Q8C050 (KS6A5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribosomal protein S6 kinase alpha-5
Short name=S6K-alpha-5
EC=2.7.11.1

Alternative name(s):
90 kDa ribosomal protein S6 kinase 5
Nuclear mitogen- and stress-activated protein kinase 1
RSK-like protein kinase
Short name=RLSK

Gene names

Name:	Rps6ka5
Synonyms:	Msk1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	863 AA.
Sequence status	Complete.
Protein existence	Evidence 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 factors RELA, STAT3 and ETV1/ER81, 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 and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. 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. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.7
Cofactor	Magnesium By similarity. Ref.7
Enzyme regulation	Activated by phosphorylation at Ser-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-211, Ser-375 and Ser-380 by the activated C-terminal kinase domain. The active N-terminal kinase domain finally phosphorylates downstream substrates, as well as Ser-814, Ser-816 and Ser-822 in its own C-terminal region.
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 RPS6KA5 associates with and phosphorylates the NF-kappa-B p65 subunit RELA. Interacts with CREBBP and EP300 By similarity.
Subcellular location	Nucleus By similarity UniProtKB O75676.
Post-translational modification	Ser-375 and Thr-645 phosphorylation is required for kinase activity. Ser-375 and Ser-211 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-359, Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-814, Ser-816 and Ser-822 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 process	Inflammatory response Stress response
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H2A-S1 phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB histone H3-S10 phosphorylation Inferred from sequence or structural similarity PubMed 12773393. Source: UniProtKB histone H3-S28 phosphorylation Inferred from sequence or structural similarity PubMed 12773393. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW interleukin-1-mediated signaling pathway Inferred from electronic annotation. Source: Compara intracellular protein kinase cascade Inferred from direct assay Ref.7. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of histone acetylation Inferred from electronic annotation. Source: Compara positive regulation of histone phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara response to external stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.7. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q8C050-1)

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 1 (identifier: Q8C050-2)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     490-554: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 863	863	Ribosomal protein S6 kinase alpha-5		PRO_0000086208
Regions
	Domain	48 – 317	270	Protein kinase 1
	Domain	318 – 386	69	AGC-kinase C-terminal
	Domain	428 – 675	248	Protein kinase 2
	Nucleotide binding	54 – 62	9	ATP By similarity UniProtKB Q15418
	Nucleotide binding	431 – 440	10	ATP By similarity
Sites
	Active site	176	1	Proton acceptor By similarity UniProtKB Q15418
	Active site	608	1	Proton acceptor By similarity UniProtKB Q15418
	Binding site	80	1	ATP By similarity UniProtKB Q15418
	Binding site	454	1	ATP By similarity UniProtKB Q15418
Amino acid modifications
	Modified residue	211	1	Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
	Modified residue	359	1	Phosphoserine; by MAPK1, MAPK3 and MAPK14 By similarity UniProtKB Q15418
	Modified residue	375	1	Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
	Modified residue	380	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	645	1	Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarity
	Modified residue	711	1	Phosphoserine By similarity
	Modified residue	721	1	Phosphoserine By similarity
	Modified residue	759	1	Phosphoserine By similarity
	Modified residue	764	1	Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarity
	Modified residue	814	1	Phosphoserine; by autocatalysis By similarity UniProtKB Q15418
	Modified residue	816	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	822	1	Phosphoserine; by autocatalysis By similarity
Natural variations
	Alternative sequence	490 – 554	65	Missing in isoform 1.		VSP_050613
Experimental info
	Sequence conflict	2 – 15	14	EGEGG…AGTSG → GGRAAAAAARAPAE in AAQ24165. Ref.1
	Sequence conflict	117	1	H → N in BAC27809. Ref.2
	Sequence conflict	376	1	F → Y in BAC27809. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified October 24, 2003. Version 2. Checksum: 7A3C76D4036EA3EA	FASTA	863	96,583
	10 20 30 40 50 60 MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL LKVLGTGAYG 70 80 90 100 110 120 KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE RQVLEHIRQS PFLVTLHYAF 130 140 150 160 170 180 QTETKLHLIL DYINGGELFT HLSQRERFTE HEVQIYVGEI VLALEHLHKL GIIYRDIKLE 190 200 210 220 230 240 NILLDSNGHV VLTDFGLSKE FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL 250 260 270 280 290 300 GVLMYELLTG ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR 310 320 330 340 350 360 LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE FTEMDPTYSP 370 380 390 400 410 420 AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD RPGVTNVARS AMMKDSPFYQ 430 440 450 460 470 480 HYDLDLKDKP LGEGSFSICR KCVHKKTNQA FAVKIISKRM EANTQKEITA LKLCEGHPNI 490 500 510 520 530 540 VKLHEVFHDQ VAASAQPPGQ VVLCSLLLLA LLFNRSLTRK PVTWTWLVHS TSQLPPLPPP 550 560 570 580 590 600 MPEIVLFILL SDNGQLHTFL VMELLNGGEL FERIKRKKHF SETEASYIMR KLVSAVSHMH 610 620 630 640 650 660 DVGVVHRDLK PENLLFTDEN DNLEIKVIDF GFARLKPPDN QPLKTPCFTL HYAAPELLTH 670 680 690 700 710 720 NGYDESCDLW SLGVILYTML SGQVPFQSHD RSLTCTSAVE IMKKIKKGDF SFEGEAWKNV 730 740 750 760 770 780 SQEAKDLIQG LLTVDPNKRL KMSGLRYNEW LQDGSQLSSN PLMTPDILGS SGAAVHTCVK 790 800 810 820 830 840 ATFHAFNKYK REGFCLQNVD KAPLAKRRKM KRTSTSTETR SSSSESSRSS SSQSHGKTTP 850 860 TKTLQPSNPT EGSNPDTLFQ FSD
	Isoform 1 (5) [UniParc]. Checksum: 57AB12399BEF7B0E	FASTA	798	89,515
	10 20 30 40 50 60 MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL LKVLGTGAYG 70 80 90 100 110 120 KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE RQVLEHIRQS PFLVTLHYAF 130 140 150 160 170 180 QTETKLHLIL DYINGGELFT HLSQRERFTE HEVQIYVGEI VLALEHLHKL GIIYRDIKLE 190 200 210 220 230 240 NILLDSNGHV VLTDFGLSKE FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL 250 260 270 280 290 300 GVLMYELLTG ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR 310 320 330 340 350 360 LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE FTEMDPTYSP 370 380 390 400 410 420 AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD RPGVTNVARS AMMKDSPFYQ 430 440 450 460 470 480 HYDLDLKDKP LGEGSFSICR KCVHKKTNQA FAVKIISKRM EANTQKEITA LKLCEGHPNI 490 500 510 520 530 540 VKLHEVFHDQ LHTFLVMELL NGGELFERIK RKKHFSETEA SYIMRKLVSA VSHMHDVGVV 550 560 570 580 590 600 HRDLKPENLL FTDENDNLEI KVIDFGFARL KPPDNQPLKT PCFTLHYAAP ELLTHNGYDE 610 620 630 640 650 660 SCDLWSLGVI LYTMLSGQVP FQSHDRSLTC TSAVEIMKKI KKGDFSFEGE AWKNVSQEAK 670 680 690 700 710 720 DLIQGLLTVD PNKRLKMSGL RYNEWLQDGS QLSSNPLMTP DILGSSGAAV HTCVKATFHA 730 740 750 760 770 780 FNKYKREGFC LQNVDKAPLA KRRKMKRTST STETRSSSSE SSRSSSSQSH GKTTPTKTLQ 790 PSNPTEGSNP DTLFQFSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of mouse ribosomal protein S6 kinase, 90kDa, polypeptide 5 (RPS6KA5)." Zhou G., Wang J., Xu W. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Brain.
[3]	"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: Mammary gland.
[4]	"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1." Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z. J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[5]	"MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells." Zhang Y., Liu G., Dong Z. J. Biol. Chem. 276:42534-42542(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3.
[6]	"MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts." Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S. Mol. Cell. Biol. 22:2871-2881(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1 AND ATF1.
[7]	"Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)." Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G. EMBO J. 22:1313-1324(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Mitogen and stress response kinase-1 (MSK1) mediates excitotoxic induced death of hippocampal neurones." Hughes J.P., Staton P.C., Wilkinson M.G., Strijbos P.J., Skaper S.D., Arthur J.S., Reith A.D. J. Neurochem. 86:25-32(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL DEATH.
[9]	"MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2." Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C. J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[10]	"ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-kappaB transactivation during oxidative stress in skeletal myoblasts." Kefaloyianni E., Gaitanaki C., Beis I. Cell. Signal. 18:2238-2251(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RELA/NFKB3.
[11]	"The kinases MSK1 and MSK2 are required for epidermal growth factor-induced, but not tumor necrosis factor-induced, histone H3 Ser10 phosphorylation." Duncan E.A., Anest V., Cogswell P., Baldwin A.S. J. Biol. Chem. 281:12521-12525(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[12]	"The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling." Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S. Nat. Immunol. 9:1028-1036(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1; ATF1 AND HISTONE H3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY341873 mRNA. Translation: AAQ24158.1. AY341881 mRNA. Translation: AAQ24165.1. AK032316 mRNA. Translation: BAC27809.1. BC035298 mRNA. Translation: AAH35298.1.
IPI	IPI00229794. IPI00380392.
RefSeq	NP_705815.1. NM_153587.2.
UniGene	Mm.220417. Mm.392855.
3D structure databases
ProteinModelPortal	Q8C050.
SMR	Q8C050. Positions 23-380, 414-793.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4116279.
STRING	10090.ENSMUSP00000042987.
PTM databases
PhosphoSite	Q8C050.
Proteomic databases
PaxDb	Q8C050.
PRIDE	Q8C050.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180.
GeneID	73086.
KEGG	mmu:73086.
UCSC	uc007ost.1. mouse. uc007osu.1. mouse.
Organism-specific databases
CTD	9252.
MGI	MGI:1920336. Rps6ka5.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00680000099806.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	Q8C050.
KO	K04445.
OMA	FQSHDKS.
OrthoDB	EOG4VMFDS.
Gene expression databases
Bgee	Q8C050.
CleanEx	MM_RPS6KA5.
Genevestigator	Q8C050.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_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. 3 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. Kinase_like. 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
NextBio	337443.
SOURCE	Search...

Entry information

Entry name

KS6A5_MOUSE

Accession

Primary (citable) accession number: Q8C050
Secondary accession number(s): Q8CI92

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	October 24, 2003
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program