Modified residue6341Phosphoserine Ref.9
Modified residue6781Phosphoserine Ref.9
Modified residue6871Phosphothreonine Ref.9 Ref.11
Modified residue7371Phosphoserine; by autocatalysis Probable UniProtKB Q15418
Modified residue7451Phosphoserine Ref.9

Natural variations

Alternative sequence401 – 4066Missing in isoform 2.
VSP_017733
Natural variant2361S → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.15
VAR_040632
Natural variant7581S → A. Ref.3 Ref.15
Corresponds to variant rs17857342 [ dbSNP | Ensembl ].
VAR_040633

Experimental info

Mutagenesis7091F → A: Strongly elevates basal activity. Ref.6
Sequence conflict4771L → P in BAD97281. Ref.3
Isoform 2:
Sequence conflict400 – 4012QQ → Q in BAD97281. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3606209693D0B5F3

FASTA77285,606
        10         20         30         40         50         60 
MGDEDDDESC AVELRITEAN LTGHEEKVSV ENFELLKVLG TGAYGKVFLV RKAGGHDAGK 

        70         80         90        100        110        120 
LYAMKVLRKA ALVQRAKTQE HTRTERSVLE LVRQAPFLVT LHYAFQTDAK LHLILDYVSG 

       130        140        150        160        170        180 
GEMFTHLYQR QYFKEAEVRV YGGEIVLALE HLHKLGIIYR DLKLENVLLD SEGHIVLTDF 

       190        200        210        220        230        240 
GLSKEFLTEE KERTFSFCGT IEYMAPEIIR SKTGHGKAVD WWSLGILLFE LLTGASPFTL 

       250        260        270        280        290        300 
EGERNTQAEV SRRILKCSPP FPPRIGPVAQ DLLQRLLCKD PKKRLGAGPQ GAQEVRNHPF 

       310        320        330        340        350        360 
FQGLDWVALA ARKIPAPFRP QIRSELDVGN FAEEFTRLEP VYSPPGSPPP GDPRIFQGYS 

       370        380        390        400        410        420 
FVAPSILFDH NNAVMTDGLE APGAGDRPGR AAVARSAMMQ DSPFFQQYEL DLREPALGQG 

       430        440        450        460        470        480 
SFSVCRRCRQ RQSGQEFAVK ILSRRLEANT QREVAALRLC QSHPNVVNLH EVHHDQLHTY 

       490        500        510        520        530        540 
LVLELLRGGE LLEHIRKKRH FSESEASQIL RSLVSAVSFM HEEAGVVHRD LKPENILYAD 

       550        560        570        580        590        600 
DTPGAPVKII DFGFARLRPQ SPGVPMQTPC FTLQYAAPEL LAQQGYDESC DLWSLGVILY 

       610        620        630        640        650        660 
MMLSGQVPFQ GASGQGGQSQ AAEIMCKIRE GRFSLDGEAW QGVSEEAKEL VRGLLTVDPA 

       670        680        690        700        710        720 
KRLKLEGLRG SSWLQDGSAR SSPPLRTPDV LESSGPAVRS GLNATFMAFN RGKREGFFLK 

       730        740        750        760        770 
SVENAPLAKR RKQKLRSATA SRRGSPAPAN PGRAPVASKG APRRANGPLP PS 

« Hide

Isoform 2 [UniParc].

Checksum: DE27817E248DA71E
Show »

FASTA76684,884

References

« Hide 'large scale' references
[1]"RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)."
Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.
J. Biol. Chem. 273:29661-29671(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK14; MAPK1 AND MAPK3, SUBCELLULAR LOCATION.
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Synovium.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-758.
Tissue: Brain.
[4]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].
[5]"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-727 (ISOFORM 2).
[6]"C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB)."
Tomas-Zuber M., Mary J.L., Lamour F., Bur D., Lesslauer W.
J. Biol. Chem. 276:5892-5899(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK14, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-709.
[7]"MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14."
Soloaga A., Thomson S., Wiggin G.R., Rampersaud N., Dyson M.H., Hazzalin C.A., Mahadevan L.C., Arthur J.S.
EMBO J. 22:2788-2797(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3 AND HMGN1/HMG14.
[8]"MSK activation and physiological roles."
Arthur J.S.
Front. Biosci. 13:5866-5879(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-634; SER-678; THR-687 AND SER-745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; THR-542 AND THR-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The versatile role of MSKs in transcriptional regulation."
Vermeulen L., Vanden Berghe W., Beck I.M., De Bosscher K., Haegeman G.
Trends Biochem. Sci. 34:311-318(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-236 AND ALA-758.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010119 mRNA. Translation: CAA09009.1.
AK223561 mRNA. Translation: BAD97281.1.
AK292163 mRNA. Translation: BAF84852.1.
CH471076 Genomic DNA. Translation: EAW74260.1.
AF074715 mRNA. Translation: AAC67395.1.
RefSeqNP_001006945.1. NM_001006944.1.
NP_003933.1. NM_003942.2.
UniGeneHs.105584.

3D structure databases

ProteinModelPortalO75676.
SMRO75676. Positions 13-365, 369-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114468. 12 interactions.
IntActO75676. 5 interactions.
MINTMINT-7944429.
STRING9606.ENSP00000333896.

Chemistry

BindingDBO75676.
ChEMBLCHEMBL3125.
GuidetoPHARMACOLOGY1524.

PTM databases

PhosphoSiteO75676.

Proteomic databases

PaxDbO75676.
PRIDEO75676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334205; ENSP00000333896; ENSG00000162302. [O75676-1]
ENST00000530504; ENSP00000432945; ENSG00000162302.
GeneID8986.
KEGGhsa:8986.
UCSCuc001oad.3. human. [O75676-2]
uc001oae.3. human. [O75676-1]

Organism-specific databases

CTD8986.
GeneCardsGC11P064126.
HGNCHGNC:10433. RPS6KA4.
HPACAB008649.
HPA023225.
MIM603606. gene.
neXtProtNX_O75676.
PharmGKBPA34848.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidO75676.
KOK16510.
OMATYVNATY.
PhylomeDBO75676.
TreeFamTF313438.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkO75676.

Gene expression databases

ArrayExpressO75676.
BgeeO75676.
CleanExHS_RPS6KA4.
GenevestigatorO75676.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS6KA4.
GenomeRNAi8986.
NextBio33697.
PROO75676.
SOURCESearch...

Entry information

Entry nameKS6A4_HUMAN
AccessionPrimary (citable) accession number: O75676
Secondary accession number(s): A8K7Z8, O75585, Q53ES8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 139 of the entry and version 1 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