Q9UBS0 (KS6B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribosomal protein S6 kinase beta-2
Short name=S6K-beta-2
Short name=S6K2
EC=2.7.11.1

Alternative name(s):
70 kDa ribosomal protein S6 kinase 2
Short name=P70S6K2
Short name=p70-S6K 2
S6 kinase-related kinase
Short name=SRK
Serine/threonine-protein kinase 14B
p70 ribosomal S6 kinase beta
Short name=S6K-beta
Short name=p70 S6 kinase beta
Short name=p70 S6K-beta
Short name=p70 S6KB
Short name=p70-beta

Gene names

Name:	RPS6KB2
Synonyms:	STK14B

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phosphorylates specifically ribosomal protein S6.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm. Nucleus Ref.8 Ref.9.
Post-translational modification	Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention. Ref.8 Ref.9
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 1 protein kinase domain.
Sequence caution	The sequence BAA34402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
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	epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of translational initiation Inferred from mutant phenotype PubMed 16763566. Source: UniProtKB protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara translation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW peptide binding Inferred from electronic annotation. Source: Compara protein serine/threonine kinase activity Traceable author statement Ref.2. Source: ProtInc ribosomal protein S6 kinase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Ribosomal protein S6 kinase beta-2		PRO_0000086214
Regions
	Domain	67 – 328	262	Protein kinase
	Domain	329 – 399	71	AGC-kinase C-terminal
	Nucleotide binding	73 – 81	9	ATP By similarity
	Motif	471 – 477	7	Nuclear localization signal Ref.9
	Compositional bias	411 – 482	72	Pro-rich
Sites
	Active site	194	1	Proton acceptor By similarity
	Binding site	99	1	ATP By similarity
Amino acid modifications
	Modified residue	15	1	Phosphoserine Ref.10
	Modified residue	416	1	Phosphoserine By similarity
	Modified residue	423	1	Phosphoserine By similarity
	Modified residue	473	1	Phosphoserine; by PKC Ref.9
Natural variations
	Natural variant	267	1	P → L. Ref.13 Corresponds to variant rs55987642 [ dbSNP | Ensembl ].		VAR_040643
	Natural variant	368	1	V → M. Ref.13 Corresponds to variant rs55642995 [ dbSNP | Ensembl ].		VAR_040644
	Natural variant	420	1	A → V. Ref.1 Ref.2 Ref.3 Ref.7 Ref.13 Corresponds to variant rs13859 [ dbSNP | Ensembl ].		VAR_040645
	Natural variant	443	1	T → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.13		VAR_040646
Experimental info
	Sequence conflict	90	1	Missing in BAA37145. Ref.2
	Sequence conflict	409	1	R → C in BAA37145. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UBS0 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 5D33660D24A2C7BE	FASTA	482	53,455
	10 20 30 40 50 60 MAAVFDLDLE TEEGSEGEGE PELSPADACP LAELRAAGLE PVGHYEEVEL TETSVNVGPE 70 80 90 100 110 120 RIGPHCFELL RVLGKGGYGK VFQVRKVQGT NLGKIYAMKV LRKAKIVRNA KDTAHTRAER 130 140 150 160 170 180 NILESVKHPF IVELAYAFQT GGKLYLILEC LSGGELFTHL EREGIFLEDT ACFYLAEITL 190 200 210 220 230 240 ALGHLHSQGI IYRDLKPENI MLSSQGHIKL TDFGLCKESI HEGAVTHTFC GTIEYMAPEI 250 260 270 280 290 300 LVRSGHNRAV DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIRGKLALPP YLTPDARDLV 310 320 330 340 350 360 KKFLKRNPSQ RIGGGPGDAA DVQRHPFFRH MNWDDLLAWR VDPPFRPCLQ SEEDVSQFDT 370 380 390 400 410 420 RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE GFSFQPKLRS PRRLNSSPRA 430 440 450 460 470 480 PVSPLKFSPF EGFRPSPSLP EPTELPLPPL LPPPPPSTTA PLPIRPPSGT KKSKRGRGRP GR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region." Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D., Yonezawa K. J. Biol. Chem. 273:30061-30064(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[2]	"Cloning and characterization of p70 S6Kbeta defines a novel family of p70 S6 kinases." Saitoh M., ten Dijke P., Miyazono K., Ichijo H. Biochem. Biophys. Res. Commun. 253:470-476(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[3]	"Characterization of S6K2, a novel kinase homologous to S6K1." Lee-Fruman K.K., Kuo C.J., Lippincott J., Terada N., Blenis J. Oncogene 18:5108-5114(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420.
[4]	"Cloning and characterization of a novel S6 kinase-related kinase, SRK." Koh H.J., Lee B.N., Choi H.S., Chung J. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , 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].
[7]	"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], VARIANT VAL-420. Tissue: Brain.
[8]	"Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin." Park I.H., Bachmann R., Shirazi H., Chen J. J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MTOR, SUBCELLULAR LOCATION.
[9]	"Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization." Valovka T., Verdier F., Cramer R., Zhyvoloup A., Fenton T., Rebholz H., Wang M.L., Gzhegotsky M., Lutsyk A., Matsuka G., Filonenko V., Wang L., Proud C.G., Parker P.J., Gout I.T. Mol. Cell. Biol. 23:852-863(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-473, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: 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] LEU-267; MET-368; VAL-420 AND MET-443.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB016869 mRNA. Translation: BAA34402.1. Different initiation. AB019245 mRNA. Translation: BAA37145.1. AF076931 mRNA. Translation: AAD46063.1. AF099739 mRNA. Translation: AAD20990.1. AP003419 Genomic DNA. No translation available. CH471076 Genomic DNA. Translation: EAW74621.1. BC000094 mRNA. Translation: AAH00094.3. BC136564 mRNA. Translation: AAI36565.1.
IPI	IPI00217069.
PIR	JE0377.
RefSeq	NP_003943.2. NM_003952.2.
UniGene	Hs.534345.
3D structure databases
ProteinModelPortal	Q9UBS0.
SMR	Q9UBS0. Positions 61-393.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBS0. 2 interactions.
MINT	MINT-207158.
STRING	9606.ENSP00000308413.
PTM databases
PhosphoSite	Q9UBS0.
Polymorphism databases
DMDM	296434560.
Proteomic databases
PaxDb	Q9UBS0.
PRIDE	Q9UBS0.
Protocols and materials databases
DNASU	6199.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000312629; ENSP00000308413; ENSG00000175634.
GeneID	6199.
KEGG	hsa:6199.
UCSC	uc001old.3. human.
Organism-specific databases
CTD	6199.
GeneCards	GC11P067195.
H-InvDB	HIX0009859.
HGNC	HGNC:10437. RPS6KB2.
HPA	CAB019404. HPA010010.
MIM	608939. gene.
neXtProt	NX_Q9UBS0.
PharmGKB	PA34852.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	Q9UBS0.
KO	K04688.
OMA	TETSVNP.
OrthoDB	EOG4Q2DFF.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9UBS0.
Bgee	Q9UBS0.
CleanEx	HS_RPS6KB2.
Genevestigator	Q9UBS0.
GermOnline	ENSG00000175634. Homo sapiens.
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. IPR016238. Ribosomal_S6_kinase. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3111.
GenomeRNAi	6199.
NextBio	24077.
SOURCE	Search...

Entry information

Entry name

KS6B2_HUMAN

Accession

Primary (citable) accession number: Q9UBS0
Secondary accession number(s): B2RMZ9, O94809, Q9UEC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 131 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.