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RSK2 (human)

Overview RSK2 an AGC kinase of the RSK family. Phosphorylated and activated by Erk1 and -2 in response to many growth factors, polypeptide hormones and neurotransmitters. Several phosphorylation sites are important for its activation. Possesses two kinase domains connected by a regulator linker region. Phosphorylates a wide range of substrates including ribosomal protein S6. Prominently expressed in brain structures essential for cognitive function and learning. Note: This description may include information from UniProtKB. Protein type: Kinase, protein; EC 2.7.11.1; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); AGC group; RSK family; RSK subfamily Cellular Component: nucleoplasm; cytosol Molecular Function: protein serine/threonine kinase activity; caspase inhibitor activity; magnesium ion binding; protein kinase binding; ATP binding; protein kinase activity Biological Process: axon guidance; central nervous system development; nerve growth factor receptor signaling pathway; stress-activated MAPK cascade; response to lipopolysaccharide; negative regulation of caspase activity; toll-like receptor 3 signaling pathway; signal transduction; synaptic transmission; skeletal development; toll-like receptor 4 signaling pathway; regulation of transcription in response to stress; MyD88-independent toll-like receptor signaling pathway; regulation of translation in response to stress; cell cycle; positive regulation of cell growth; Toll signaling pathway; toll-like receptor 2 signaling pathway; toll-like receptor 1 signaling pathway; MyD88-dependent toll-like receptor signaling pathway; toll-like receptor signaling pathway; innate immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of cell differentiation; negative regulation of apoptosis Reference #:  P51812 (UniProtKB) Alt. Names/Synonyms: 90 kDa ribosomal protein S6 kinase 3; CLS; HU-3; Insulin-stimulated protein kinase 1; ISPK-1; ISPK1; KS6A3; MAP kinase-activated protein kinase 1b; MAPK-activated protein kinase 1b; MAPKAP kinase 1b; MAPKAPK-1b; MAPKAPK1B; mental retardation, X-linked 19; MRX19; p90-RSK 3; p90-RSK2; p90RSK3; pp90RSK2; Ribosomal protein S6 kinase alpha-3; ribosomal protein S6 kinase, 90kDa, polypeptide 3; Ribosomal S6 kinase 2; RPS6KA3; RSK; RSK-2; RSK2; S6K-alpha-3; S6K-alpha3 Gene Symbols: RPS6KA3 Molecular weight: 83,736 Da Basal Isoelectric point: 6.41  Predict pI for various phosphorylation states CST Pathways:  Apoptosis  |  Cell Cycle: G2/M DNA Damage Checkpoint  |  GPCRs Signaling to MAPK/Erk  |  Inhibition of Apoptosis  |  MAPK/Erk in Growth and Differentiation  |  Mitochondrial Control of Apoptosis  |  mTOR Signaling  |  Regulation of Microtubule Dynamics  |  Translation: eIF4E and p70S6K Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below RSK2 4D9T - A=399-740 (human) 4D9U - A=399-740 (human) 4JG6 - A=399-740 (human) 4JG7 - A=399-740 (human) 4JG8 - A=399-740 (human) 2QR7 - A=399-740 (mouse) 2QR8 - A=399-740 (mouse) 3G51 - A=44-367 (mouse) 3UBD - A=45-346 (mouse) 4EL9 - A=45-346 (mouse) 4GUE - A=45-346 (mouse) Substrate Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 4D9T 4D9U 4JG6 4JG7 4JG8  |  ENZYME  |  DISEASE 300075 303600  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
apoptosis, altered: Y529‑p transcription, altered: S369‑p enzymatic activity, induced: S227‑p, S369‑p, T577‑p molecular association, regulation: Y529‑p protein conformation: S369‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S17-p	WQKMAVEsPsDSAEN
0	1		S19-p	KMAVEsPsDSAENGQ
0	2		K72-u	PSQFELLkVLGQGsF
0	2		S78-p	LkVLGQGsFGkVFLV
0	3		K81-a	LGQGsFGkVFLVKKI
0	1		K100-a	ARQLYAMkVLkKATL
0	1		K103-a	LYAMkVLkKATLKVR
0	2		R192	HSLGIIYRDLKPENI
0	38		Y226-p	IDHEKKAysFCGtVE
7	148		S227-p	DHEKKAysFCGtVEy
0	48		T231-p	KAysFCGtVEyMAPE
0	4		Y234-p	sFCGtVEyMAPEVVN
0	2		K274	PFQGKDRKETMtMIL
0	1		T278-p	KDRKETMtMILKAKL
0	2		K282	ETMtMILKAKLGMPQ
0	1		K284	MtMILKAKLGMPQFL
0	5		K322-u	PDGVEEIkRHSFFST
0	1		S325	VEEIkRHSFFSTIDW
0	1		S328	IkRHSFFSTIDWNKL
0	5		Y356-p	GRPEDTFyFDPEFtA
0	3		T362-p	FyFDPEFtAKtPKDs
5	25		T365-p	DPEFtAKtPKDsPGI
9	34		S369-p	tAKtPKDsPGIPPsA
0	13		S375-p	DsPGIPPsANAHQLF
8	52		S386-p	HQLFRGFsFVAItsD
0	1		T391-p	GFsFVAItsDDESQA
0	3		S392-p	FsFVAItsDDESQAM
0	16		S415-p	VQQLHRNsIQFTDGY
0	3		Y433-p	EDIGVGSySVCKRCI
1	4		Y470-p	EIEILLRyGQHPNII
1	4		Y483-p	IITLKDVyDDGKyVy
2	15		Y488-p	DVyDDGKyVyVVTEL
0	1		Y490-p	yDDGKyVyVVTELMK
0	1		S517-p	FFSEREAsAVLFTIT
2	5		Y529-p	TITKTVEyLHAQGVV
0	1		Y547-p	LKPSNILyVDESGNP
0	1		S556-p	DESGNPEsIRICDFG
0	3		K566	ICDFGFAKQLRAENG
5	174		T577-p	AENGLLMtPCytANF
1	83		Y580-p	GLLMtPCytANFVAP
0	26		T581-p	LLMtPCytANFVAPE
1	4		Y644-p	KFSLSGGyWNSVSDT
0	21		Y688-p	HWDQLPQyQLNRQDA
2	91		Y707-p	KGAMAATysALNRNQ
0	1		S708-p	GAMAATysALNRNQs
0	36		S715-p	sALNRNQsPVLEPVG
0	1		S737	RGIKKITSTAL____

	mouse
S17	WQKMAVESPSDSAEN
S19	KMAVESPSDSAENGQ
K72	PSQFELLKVLGQGSF
S78	LKVLGQGSFGKVFLV
K81	LGQGSFGKVFLVKKI
K100	ARQLYAMKVLKKATL
K103	LYAMKVLKKATLKVR
R192-m1	HSLGIIYrDLKPENI
Y226-p	IDHEKKAysFCGtVE
S227-p	DHEKKAysFCGtVEy
T231-p	KAysFCGtVEyMAPE
Y234-p	sFCGtVEyMAPEVVN
K274-u	PFQGKDRkETMTMIL
T278	KDRkETMTMILkAkL
K282-u	ETMTMILkAkLGMPQ
K284-a	MTMILkAkLGMPQFL
K322	PDGVEEIKRHsFFsT
S325-p	VEEIKRHsFFsTIDW
S328-p	IKRHsFFsTIDWNKL
Y356	GRPEDTFYFDPEFtA
T362-p	FYFDPEFtAKtPKDs
T365-p	DPEFtAKtPKDsPGI
S369-p	tAKtPKDsPGIPPsA
S375-p	DsPGIPPsANAHQLF
S386-p	HQLFRGFsFVAITSD
T391	GFsFVAITSDDESQA
S392	FsFVAITSDDESQAM
S415-p	VQQLHRNsIQFTDGY
Y433	EDIGVGSYSVCKRCI
Y470	EIEILLRYGQHPNII
Y483-p	IITLKDVyDDGKyVy
Y488-p	DVyDDGKyVyVVTEL
Y490-p	yDDGKyVyVVTELMK
S517	FFSEREASAVLFTIT
Y529-p	TITKTVEyLHAQGVV
Y547	LKPSNILYVDESGNP
S556	DESGNPESIRICDFG
K566-u	ICDFGFAkQLRAENG
T577-p	AENGLLMtPCYTANF
Y580	GLLMtPCYTANFVAP
T581	LLMtPCYTANFVAPE
Y644	KFSLSGGYWNSVSDT
Y688	HWDQLPQYQLNRQDA
Y707	KGAMAATYSALNRNQ
S708	GAMAATYSALNRNQs
S715-p	SALNRNQsPVLEPVG
S737-p	RGIKKITsTAL____

	rat
S17	WQKMAVESPSDSAEN
S19	KMAVESPSDSAENGQ
K72	PSQFELLKVLGQGSF
S78	LKVLGQGSFGKVFLV
K81	LGQGSFGKVFLVKKI
K100	ARQLYAMKVLKKATL
K103	LYAMKVLKKATLKVR
R192	HSLGIIYRDLKPENI
Y226	IDHEKKAYsFCGTVE
S227-p	DHEKKAYsFCGTVEY
T231	KAYsFCGTVEYMAPE
Y234	sFCGTVEYMAPEVVN
K274	PFQGKDRKETMTMIL
T278	KDRKETMTMILKAKL
K282	ETMTMILKAKLGMPQ
K284	MTMILKAKLGMPQFL
K322	PDGVEEIKRHSFFST
S325	VEEIKRHSFFSTIDW
S328	IKRHSFFSTIDWNKL
Y356	GRPEDTFYFDPEFTA
T362	FYFDPEFTAKtPKDs
T365-p	DPEFTAKtPKDsPGI
S369-p	TAKtPKDsPGIPPSA
S375	DsPGIPPSANAHQLF
S386	HQLFRGFSFVAITSD
T391	GFSFVAITSDDESQA
S392	FSFVAITSDDESQAM
S415	VQQLHRNSIQFTDGY
Y433	EDIGVGSYSVCKRCI
Y470	EIEILLRYGQHPNII
Y483	IITLKDVYDDGKYVY
Y488	DVYDDGKYVYVVTEL
Y490	YDDGKYVYVVTELMK
S517	FFSEREASAVLFTIT
Y529	TITKTVEYLHTQGVV
Y547	LKPSNILYVDESGNP
S556	DESGNPESIRICDFG
K566	ICDFGFAKQLRAENG
T577	AENGLLMTPCYTANF
Y580	GLLMTPCYTANFVAP
T581	LLMTPCYTANFVAPE
Y644	KFSLSGGYWNSVSDT
Y688	HWDQLPQYQLNRQDA
Y707	KGAMAATYSALNRNQ
S708	GAMAATYSALNRNQs
S715-p	SALNRNQsPVLEPVG
S737	RGIKKITSTAL____

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