dbPTM

SGK3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGK3_HUMAN
UniProt AC	Q96BR1
Protein Name	Serine/threonine-protein kinase Sgk3
Gene Name	SGK3
Organism	Homo sapiens (Human).
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 phospho
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	MQRDHTMDYKESCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMDSPKHQSDPSEDEDERSSQKLHSTSQNINLGPSGNPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLGAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADDAFVGFSYAPPSEDLFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	DYKESCPSVSIPSSD CCHHHCCCCCCCCCH	32.59	27251275
17	Phosphorylation	KESCPSVSIPSSDEH HHHCCCCCCCCCHHH	32.87	27251275
32	Phosphorylation	REKKKRFTVYKVLVS HHHHHCEEEEEEHHC	27.27	24719451
39	Phosphorylation	TVYKVLVSVGRSEWF EEEEEHHCCCCCHHE	18.07	24114839
51	Phosphorylation	EWFVFRRYAEFDKLY HHEEEEHHHHHHHHH	13.26	30622161
58	Phosphorylation	YAEFDKLYNTLKKQF HHHHHHHHHHHHHHC	16.31	30622161
60	Phosphorylation	EFDKLYNTLKKQFPA HHHHHHHHHHHHCCH	26.80	30622161
71	Acetylation	QFPAMALKIPAKRIF HCCHHHCCCCHHHHH	36.79	25953088
75	"N6,N6-dimethyllysine"	MALKIPAKRIFGDNF HHCCCCHHHHHCCCC	40.44	-
75	Acetylation	MALKIPAKRIFGDNF HHCCCCHHHHHCCCC	40.44	25953088
75	Methylation	MALKIPAKRIFGDNF HHCCCCHHHHHCCCC	40.44	23644510
121	Phosphorylation	RAFLQMDSPKHQSDP HHHHCCCCCCCCCCC	30.42	21815630
126	Phosphorylation	MDSPKHQSDPSEDED CCCCCCCCCCCCCCC	51.73	23401153
129	Phosphorylation	PKHQSDPSEDEDERS CCCCCCCCCCCCHHH	63.77	23401153
136	Phosphorylation	SEDEDERSSQKLHST CCCCCHHHHHHHHHC	34.76	29052541
137	Phosphorylation	EDEDERSSQKLHSTS CCCCHHHHHHHHHCC	37.24	24850871
139	Ubiquitination	EDERSSQKLHSTSQN CCHHHHHHHHHCCCC	50.55	-
142	Phosphorylation	RSSQKLHSTSQNINL HHHHHHHHCCCCCCC	39.94	27251275
143	Phosphorylation	SSQKLHSTSQNINLG HHHHHHHCCCCCCCC	24.47	27251275
144	Phosphorylation	SQKLHSTSQNINLGP HHHHHHCCCCCCCCC	25.01	27251275
158	Ubiquitination	PSGNPHAKPTDFDFL CCCCCCCCCCCCCCE	45.47	-
166	Ubiquitination	PTDFDFLKVIGKGSF CCCCCCEEEECCCCH	31.62	-
188	Phosphorylation	RKLDGKFYAVKVLQK ECCCCCEEHHEEHHH	17.61	-
191	Ubiquitination	DGKFYAVKVLQKKIV CCCEEHHEEHHHHHH	29.11	21890473
216	Ubiquitination	AERNVLLKNVKHPFL HHHCHHHHHCCCCEE	56.38	-
315	Phosphorylation	CKEGIAISDTTTTFC CCCCEEECCCCCCCC	21.63	22322096
318	Phosphorylation	GIAISDTTTTFCGTP CEEECCCCCCCCCCH	28.91	22322096
319	Phosphorylation	IAISDTTTTFCGTPE EEECCCCCCCCCCHH	21.70	28348404
320	Phosphorylation	AISDTTTTFCGTPEY EECCCCCCCCCCHHH	18.16	22322096
320 (in isoform 2)	Phosphorylation	-	18.16	10548550
324 (in isoform 2)	Phosphorylation	-	17.71	29507054
324	Phosphorylation	TTTTFCGTPEYLAPE CCCCCCCCHHHHCHH	17.71	22322096
407	Ubiquitination	RQNRLGAKEDFLEIQ HHCCCCCCCHHHHHC	56.89	-
461	Phosphorylation	TEETVPYSVCVSSDY CCCCCCCEEEECCCC	11.72	-
465	Phosphorylation	VPYSVCVSSDYSIVN CCCEEEECCCCCEEE	16.62	-
486	Phosphorylation	DDAFVGFSYAPPSED CCCCCCCCCCCCCHH	17.92	16888620

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	PDK1	Q15118	GPS
320	T	Phosphorylation	Kinase	PDK1	O15530	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
320	T	Phosphorylation	10548550
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	10548550
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GSK3B_HUMAN	GSK3B	physical	12054501
ITCH_HUMAN	ITCH	physical	16888620
A4_HUMAN	APP	physical	21832049
NED4L_HUMAN	NEDD4L	physical	23589291

Drug and Disease Associations

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

Regulatory Network of SGK3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Role of the Phox homology domain and phosphorylation in activation ofserum and glucocorticoid-regulated kinase-3."; Tessier M., Woodgett J.R.; J. Biol. Chem. 281:23978-23989(2006). Cited for: PHOSPHORYLATION AT THR-320 AND SER-486, AND MUTAGENESIS OF ARG-90 ANDLYS-191.	16790420 [Abstract]
"CISK attenuates degradation of the chemokine receptor CXCR4 via theubiquitin ligase AIP4."; Slagsvold T., Marchese A., Brech A., Stenmark H.; EMBO J. 25:3738-3749(2006). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITHC/AIP4, ANDPHOSPHORYLATION AT SER-486.	16888620 [Abstract]
"Characterization of the structure and regulation of two novelisoforms of serum- and glucocorticoid-induced protein kinase."; Kobayashi T., Deak M., Morrice N., Cohen P.; Biochem. J. 344:189-197(1999). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-320,AND MUTAGENESIS OF SER-486.	10548550 [Abstract]

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