Tag | Content |
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EKPD ID | EKS-RAN-00440 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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AGC/SGK | 540.6 | 8.4E-163 | 84 | 341 | 258 |
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Status | Reviewed |
Ensembl Protein | ENSRNOP00000046277 |
UniProt Accession | Q06226; |
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 | Rattus norvegicus |
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 SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. 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 (By similarity). Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. May also play an important role in the development of particular groups of neurons in the postnatal brain. |
Protein Length | 417 |
Protein Sequence (FASTA) | MREEALRSPW KAFMKQRRMG LNDFIQKLAN NSYACKHPEV QSYLKISQPQ EPELMNANPS 60 | PPPSPSQQIN LGPSSNPHAK PSDFHFLKVI GKGSFGKVLL ARHKAEEAFY AVKVLQKKAI 120 | LKKKEEKHIM SERNVLLKNV KHPFLVGLHF SFQTADKLYF VLDYINGGEL FYHLQRERCF 180 | LEPRARFYAA EIASALGYLH SLNIVYRDLK PENILLDSQG HIVLTDFGLC KENIEHNGTT 240 | STFCGTPEYL APEVLHKQPY DRTVDWWCLG AVLYEMLYGL PPFYSRNTAE MYDNILNKPL 300 | QLKPNITNSA RHLLEGLLQK DRTKRLGAKD DFMEIKSHIF FSLINWDDLI NKKITPPFNP 360 | NVSGPSDLRH FDPEFTEEPV PSSIGRSPDS ILVTASVKEA AEAFLGFSYA PPMDSFL 417 |
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Nucleotide Sequence (FASTA) | ATGAGAGAGG AGGCCTTAAG ATCCCCTTGG AAAGCTTTCA TGAAACAGAG AAGGATGGGC 60 | CTGAACGATT TTATTCAGAA GCTTGCCAAC AACTCCTATG CATGCAAACA CCCTGAAGTT 120 | CAATCCTATT TGAAAATCTC CCAACCTCAG GAGCCCGAAC TTATGAACGC CAACCCCTCA 180 | CCTCCTCCAA GTCCCTCTCA ACAAATCAAC CTGGGTCCAT CCTCAAATCC CCACGCCAAA 240 | CCCTCTGACT TCCACTTCTT GAAAGTGATC GGAAAAGGCA GTTTTGGAAA GGTTCTTCTA 300 | GCAAGGCACA AGGCAGAAGA AGCATTCTAT GCCGTCAAAG TTTTGCAGAA GAAAGCCATC 360 | TTGAAGAAGA AGGAGGAGAA GCATATTATG TCAGAGCGCA ATGTTCTGTT GAAGAATGTG 420 | AAGCACCCTT TCCTGGTGGG CCTTCACTTC TCTTTCCAGA CTGCTGACAA ACTCTACTTC 480 | GTCCTAGACT ACATTAATGG CGGAGAGCTG TTCTACCATC TCCAGAGGGA GCGCTGCTTC 540 | CTGGAACCCC GTGCTCGCTT CTACGCAGCT GAAATAGCCA GTGCCTTGGG TTATCTGCAC 600 | TCCCTAAACA TCGTTTATCG AGACTTAAAA CCAGAGAATA TTCTCCTAGA CTCACAGGGA 660 | CACATCGTCC TCACTGACTT TGGGCTCTGC AAGGAGAACA TCGAGCACAA TGGGACAACG 720 | TCCACCTTCT GTGGCACGCC TGAGTATCTC GCTCCTGAGG TTCTCCATAA GCAGCCGTAC 780 | GACCGGACAG TGGACTGGTG GTGCCTCGGG GCTGTCTTGT ATGAGATGCT CTATGGCCTG 840 | CCTCCGTTCT ACAGCCGGAA CACAGCCGAG ATGTATGACA ATATTCTGAA CAAGCCTCTC 900 | CAGCTGAAAC CAAATATCAC CAACTCAGCA AGGCACCTGC TGGAGGGCCT CCTGCAGAAG 960 | GACCGGACCA AGAGGCTGGG TGCCAAGGAT GACTTTATGG AGATTAAGAG TCATATTTTC 1020 | TTCTCTTTGA TTAACTGGGA TGATCTCATT AATAAGAAGA TCACGCCCCC ATTTAACCCA 1080 | AATGTGAGCG GGCCCAGTGA CCTTCGGCAC TTTGATCCCG AGTTTACTGA GGAGCCGGTC 1140 | CCCAGCTCCA TCGGGCGATC CCCTGACAGC ATCCTTGTCA CAGCCAGTGT GAAAGAAGCC 1200 | GCGGAAGCCT TCCTTGGCTT CTCCTATGCC CCTCCTATGG ACTCCTTCCT CTGA 1254 |
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Domain Profile | S: 1 fdflkvigkgsfgkvllakrkadekfyavkvlqkkailkkkeekhimaernvllknvkhp 60 | f+flkvigkgsfgkvlla++ka+e+fyavkvlqkkailkkkeekhim+ernvllknvkhp | Q: 84 FHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHP 143 | 9*********************************************************** |
| S: 61 flvglhysfqtaeklyfvldyvnggelffhlqrersfleprarfyaaeiasalgylhsln 120 | flvglh+sfqta+klyfvldy+nggelf+hlqrer+fleprarfyaaeiasalgylhsln | Q: 144 FLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLN 203 | ************************************************************ |
| S: 121 ivyrdlkpenilldskghvvltdfglckeeieaedttstfcgtpeylapevlrkkpydrt 180 | ivyrdlkpenillds+gh+vltdfglcke+ie++ ttstfcgtpeylapevl+k+pydrt | Q: 204 IVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRT 263 | ************************************************************ |
| S: 181 vdwwclgavlyemlyglppfysrdvaemydnilnkplqlkpgisvaalelleellekdrk 240 | vdwwclgavlyemlyglppfysr++aemydnilnkplqlkp+i+++a++lle+ll+kdr+ | Q: 264 VDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRT 323 | ************************************************************ |
| S: 241 krlgakedfleiknhvff 258 | krlgak+df+eik+h+ff | Q: 324 KRLGAKDDFMEIKSHIFF 341 | *****************9 |
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Domain Sequence (FASTA) | FHFLKVIGKG SFGKVLLARH KAEEAFYAVK 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 |
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Keyword | 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 | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |