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Q15349 (KS6A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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-2

Short name=S6K-alpha-2
EC=2.7.11.1
Alternative name(s):
90 kDa ribosomal protein S6 kinase 2
Short name=p90-RSK 2
Short name=p90RSK2
MAP kinase-activated protein kinase 1c
Short name=MAPK-activated protein kinase 1c
Short name=MAPKAP kinase 1c
Short name=MAPKAPK-1c
Ribosomal S6 kinase 3
Short name=RSK-3
pp90RSK3
Gene names
Name:RPS6KA2
Synonyms:MAPKAPK1C, RSK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells. Ref.1 Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-570 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-377, allowing binding of PDPK1, which in turn phosphorylates Ser-218 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD. Ref.7

Subunit structure

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation By similarity.

Subcellular location

Nucleus. Cytoplasm Ref.1.

Tissue specificity

Widely expressed with higher expression in lung, skeletal muscle, brain, uterus, ovary, thyroid and prostate. Ref.1 Ref.8

Post-translational modification

Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 By similarity. Ref.7

N-terminal myristoylation results in an activated kinase in the absence of added growth factors By similarity.

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.

Sequence caution

The sequence AAC82496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAD92353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG53121.1 differs from that shown. Reason: Frameshift at position 527.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

brain renin-angiotensin system

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

cellular response to carbohydrate stimulus

Inferred from electronic annotation. Source: Ensembl

heart contraction

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement Ref.1Ref.6. Source: ProtInc

negative regulation of cell cycle

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

oocyte maturation

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

regulation of protein processing

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement Ref.1. Source: ProtInc

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 16810323. Source: IntAct

protein serine/threonine kinase activity

Traceable author statement Ref.1. Source: ProtInc

ribosomal protein S6 kinase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15349-1)

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: Q15349-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELW...ACKTKVAGSV
Note: No experimental confirmation available.
Isoform 3 (identifier: Q15349-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELWKKIEVEPMEIETTEEDLNLDVEPTTEDTAE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 733733Ribosomal protein S6 kinase alpha-2
PRO_0000086201

Regions

Domain59 – 318260Protein kinase 1
Domain319 – 38870AGC-kinase C-terminal
Domain415 – 672258Protein kinase 2
Nucleotide binding65 – 739ATP By similarity
Nucleotide binding421 – 4299ATP By similarity

Sites

Active site1841Proton acceptor By similarity
Active site5321Proton acceptor By similarity
Binding site911ATP By similarity
Binding site4441ATP By similarity

Amino acid modifications

Modified residue2181Phosphoserine; by PDPK1 Ref.7
Modified residue3771Phosphoserine Ref.12
Cross-link630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVGPATEDTAE EGKSDSAACKTKVAGSV in isoform 2.
VSP_017732
Alternative sequence1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVEPTTEDTAE in isoform 3.
VSP_041836
Natural variant3111E → K in a metastatic melanoma sample; somatic mutation. Ref.13
VAR_040627
Natural variant7321R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.13
VAR_040628

Experimental info

Sequence conflict2561S → A in AAC82496. Ref.6
Sequence conflict2691A → S in AAC82496. Ref.6
Sequence conflict3391V → L in CAA59427. Ref.1
Sequence conflict3391V → L in AAC82496. Ref.6
Sequence conflict4471D → G in AAC82496. Ref.6
Isoform 3:
Sequence conflict321E → G in BAG53121. Ref.3
Sequence conflict341T → A in BAG53121. Ref.3

Sequences

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

Last modified March 21, 2006. Version 2.
Checksum: 087CFB819A313760

FASTA73383,239
        10         20         30         40         50         60 
MDLSMKKFAV RRFFSVYLRR KSRSKSSSLS RLEEEGVVKE IDISHHVKEG FEKADPSQFE 

        70         80         90        100        110        120 
LLKVLGQGSY GKVFLVRKVK GSDAGQLYAM KVLKKATLKV RDRVRSKMER DILAEVNHPF 

       130        140        150        160        170        180 
IVKLHYAFQT EGKLYLILDF LRGGDLFTRL SKEVMFTEED VKFYLAELAL ALDHLHSLGI 

       190        200        210        220        230        240 
IYRDLKPENI LLDEEGHIKI TDFGLSKEAI DHDKRAYSFC GTIEYMAPEV VNRRGHTQSA 

       250        260        270        280        290        300 
DWWSFGVLMF EMLTGSLPFQ GKDRKETMAL ILKAKLGMPQ FLSGEAQSLL RALFKRNPCN 

       310        320        330        340        350        360 
RLGAGIDGVE EIKRHPFFVT IDWNTLYRKE IKPPFKPAVG RPEDTFHFDP EFTARTPTDS 

       370        380        390        400        410        420 
PGVPPSANAH HLFRGFSFVA SSLIQEPSQQ DLHKVPVHPI VQQLHGNNIH FTDGYEIKED 

       430        440        450        460        470        480 
IGVGSYSVCK RCVHKATDTE YAVKIIDKSK RDPSEEIEIL LRYGQHPNII TLKDVYDDGK 

       490        500        510        520        530        540 
FVYLVMELMR GGELLDRILR QRYFSEREAS DVLCTITKTM DYLHSQGVVH RDLKPSNILY 

       550        560        570        580        590        600 
RDESGSPESI RVCDFGFAKQ LRAGNGLLMT PCYTANFVAP EVLKRQGYDA ACDIWSLGIL 

       610        620        630        640        650        660 
LYTMLAGFTP FANGPDDTPE EILARIGSGK YALSGGNWDS ISDAAKDVVS KMLHVDPHQR 

       670        680        690        700        710        720 
LTAMQVLKHP WVVNREYLSP NQLSRQDVHL VKGAMAATYF ALNRTPQAPR LEPVLSSNLA 

       730 
QRRGMKRLTS TRL 

« Hide

Isoform 2 [UniParc].

Checksum: 1C30759D0B188D4A
Show »

FASTA75885,532
Isoform 3 [UniParc].

Checksum: 146D3569D1C9A193
Show »

FASTA74184,014

References

« Hide 'large scale' references
[1]"RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation."
Zhao Y., Bjoerbaek C., Weremowicz S., Morton C.C., Moller D.E.
Mol. Cell. Biol. 15:4353-4363(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]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).
Tissue: Brain.
[3]"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 3).
Tissue: Brain.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Muscle.
[6]"Human rsk isoforms: cloning and characterization of tissue-specific expression."
Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.
Am. J. Physiol. 266:C351-C359(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-540 (ISOFORM 1).
[7]"90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1."
Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M.
J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-218.
[8]"RPS6KA2, a putative tumour suppressor gene at 6q27 in sporadic epithelial ovarian cancer."
Bignone P.A., Lee K.Y., Liu Y., Emilion G., Finch J., Soosay A.E., Charnock F.M., Beck S., Dunham I., Mungall A.J., Ganesan T.S.
Oncogene 26:683-700(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TUMORIGENESIS, TISSUE SPECIFICITY.
[9]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-630.
Tissue: Mammary cancer.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"The RSK family of kinases: emerging roles in cellular signalling."
Anjum R., Blenis J.
Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[12]"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-377, 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] LYS-311 AND GLN-732.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85106 mRNA. Translation: CAA59427.1.
AB209116 mRNA. Translation: BAD92353.1. Different initiation.
AK095751 mRNA. Translation: BAG53121.1. Frameshift.
AL022069, Z98049 Genomic DNA. Translation: CAI19651.1.
AL023775 Genomic DNA. No translation available.
AL159163 Genomic DNA. No translation available.
Z98049, AL022069 Genomic DNA. Translation: CAI20579.1.
BC002363 mRNA. Translation: AAH02363.1.
L07598 mRNA. Translation: AAC82496.1. Different initiation.
CCDSCCDS34570.1. [Q15349-3]
CCDS5294.1. [Q15349-1]
PIRA57459.
RefSeqNP_001006933.1. NM_001006932.1. [Q15349-3]
NP_066958.2. NM_021135.4. [Q15349-1]
UniGeneHs.655277.

3D structure databases

ProteinModelPortalQ15349.
SMRQ15349. Positions 24-704.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112110. 13 interactions.
DIPDIP-295N.
IntActQ15349. 10 interactions.
MINTMINT-1542928.
STRING9606.ENSP00000386050.

Chemistry

BindingDBQ15349.
ChEMBLCHEMBL3906.
GuidetoPHARMACOLOGY1529.

PTM databases

PhosphoSiteQ15349.

Polymorphism databases

DMDM90110031.

2D gel databases

REPRODUCTION-2DPAGEQ15349.

Proteomic databases

MaxQBQ15349.
PaxDbQ15349.
PRIDEQ15349.

Protocols and materials databases

DNASU6196.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265678; ENSP00000265678; ENSG00000071242. [Q15349-1]
ENST00000503859; ENSP00000427015; ENSG00000071242. [Q15349-3]
GeneID6196.
KEGGhsa:6196.
UCSCuc003qvb.1. human. [Q15349-1]
uc003qvc.1. human. [Q15349-3]

Organism-specific databases

CTD6196.
GeneCardsGC06M166822.
HGNCHGNC:10431. RPS6KA2.
HPACAB026243.
HPA045061.
HPA054237.
MIM601685. gene.
neXtProtNX_Q15349.
PharmGKBPA34846.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
KOK04373.
OrthoDBEOG7B8S38.
PhylomeDBQ15349.
TreeFamTF313438.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_13685. Neuronal System.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ15349.

Gene expression databases

ArrayExpressQ15349.
BgeeQ15349.
CleanExHS_RPS6KA2.
GenevestigatorQ15349.

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

ChiTaRSRPS6KA2. human.
GeneWikiRPS6KA2.
GenomeRNAi6196.
NextBio24063.
PROQ15349.
SOURCESearch...

Entry information

Entry nameKS6A2_HUMAN
AccessionPrimary (citable) accession number: Q15349
Secondary accession number(s): B3KTK9 expand/collapse secondary AC list , Q15419, Q59GJ3, Q5TI68, Q96J38, Q9UJN5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 150 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 6

Human chromosome 6: entries, gene names and cross-references to MIM