dbPTM

SGK3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGK3_MOUSE
UniProt AC	Q9ERE3
Protein Name	Serine/threonine-protein kinase Sgk3
Gene Name	Sgk3
Organism	Mus musculus (Mouse).
Sequence Length	496
Subcellular Localization	Cytoplasmic vesicle . Early endosome . Recycling endosome. Endosomal localization is a prerequisite for complete kinase activity. It is essential for its colocalization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosp
Protein Description	Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes..
Protein Sequence	MQRDCIMDYKESCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNSLKKQFPAMALKIPAKRIFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMDSPRHQSDPSEDEDERSTSKPHSTSRNINLGPTGNPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSMGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLNLRPGVSLTAWSILEELLEKNRQNRLGAKEDFLEIQNHPFFESLSWTDLVQKKIPPPFNPNVAGPDDIRNFDAVFTEETVPYSVCVSSDYSIVNASVLEADDAFVGFSYAPPSEDLFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	REKKKRFTVYKVLVS HHHHHCEEEEEEHHC	27.27	-
71	Acetylation	QFPAMALKIPAKRIF HCCHHHCCCCHHHHH	36.79	23806337
71	Succinylation	QFPAMALKIPAKRIF HCCHHHCCCCHHHHH	36.79	23806337
121	Phosphorylation	RAFLQMDSPRHQSDP HHHHCCCCCCCCCCC	20.63	26643407
126	Phosphorylation	MDSPRHQSDPSEDED CCCCCCCCCCCCCCC	45.42	25521595
129	Phosphorylation	PRHQSDPSEDEDERS CCCCCCCCCCCCHHH	63.77	25521595
136	Phosphorylation	SEDEDERSTSKPHST CCCCCHHHCCCCCCC	34.68	26643407
137	Phosphorylation	EDEDERSTSKPHSTS CCCCHHHCCCCCCCC	47.17	26643407
138	Phosphorylation	DEDERSTSKPHSTSR CCCHHHCCCCCCCCC	45.49	26643407
142	Phosphorylation	RSTSKPHSTSRNINL HHCCCCCCCCCCEEC	36.28	30635358
143	Phosphorylation	STSKPHSTSRNINLG HCCCCCCCCCCEECC	28.77	30635358
144	Phosphorylation	TSKPHSTSRNINLGP CCCCCCCCCCEECCC	26.75	30635358
166	Ubiquitination	PTDFDFLKVIGKGSF CCCCCCEEEECCCCH	31.62	-
320	Phosphorylation	AISDTTTTFCGTPEY EECCCCCCCCCCHHH	18.16	-
461	Phosphorylation	TEETVPYSVCVSSDY CCCCCCCEEEECCCC	11.72	-
465	Phosphorylation	VPYSVCVSSDYSIVN CCCEEEECCCCCEEE	16.62	-
486	Phosphorylation	DDAFVGFSYAPPSED CCCCCCCCCCCCCHH	17.92	15871460

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
320	T	Phosphorylation	Kinase	PDPK1	Q9Z2A0	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
320	T	Phosphorylation	-
Activated by phosphorylation on Ser-486 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-320.
486	S	Phosphorylation	-
Activated by phosphorylation on Ser-486 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-320.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SGK3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SGK3_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SGK3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, ANDMASS SPECTROMETRY.	19367708 [Abstract]

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