AiPD: Autoinhibited Protein Database

Q5R4K3

Gene name	RPS6KA5
Protein name	Ribosomal protein S6 kinase alpha-5
Names	S6K-alpha-5
Species	Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway	pon:100173967
EC number	2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

709-727 (Putative autoinhibitory alpha helix) SS

Target domain	426-687 (Protein kinase domain)
Relief mechanism	PTM, Partner binding
Assay

AID

709-727 (Putative autoinhibitory alpha helix)

Target domain

426-687 (Protein kinase domain)

Relief mechanism

PTM (Phosphorylation by ERK1/2), Partner binding (Binding of ERKs to C-terminal ERK-binding site (726-735))

Assay

Accessory elements

194-218 (Activation loop from InterPro)

Target domain	49-318 (Protein kinase domain)
Relief mechanism
Assay

564-587 (Activation loop from InterPro)

Target domain	426-687 (Protein kinase domain)
Relief mechanism
Assay

References

Vermeulen L et al. (2003) "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)", The EMBO journal, 22, 1313-24

Poteet-Smith CE et al. (1999) "Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family", The Journal of biological chemistry, 274, 22135-8

Autoinhibited structure

Activated structure

1 structures for Q5R4K3

Entry ID	Method	Resolution	Chain	Position	Source
AF-Q5R4K3-F1	Predicted				AlphaFoldDB

No variants for Q5R4K3

Variant ID(s)	Position	Change	Description	Diseaes Association	Provenance
No variants for Q5R4K3

No associated diseases with Q5R4K3

6 regional properties for Q5R4K3

Type	Name	Position	InterPro Accession
domain	Protein kinase domain	49 - 318	IPR000719-1
domain	Protein kinase domain	426 - 687	IPR000719-2
domain	AGC-kinase, C-terminal	319 - 387	IPR000961
active_site	Serine/threonine-protein kinase, active site	173 - 185	IPR008271-1
active_site	Serine/threonine-protein kinase, active site	540 - 552	IPR008271-2
domain	Protein kinase, C-terminal	339 - 377	IPR017892

Functions

		Description
EC Number	2.7.11.1	Protein-serine/threonine kinases
Subcellular Localization	Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category	No pathway information available

2 GO annotations of cellular component

Name	Definition
cytoplasm	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus	A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

5 GO annotations of molecular function

Name	Definition
ATP binding	Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding	Binding to a magnesium (Mg) ion.
protein serine kinase activity	Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity	Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine/threonine/tyrosine kinase activity	Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

8 GO annotations of biological process

Name	Definition
histone H2A-S1 phosphorylation	OBSOLETE. The modification of histone H2A by the addition of an phosphate group to a serine residue at position 1 of the histone.
histone H3-S10 phosphorylation	OBSOLETE. The modification of histone H3 by the addition of an phosphate group to a serine residue at position 10 of the histone.
histone H3-S28 phosphorylation	OBSOLETE. The modification of histone H3 by the addition of an phosphate group to a serine residue at position 28 of the histone.
inflammatory response	The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
intracellular signal transduction	The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
negative regulation of transcription, DNA-templated	Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
positive regulation of NF-kappaB transcription factor activity	Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
regulation of transcription, DNA-templated	Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.

No homologous proteins in AiPD

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
No homologous proteins

10	20	30	40	50	60
MEEEGGSSGG	AAGTSADGGD	GGEQLLTVKH	ELRTANLTGH	AERVGIENFE	LLKVLGTGAY
70	80	90	100	110	120
GKVFLVRKIS	GHDTGKLYAM	KVLKKATIVQ	KAKTTEHTRT	ERQVLEHTRQ	SPFLVTLHYA
130	140	150	160	170	180
FQTETKLHLI	LDYINGGELF	THLSQRERFT	EHEVQIYVGE	IVLALEHLHK	LGIIYRDIKL
190	200	210	220	230	240
ENILLDSNGH	VMLTDFGLSK	EFVADETERA	YSFCGTIEYM	APDIVRGGDS	GHDKAVDWWS
250	260	270	280	290	300
LGVLMYELLT	GASPFTVDGE	KNSQAEISRR	ILKSEPPYPQ	EMSALAKDLI	QHLLMKDPKK
310	320	330	340	350	360
RLGCGPRDAD	EIKEHLFFQK	INWDDLAAKK	VPAPFKPVIR	DELDVSNFAE	EFTEMDPTYS
370	380	390	400	410	420
PAALPQSSEK	LFQGYSFVAP	SILFKRNAAV	IDPLQFHMEV	ERPGVTNVAR	SAMMKDSPFY
430	440	450	460	470	480
QHYDLDLKDK	PLGEGSFSIC	RKCVHKKSNQ	AFAVKIISKR	MEANTQKEIT	ALKLCEGHPN
490	500	510	520	530	540
IVKLHEVFHD	QLHTFLVMEL	LNGGELFERI	KKKKHFSETE	ASYIMRKLVS	AVSHMHDVGV
550	560	570	580	590	600
VHRDLKPENL	LFTDENDNLE	IKIIDFGFAR	PKPPDNQPLK	TPCFTLHYAA	PELLNQNGYD
610	620	630	640	650	660
ESCDLWSLGV	ILYTMLSGQV	PFQSHDRSLT	CTSAVEIMKK	IKKGDFSFEG	EAWKNVSQEA
670	680	690	700	710	720
KDLIQGLLTV	DPNKRLKMSG	LRYNEWLQDG	SQLSSNPLMT	PDILGSSGAA	VHTCVKATFH
730	740	750	760	770	780
AFNKYKREGF	CLQNVDKAPL	AKRRKMKKTS	TSTETRSSSS	ESSHSSSSHS	HGKTTPTKTL
790	800
QPSNPADSNN	PETLFQFSDS	VA