| Tag | Content |
|---|
| EKPD ID | EKS-MUM-00455 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| AGC/SGK | 540.6 | 1.7E-162 | 71 | 328 | 258 |
|
| Status | Reviewed |
| Ensembl Protein | ENSMUSP00000128873 |
| UniProt Accession | Q9WVC6; Q3TJN4; Q3UKD0; Q3UKF2; Q3V1V1; Q6NS85; |
| Protein Name | Serine/threonine-protein kinase Sgk1 |
| Protein Synonyms/Alias | Serum/glucocorticoid-regulated kinase 1; |
| Gene Name | Sgk1 |
| Gene Synonyms/Alias | Sgk1; Sgk; |
| Ensembl Information | |
| Organism | Mus musculus |
| Functional Description | Serine/threonine-protein kinase which is involved in theregulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. |
| Protein Length | 404 |
Protein Sequence
(FASTA) | | MKQRRMGLND FIQKIASNTY ACKHAEVQSI LKMSHPQEPE LMNANPSPPP SPSQQINLGP 60 | | SSNPHAKPSD FHFLKVIGKG SFGKVLLARH KAEEVFYAVK VLQKKAILKK KEEKHIMSER 120 | | NVLLKNVKHP FLVGLHFSFQ TADKLYFVLD YINGGELFYH LQRERCFLEP RARFYAAEIA 180 | | SALGYLHSLN IVYRDLKPEN ILLDSQGHIV LTDFGLCKEN IEHNGTTSTF CGTPEYLAPE 240 | | VLHKQPYDRT VDWWCLGAVL YEMLYGLPPF YSRNTAEMYD NILNKPLQLK PNITNSARHL 300 | | LEGLLQKDRT KRLGAKDDFM EIKSHIFFSL INWDDLINKK ITPPFNPNVS GPSDLRHFDP 360 | | EFTEEPVPSS IGRSPDSILV TASVKEAAEA FLGFSYAPPV DSFL 404 |
|
Nucleotide Sequence
(FASTA) | | ATGAAACAGA GAAGGATGGG CCTGAACGAT TTTATTCAGA AGATTGCCAG CAACACCTAT 60 | | GCATGCAAAC ACGCTGAAGT TCAGTCCATT TTGAAAATGT CCCATCCTCA GGAGCCGGAG 120 | | CTTATGAACG CTAACCCCTC TCCTCCGCCA AGTCCCTCTC AACAAATCAA CCTGGGTCCG 180 | | TCCTCCAACC CTCACGCCAA ACCCTCCGAC TTTCACTTCT TGAAAGTGAT CGGAAAGGGC 240 | | AGTTTTGGAA AGGTTCTTCT GGCTAGGCAC AAGGCAGAAG AAGTATTCTA TGCAGTCAAA 300 | | GTTTTACAGA AGAAAGCCAT CCTGAAGAAG AAAGAGGAGA AGCATATTAT GTCAGAGCGG 360 | | AATGTTCTGT TGAAGAATGT GAAGCACCCT TTCCTGGTGG GCCTTCACTT CTCATTCCAG 420 | | ACCGCTGACA AGCTCTACTT TGTCCTGGAC TACATTAATG GTGGAGAGCT GTTCTACCAT 480 | | CTCCAGAGGG AGCGCTGCTT CCTGGAACCA CGGGCTCGAT TCTACGCAGC TGAAATAGCC 540 | | AGTGCCCTGG GCTATCTGCA CTCCCTAAAC ATCGTTTATA GAGACTTAAA ACCTGAGAAT 600 | | ATTCTCCTAG ACTCCCAGGG GCACATCGTC CTCACTGACT TTGGGCTCTG CAAAGAGAAT 660 | | ATTGAGCATA ACGGGACAAC ATCTACCTTC TGTGGCACGC CTGAGTATCT GGCTCCTGAG 720 | | GTCCTCCATA AGCAGCCGTA TGACCGGACG GTGGACTGGT GGTGTCTTGG GGCTGTCCTG 780 | | TATGAGATGC TCTACGGCCT GCCCCCGTTT TATAGCCGGA ACACGGCTGA GATGTACGAC 840 | | AATATTCTGA ACAAGCCTCT CCAGTTGAAA CCAAATATTA CAAACTCGGC AAGGCACCTC 900 | | CTGGAAGGCC TCCTGCAGAA GGACCGGACC AAGAGGCTGG GTGCCAAGGA TGACTTTATG 960 | | GAGATTAAGA GTCATATTTT CTTCTCTTTA ATTAACTGGG ATGATCTCAT CAATAAGAAG 1020 | | ATTACACCCC CATTTAACCC AAATGTGAGT GGGCCCAGTG ACCTTCGGCA CTTCGATCCC 1080 | | GAGTTTACCG AGGAGCCGGT CCCCAGCTCC ATCGGCAGGT CCCCTGACAG CATCCTTGTC 1140 | | ACGGCCAGTG TGAAGGAAGC AGCAGAAGCC TTCCTCGGCT TCTCCTATGC ACCTCCTGTG 1200 | | GATTCCTTCC TCTGA 1215 |
|
| Domain Profile | S: 1 fdflkvigkgsfgkvllakrkadekfyavkvlqkkailkkkeekhimaernvllknvkhp 60 | f+flkvigkgsfgkvlla++ka+e+fyavkvlqkkailkkkeekhim+ernvllknvkhp | Q: 71 FHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHP 130 | 9*********************************************************** |
| S: 61 flvglhysfqtaeklyfvldyvnggelffhlqrersfleprarfyaaeiasalgylhsln 120 | flvglh+sfqta+klyfvldy+nggelf+hlqrer+fleprarfyaaeiasalgylhsln | Q: 131 FLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLN 190 | ************************************************************ |
| S: 121 ivyrdlkpenilldskghvvltdfglckeeieaedttstfcgtpeylapevlrkkpydrt 180 | ivyrdlkpenillds+gh+vltdfglcke+ie++ ttstfcgtpeylapevl+k+pydrt | Q: 191 IVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRT 250 | ************************************************************ |
| S: 181 vdwwclgavlyemlyglppfysrdvaemydnilnkplqlkpgisvaalelleellekdrk 240 | vdwwclgavlyemlyglppfysr++aemydnilnkplqlkp+i+++a++lle+ll+kdr+ | Q: 251 VDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRT 310 | ************************************************************ |
| S: 241 krlgakedfleiknhvff 258 | krlgak+df+eik+h+ff | Q: 311 KRLGAKDDFMEIKSHIFF 328 | *****************9 |
|
Domain Sequence
(FASTA) | | FHFLKVIGKG SFGKVLLARH KAEEVFYAVK VLQKKAILKK KEEKHIMSER NVLLKNVKHP 60 | | FLVGLHFSFQ TADKLYFVLD YINGGELFYH LQRERCFLEP RARFYAAEIA SALGYLHSLN 120 | | IVYRDLKPEN ILLDSQGHIV LTDFGLCKEN IEHNGTTSTF CGTPEYLAPE VLHKQPYDRT 180 | | VDWWCLGAVL YEMLYGLPPF YSRNTAEMYD NILNKPLQLK PNITNSARHL LEGLLQKDRT 240 | | KRLGAKDDFM EIKSHIFF 258 |
|
| Keyword | Alternative splicing; Apoptosis; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Disulfide bond; Endoplasmic reticulum; Kinase; Membrane; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Stress response; Transferase; Ubl conjugation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
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| Pfam | |
| SMARTs | |
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| Prints | |
| Created Date | 20-Feb-2013 |