Q96BR1 (SGK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Sgk3
EC=2.7.11.1

Alternative name(s):
Cytokine-independent survival kinase
Serum/glucocorticoid-regulated kinase 3
Serum/glucocorticoid-regulated kinase-like

Gene names

Name:	SGK3
Synonyms:	CISK, SGKL

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	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 Ca2+ 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Two specific sites, one in the kinase domain (Thr-320) and the other in the C-terminal regulatory region (Ser-486), need to be phosphorylated for its full activation.
Subunit structure	Interacts with GSK3B and FLII. Interacts with PDPK1 in a phosphorylation-dependent manner. Ref.7 Ref.17 Ref.24 Ref.27
Subcellular location	Cytoplasmic vesicle By similarity. Early endosome. Recycling endosome. Note: Endosomal localization is a prerequisite for complete kinase activity. It is essential for its co-localization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosphorylation of Thr-320 resulting in complete activation of SGK3. Localized in vesicle-like structures and in the early endosome. Co-localizes with SLC9A3/NHE3 in the recycling endosomes. Ref.24 Ref.29
Tissue specificity	Expressed in most tissues with highest levels in pancreas, kidney liver, heart and brain and lower levels in lung, placenta and skeletal muscle. Expression is higher in ER-positive breast tumors than ER-negative breast tumors. Ref.30
Induction	Induced by estrogen/ER in breast cancer cells. Ref.30
Post-translational modification	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.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain. Contains 1 PX (phox homology) domain.
Sequence caution	The sequence AAF12758.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Endosome
Coding sequence diversity	Alternative splicing 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	cell communication Inferred from electronic annotation. Source: InterPro negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara regulation of cell growth Traceable author statement Ref.32. Source: UniProtKB regulation of cell migration Traceable author statement Ref.32. Source: UniProtKB regulation of cell proliferation Traceable author statement Ref.32. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Traceable author statement Ref.32. Source: UniProtKB response to stress Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium channel regulator activity Traceable author statement Ref.31. Source: UniProtKB chloride channel regulator activity Traceable author statement Ref.31. Source: UniProtKB phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro potassium channel regulator activity Traceable author statement Ref.31. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc sodium channel regulator activity Traceable author statement Ref.31. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96BR1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q96BR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     327-358: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Serine/threonine-protein kinase Sgk3		PRO_0000086649
Regions
	Domain	12 – 124	113	PX
	Domain	162 – 419	258	Protein kinase
	Domain	420 – 496	77	AGC-kinase C-terminal
	Nucleotide binding	168 – 176	9	ATP By similarity
	Motif	195 – 205	11	Nuclear localization signal By similarity
Sites
	Active site	286	1	Proton acceptor By similarity
	Binding site	191	1	ATP By similarity
Amino acid modifications
	Modified residue	126	1	Phosphoserine By similarity
	Modified residue	129	1	Phosphoserine By similarity
	Modified residue	320	1	Phosphothreonine; by PDPK1 Ref.1 Ref.25
	Modified residue	486	1	Phosphoserine Ref.24 Ref.25
Natural variations
	Alternative sequence	327 – 358	32	Missing in isoform 2.		VSP_041903
	Natural variant	92	1	A → V in a breast cancer sample; somatic mutation. Ref.33		VAR_035636
	Natural variant	355	1	L → P. Ref.34		VAR_041076
Experimental info
	Mutagenesis	90	1	R → A: Partially localized to the membrane. Ref.25
	Mutagenesis	191	1	K → M: Abolishes activity. Ref.25
	Mutagenesis	486	1	S → D: Increased activation. Ref.1
	Sequence conflict	54	1	F → V in AAF27051. Ref.2
	Sequence conflict	127	1	D → G in AAF27051. Ref.2
	Sequence conflict	187	1	F → V in AAF27051. Ref.2
	Sequence conflict	294	1	L → V in AAF27051. Ref.2
	Sequence conflict	387	1	T → R in AAF27051. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 76A6CCEB69006CF1	FASTA	496	57,108
	10 20 30 40 50 60 MQRDHTMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNT 70 80 90 100 110 120 LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD 130 140 150 160 170 180 SPKHQSDPSE DEDERSSQKL HSTSQNINLG PSGNPHAKPT DFDFLKVIGK GSFGKVLLAK 190 200 210 220 230 240 RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL 250 260 270 280 290 300 DFVNGGELFF HLQRERSFPE HRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSVGHV 310 320 330 340 350 360 VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV LYEMLYGLPP 370 380 390 400 410 420 FYCRDVAEMY DNILHKPLSL RPGVSLTAWS ILEELLEKDR QNRLGAKEDF LEIQNHPFFE 430 440 450 460 470 480 SLSWADLVQK KIPPPFNPNV AGPDDIRNFD TAFTEETVPY SVCVSSDYSI VNASVLEADD 490 AFVGFSYAPP SEDLFL
	Isoform 2 [UniParc]. Checksum: D5028F96C651C465	FASTA	464	53,306
	10 20 30 40 50 60 MQRDHTMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNT 70 80 90 100 110 120 LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD 130 140 150 160 170 180 SPKHQSDPSE DEDERSSQKL HSTSQNINLG PSGNPHAKPT DFDFLKVIGK GSFGKVLLAK 190 200 210 220 230 240 RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL 250 260 270 280 290 300 DFVNGGELFF HLQRERSFPE HRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSVGHV 310 320 330 340 350 360 VLTDFGLCKE GIAISDTTTT FCGTPEPPFY CRDVAEMYDN ILHKPLSLRP GVSLTAWSIL 370 380 390 400 410 420 EELLEKDRQN RLGAKEDFLE IQNHPFFESL SWADLVQKKI PPPFNPNVAG PDDIRNFDTA 430 440 450 460 FTEETVPYSV CVSSDYSIVN ASVLEADDAF VGFSYAPPSE DLFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase." Kobayashi T., Deak M., Morrice N., Cohen P. Biochem. J. 344:189-197(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-320, MUTAGENESIS OF SER-486.
[2]	"Cloning and mapping of a novel human Serum/Glucocorticoid regulated kinase-like gene, SGKL, to chromosome 8q12.3-q13.1." Dai F., Yu L., He H., Zhao Y., Yang J., Zhang X., Zhao S. Genomics 62:95-97(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	Zhao Y. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain and Mammary gland.
[5]	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].
[6]	"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] (ISOFORM 1). Tissue: Mammary gland.
[7]	"Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction." Dai F., Yu L., He H., Chen Y., Yu J., Yang Y., Xu Y., Ling W., Zhao S. Biochem. Biophys. Res. Commun. 293:1191-1196(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GSK3B, INTERACTION WITH GSK3B.
[8]	"Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent kinase isoforms." Henke G., Setiawan I., Boehmer C., Lang F. Kidney Blood Press. Res. 25:370-374(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF NA(+)/K(+) ATPASE.
[9]	"K(+) channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK." Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G., Huber S.M., Kobayashi T., Cohen P., Lang F. Pflugers Arch. 445:60-66(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Serum and glucocorticoid inducible kinases in the regulation of the cardiac sodium channel SCN5A." Boehmer C., Wilhelm V., Palmada M., Wallisch S., Henke G., Brinkmeier H., Cohen P., Pieske B., Lang F. Cardiovasc. Res. 57:1079-1084(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SCN5A.
[11]	"Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B." Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D., Broeer S., Lang F. J. Neurochem. 86:1181-1188(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC1A3/EAAT1.
[12]	"Regulation of KCNE1-dependent K(+) current by the serum and glucocorticoid-inducible kinase (SGK) isoforms." Embark H.M., Boehmer C., Vallon V., Luft F., Lang F. Pflugers Arch. 445:601-606(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF KCNE1 AND KCNQ1.
[13]	"The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel alpha,beta,gamma-ENaC." Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S., Wang J., Pearce D., Lang F. Pflugers Arch. 445:693-696(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SCNN1A/ENAC.
[14]	"Regulation of intestinal phosphate cotransporter NaPi IIb by ubiquitin ligase Nedd4-2 and by serum- and glucocorticoid-dependent kinase 1." Palmada M., Dieter M., Speil A., Boehmer C., Mack A.F., Wagner H.J., Klingel K., Kandolf R., Murer H., Biber J., Closs E.I., Lang F. Am. J. Physiol. 287:G143-G150(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC34A2/NAPI-2B, FUNCTION IN PHOSPHORYLATION OF NEDD4L.
[15]	"Stimulation of renal Na+ dicarboxylate cotransporter 1 by Na+/H+ exchanger regulating factor 2, serum and glucocorticoid inducible kinase isoforms, and protein kinase B." Boehmer C., Embark H.M., Bauer A., Palmada M., Yun C.H., Weinman E.J., Endou H., Cohen P., Lahme S., Bichler K.H., Lang F. Biochem. Biophys. Res. Commun. 313:998-1003(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC13A2/NADC1.
[16]	"Regulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase isoforms SGK1 and SGK3 expressed in Xenopus oocytes." Embark H.M., Setiawan I., Poppendieck S., van de Graaf S.F., Boehmer C., Palmada M., Wieder T., Gerstberger R., Cohen P., Yun C.C., Bindels R.J., Lang F. Cell. Physiol. Biochem. 14:203-212(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF TRPV5.
[17]	"Peroxisomal targeting as a tool for assaying protein-protein interactions in the living cell: cytokine-independent survival kinase (CISK) binds PDK-1 in vivo in a phosphorylation-dependent manner." Nilsen T., Slagsvold T., Skjerpen C.S., Brech A., Stenmark H., Olsnes S. J. Biol. Chem. 279:4794-4801(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDPK1, PHOSPHORYLATION BY PDPK1.
[18]	"Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1." Henke G., Maier G., Wallisch S., Boehmer C., Lang F. J. Cell. Physiol. 199:194-199(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF KCNA3/KV1.3.
[19]	"Regulation of CLC-Ka/barttin by the ubiquitin ligase Nedd4-2 and the serum- and glucocorticoid-dependent kinases." Embark H.M., Boehmer C., Palmada M., Rajamanickam J., Wyatt A.W., Wallisch S., Capasso G., Waldegger P., Seyberth H.W., Waldegger S., Lang F. Kidney Int. 66:1918-1925(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF BSND.
[20]	"The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid transporter ASCT2." Palmada M., Speil A., Jeyaraj S., Boehmer C., Lang F. Biochem. Biophys. Res. Commun. 331:272-277(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC1A5/ASCT2.
[21]	"Regulation of the excitatory amino acid transporter EAAT5 by the serum and glucocorticoid dependent kinases SGK1 and SGK3." Boehmer C., Rajamanickam J., Schniepp R., Kohler K., Wulff P., Kuhl D., Palmada M., Lang F. Biochem. Biophys. Res. Commun. 329:738-742(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC1A7/EAAT5.
[22]	"Stimulation of the creatine transporter SLC6A8 by the protein kinases SGK1 and SGK3." Shojaiefard M., Christie D.L., Lang F. Biochem. Biophys. Res. Commun. 334:742-746(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC6A8.
[23]	"Upregulation of HERG channels by the serum and glucocorticoid inducible kinase isoform SGK3." Maier G., Palmada M., Rajamanickam J., Shumilina E., Boehmer C., Lang F. Cell. Physiol. Biochem. 18:177-186(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF KCNH2/HERG.
[24]	"CISK attenuates degradation of the chemokine receptor CXCR4 via the ubiquitin ligase AIP4." Slagsvold T., Marchese A., Brech A., Stenmark H. EMBO J. 25:3738-3749(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITHC/AIP4, PHOSPHORYLATION AT SER-486.
[25]	"Role of the Phox homology domain and phosphorylation in activation of serum and glucocorticoid-regulated kinase-3." Tessier M., Woodgett J.R. J. Biol. Chem. 281:23978-23989(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-320 AND SER-486, MUTAGENESIS OF ARG-90 AND LYS-191.
[26]	"Regulation of the epithelial calcium channel TRPV6 by the serum and glucocorticoid-inducible kinase isoforms SGK1 and SGK3." Boehmer C., Palmada M., Kenngott C., Lindner R., Klaus F., Laufer J., Lang F. FEBS Lett. 581:5586-5590(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF TRPV6.
[27]	"Identification of Flightless-I as a substrate of the cytokine-independent survival kinase CISK." Xu J., Liao L., Qin J., Xu J., Liu D., Songyang Z. J. Biol. Chem. 284:14377-14385(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FLII, INTERACTION WITH FLII.
[28]	"The serum and glucocorticoid inducible kinases SGK1-3 stimulate the neutral amino acid transporter SLC6A19." Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S., Lang F., Palmada M. Cell. Physiol. Biochem. 25:723-732(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC6A19.
[29]	"Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates acute activation of Na+/H+ exchanger NHE3 by glucocorticoids." He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G., Naray-Fejes-Toth A., Yun C.C. Mol. Biol. Cell 22:3812-3825(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC9A3/NHE3, SUBCELLULAR LOCATION.
[30]	"SGK3 is an estrogen-inducible kinase promoting estrogen-mediated survival of breast cancer cells." Wang Y., Zhou D., Phung S., Masri S., Smith D., Chen S. Mol. Endocrinol. 25:72-82(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, TISSUE SPECIFICITY.
[31]	"Sgk kinases and their role in epithelial transport." Loffing J., Flores S.Y., Staub O. Annu. Rev. Physiol. 68:461-490(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[32]	"Second AKT: the rise of SGK in cancer signalling." Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E. Growth Factors 28:394-408(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[33]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-92.
[34]	"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: VARIANT [LARGE SCALE ANALYSIS] PRO-355.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF169035 mRNA. Translation: AAF12758.1. Different initiation. AF085233 mRNA. Translation: AAF27051.2. AK074666 mRNA. Translation: BAG51984.1. AK291428 mRNA. Translation: BAF84117.1. AC011031 Genomic DNA. No translation available. AC090154 Genomic DNA. No translation available. CH471068 Genomic DNA. Translation: EAW86919.1. BC015326 mRNA. Translation: AAH15326.1.
IPI	IPI00655852.
RefSeq	NP_001028750.1. NM_001033578.2. NP_001191102.1. NM_001204173.1. NP_037389.4. NM_013257.4. NP_733827.2. NM_170709.2.
UniGene	Hs.613417. Hs.733251.
3D structure databases
ProteinModelPortal	Q96BR1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96BR1. 3 interactions.
MINT	MINT-2813751.
STRING	9606.ENSP00000262211.
PTM databases
PhosphoSite	Q96BR1.
Polymorphism databases
DMDM	28558163.
Proteomic databases
PaxDb	Q96BR1.
PRIDE	Q96BR1.
Protocols and materials databases
DNASU	23678.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262211; ENSP00000262211; ENSG00000104205. ENST00000345714; ENSP00000331816; ENSG00000104205. ENST00000396596; ENSP00000379842; ENSG00000104205. ENST00000519289; ENSP00000429022; ENSG00000104205. ENST00000520976; ENSP00000430691; ENSG00000104205. ENST00000521198; ENSP00000430463; ENSG00000104205. ENST00000522398; ENSP00000430256; ENSG00000104205.
GeneID	100533105. 23678.
KEGG	hsa:100533105. hsa:23678.
UCSC	uc003xwp.3. human.
Organism-specific databases
CTD	100533105. 23678.
GeneCards	GC08P067624.
HGNC	HGNC:10812. SGK3.
HPA	HPA027146.
MIM	607591. gene.
neXtProt	NX_Q96BR1.
PharmGKB	PA35722.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	Q96BR1.
KO	K13304.
OMA	HPELYNH.
OrthoDB	EOG40GCQK.
PhylomeDB	Q96BR1.
Gene expression databases
ArrayExpress	Q96BR1.
Bgee	Q96BR1.
CleanEx	HS_SGK2. HS_SGK3.
Genevestigator	Q96BR1.
GermOnline	ENSG00000104205. Homo sapiens.
Family and domain databases
Gene3D	3.30.1520.10. 1 hit.
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR001683. Phox. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. PF00787. PX. 1 hit. [Graphical view]
SMART	SM00312. PX. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF64268. PX. 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. PS50195. PX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q96BR1.
ChEMBL	CHEMBL6186.
NextBio	46545.
SOURCE	Search...

Entry information

Entry name

SGK3_HUMAN

Accession

Primary (citable) accession number: Q96BR1
Secondary accession number(s): A8K5W3 , B3KQC2, Q9P1Q7, Q9UKG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 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.