Q15349 (KS6A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	733 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-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_component	cytoplasm 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_function	ATP 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

With	Entry	#Exp.	IntAct	Notes
BRAF	P15056	2	EBI-1384149,EBI-365980
PRKCE	Q02156	2	EBI-1384149,EBI-706254

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 733	733	Ribosomal protein S6 kinase alpha-2		PRO_0000086201
Regions
	Domain	59 – 318	260	Protein kinase 1
	Domain	319 – 388	70	AGC-kinase C-terminal
	Domain	415 – 672	258	Protein kinase 2
	Nucleotide binding	65 – 73	9	ATP By similarity
	Nucleotide binding	421 – 429	9	ATP By similarity
Sites
	Active site	184	1	Proton acceptor By similarity
	Active site	532	1	Proton acceptor By similarity
	Binding site	91	1	ATP By similarity
	Binding site	444	1	ATP By similarity
Amino acid modifications
	Modified residue	218	1	Phosphoserine; by PDPK1 Ref.7
	Modified residue	377	1	Phosphoserine Ref.12
	Cross-link	630		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Natural variations
	Alternative sequence	1 – 32	32	MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVGPATEDTAE EGKSDSAACKTKVAGSV in isoform 2.		VSP_017732
	Alternative sequence	1 – 32	32	MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVEPTTEDTAE in isoform 3.		VSP_041836
	Natural variant	311	1	E → K in a metastatic melanoma sample; somatic mutation. Ref.13		VAR_040627
	Natural variant	732	1	R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.13		VAR_040628
Experimental info
	Sequence conflict	256	1	S → A in AAC82496. Ref.6
	Sequence conflict	269	1	A → S in AAC82496. Ref.6
	Sequence conflict	339	1	V → L in CAA59427. Ref.1
	Sequence conflict	339	1	V → L in AAC82496. Ref.6
	Sequence conflict	447	1	D → G in AAC82496. Ref.6
Isoform 3:
	Sequence conflict	32	1	E → G in BAG53121. Ref.3
	Sequence conflict	34	1	T → A in BAG53121. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 21, 2006. Version 2. Checksum: 087CFB819A313760	FASTA	733	83,239
	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
	Isoform 2 [UniParc]. Checksum: 1C30759D0B188D4A	FASTA	758	85,532
	10 20 30 40 50 60 MPIAQLLELW KKIEVEPMEI ETTEEDLNLD VGPATEDTAE EGKSDSAACK TKVAGSVEEE 70 80 90 100 110 120 GVVKEIDISH HVKEGFEKAD PSQFELLKVL GQGSYGKVFL VRKVKGSDAG QLYAMKVLKK 130 140 150 160 170 180 ATLKVRDRVR SKMERDILAE VNHPFIVKLH YAFQTEGKLY LILDFLRGGD LFTRLSKEVM 190 200 210 220 230 240 FTEEDVKFYL AELALALDHL HSLGIIYRDL KPENILLDEE GHIKITDFGL SKEAIDHDKR 250 260 270 280 290 300 AYSFCGTIEY MAPEVVNRRG HTQSADWWSF GVLMFEMLTG SLPFQGKDRK ETMALILKAK 310 320 330 340 350 360 LGMPQFLSGE AQSLLRALFK RNPCNRLGAG IDGVEEIKRH PFFVTIDWNT LYRKEIKPPF 370 380 390 400 410 420 KPAVGRPEDT FHFDPEFTAR TPTDSPGVPP SANAHHLFRG FSFVASSLIQ EPSQQDLHKV 430 440 450 460 470 480 PVHPIVQQLH GNNIHFTDGY EIKEDIGVGS YSVCKRCVHK ATDTEYAVKI IDKSKRDPSE 490 500 510 520 530 540 EIEILLRYGQ HPNIITLKDV YDDGKFVYLV MELMRGGELL DRILRQRYFS EREASDVLCT 550 560 570 580 590 600 ITKTMDYLHS QGVVHRDLKP SNILYRDESG SPESIRVCDF GFAKQLRAGN GLLMTPCYTA 610 620 630 640 650 660 NFVAPEVLKR QGYDAACDIW SLGILLYTML AGFTPFANGP DDTPEEILAR IGSGKYALSG 670 680 690 700 710 720 GNWDSISDAA KDVVSKMLHV DPHQRLTAMQ VLKHPWVVNR EYLSPNQLSR QDVHLVKGAM 730 740 750 AATYFALNRT PQAPRLEPVL SSNLAQRRGM KRLTSTRL
	Isoform 3 [UniParc]. Checksum: 146D3569D1C9A193	FASTA	741	84,014
	10 20 30 40 50 60 MPIAQLLELW KKIEVEPMEI ETTEEDLNLD VEPTTEDTAE EEEGVVKEID ISHHVKEGFE 70 80 90 100 110 120 KADPSQFELL KVLGQGSYGK VFLVRKVKGS DAGQLYAMKV LKKATLKVRD RVRSKMERDI 130 140 150 160 170 180 LAEVNHPFIV KLHYAFQTEG KLYLILDFLR GGDLFTRLSK EVMFTEEDVK FYLAELALAL 190 200 210 220 230 240 DHLHSLGIIY RDLKPENILL DEEGHIKITD FGLSKEAIDH DKRAYSFCGT IEYMAPEVVN 250 260 270 280 290 300 RRGHTQSADW WSFGVLMFEM LTGSLPFQGK DRKETMALIL KAKLGMPQFL SGEAQSLLRA 310 320 330 340 350 360 LFKRNPCNRL GAGIDGVEEI KRHPFFVTID WNTLYRKEIK PPFKPAVGRP EDTFHFDPEF 370 380 390 400 410 420 TARTPTDSPG VPPSANAHHL FRGFSFVASS LIQEPSQQDL HKVPVHPIVQ QLHGNNIHFT 430 440 450 460 470 480 DGYEIKEDIG VGSYSVCKRC VHKATDTEYA VKIIDKSKRD PSEEIEILLR YGQHPNIITL 490 500 510 520 530 540 KDVYDDGKFV YLVMELMRGG ELLDRILRQR YFSEREASDV LCTITKTMDY LHSQGVVHRD 550 560 570 580 590 600 LKPSNILYRD ESGSPESIRV CDFGFAKQLR AGNGLLMTPC YTANFVAPEV LKRQGYDAAC 610 620 630 640 650 660 DIWSLGILLY TMLAGFTPFA NGPDDTPEEI LARIGSGKYA LSGGNWDSIS DAAKDVVSKM 670 680 690 700 710 720 LHVDPHQRLT AMQVLKHPWV VNREYLSPNQ LSRQDVHLVK GAMAATYFAL NRTPQAPRLE 730 740 PVLSSNLAQR RGMKRLTSTR L

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
CCDS	CCDS34570.1. [Q15349-3] CCDS5294.1. [Q15349-1]
PIR	A57459.
RefSeq	NP_001006933.1. NM_001006932.1. [Q15349-3] NP_066958.2. NM_021135.4. [Q15349-1]
UniGene	Hs.655277.
3D structure databases
ProteinModelPortal	Q15349.
SMR	Q15349. Positions 24-704.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	112110. 13 interactions.
DIP	DIP-295N.
IntAct	Q15349. 10 interactions.
MINT	MINT-1542928.
STRING	9606.ENSP00000386050.
Chemistry
BindingDB	Q15349.
ChEMBL	CHEMBL3906.
GuidetoPHARMACOLOGY	1529.
PTM databases
PhosphoSite	Q15349.
Polymorphism databases
DMDM	90110031.
2D gel databases
REPRODUCTION-2DPAGE	Q15349.
Proteomic databases
MaxQB	Q15349.
PaxDb	Q15349.
PRIDE	Q15349.
Protocols and materials databases
DNASU	6196.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265678; ENSP00000265678; ENSG00000071242. [Q15349-1] ENST00000503859; ENSP00000427015; ENSG00000071242. [Q15349-3]
GeneID	6196.
KEGG	hsa:6196.
UCSC	uc003qvb.1. human. [Q15349-1] uc003qvc.1. human. [Q15349-3]
Organism-specific databases
CTD	6196.
GeneCards	GC06M166822.
HGNC	HGNC:10431. RPS6KA2.
HPA	CAB026243. HPA045061. HPA054237.
MIM	601685. gene.
neXtProt	NX_Q15349.
PharmGKB	PA34846.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
KO	K04373.
OrthoDB	EOG7B8S38.
PhylomeDB	Q15349.
TreeFam	TF313438.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Reactome	REACT_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.
SignaLink	Q15349.
Gene expression databases
ArrayExpress	Q15349.
Bgee	Q15349.
CleanEx	HS_RPS6KA2.
Genevestigator	Q15349.
Family and domain databases
InterPro	IPR000961. 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]
Pfam	PF00069. Pkinase. 2 hits. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 2 hits. [Graphical view]
SUPFAM	SSF56112. SSF56112. 2 hits.
PROSITE	PS51285. 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]
ProtoNet	Search...
Other
ChiTaRS	RPS6KA2. human.
GeneWiki	RPS6KA2.
GenomeRNAi	6196.
NextBio	24063.
PRO	Q15349.
SOURCE	Search...

Entry information

Entry name

KS6A2_HUMAN

Accession

Primary (citable) accession number: Q15349
Secondary accession number(s): B3KTK9 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.