Tag | Content |
---|
EKPD ID | EKS-ORC-00400 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
---|
AGC/SGK | 541.3 | 4.8E-163 | 98 | 355 | 258 |
|
Status | Reviewed |
Ensembl Protein | ENSOCUP00000018052 |
UniProt Accession | Q9XT18; |
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 | Oryctolagus cuniculus |
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 (By similarity). |
Protein Length | 431 |
Protein Sequence (FASTA) | MTVKTEAARG PLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK HTEVQSILKI 60 | SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE 120 | EAFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN 180 | GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD 240 | FGLCKENIEH NGTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR 300 | NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIR NHVFFSLINW 360 | DDLINKKITP PFNPNVSGPS DLRHFDPEFT EEPVPSSIGR SPDSILITAS VKEAAEAFLG 420 | FSYAPPMDSF L 431 |
|
Nucleotide Sequence (FASTA) | ATGACCGTGA AAACCGAGGC TGCTAGGGGC CCCCTCACTT ACTCCAGGAT GAGGGGCATG 60 | GTGGCCATCC TCATCGCGTT CATGAAGCAG AGGAGGATGG GCCTGAACGA CTTTATTCAG 120 | AAGATCGCTA ATAATTCCTA TGCGTGCAAG CACACTGAAG TTCAGTCCAT TTTGAAAATC 180 | TCCCAACCTC AGGAGCCCGA GCTTATGAAC GCCAACCCTT CGCCTCCGCC AAGTCCGTCT 240 | CAACAAATCA ACCTTGGCCC ATCATCAAAC CCTCATGCTA AACCATCAGA CTTTCACTTC 300 | CTAAAAGTGA TTGGAAAGGG CAGTTTTGGA AAGGTTCTAC TAGCAAGACA CAAAGCAGAG 360 | GAAGCCTTCT ATGCAGTCAA GGTGTTGCAG AAAAAAGCAA TCCTGAAAAA GAAGGAGGAG 420 | AAGCATATTA TGTCTGAGCG GAACGTGCTG CTGAAAAATG TGAAACACCC TTTCCTGGTG 480 | GGCCTGCACT TCTCCTTCCA GACGGCCGAC AAGCTGTACT TTGTCCTAGA CTACATTAAC 540 | GGTGGAGAGT TGTTCTACCA TCTCCAGAGG GAGCGCTGCT TCCTGGAACC ACGGGCTCGT 600 | TTCTATGCTG CTGAGATAGC CAGTGCCTTG GGTTACCTGC ACTCTCTGAA CATCGTTTAT 660 | AGAGACTTGA AGCCGGAGAA TATTCTACTA GATTCACAGG GACACATCGT CCTGACTGAC 720 | TTTGGGCTGT GCAAGGAGAA CATTGAACAC AACGGCACGA CGTCCACCTT CTGCGGCACA 780 | CCCGAGTATC TTGCACCTGA GGTGCTTCAT AAGCAGCCTT ATGACAGGAC GGTGGACTGG 840 | TGGTGCCTGG GGGCCGTCTT GTATGAGATG CTGTATGGCC TGCCTCCGTT TTATAGCCGA 900 | AACACAGCTG AGATGTACGA CAACATTCTG AACAAGCCTC TCCAGCTGAA ACCAAATATA 960 | ACAAATTCTG CAAGACACCT CCTAGAGGGC CTCCTGCAGA AGGACAGGAC AAAGAGACTC 1020 | GGGGCCAAGG ATGACTTTAT GGAGATTAGG AATCACGTCT TCTTCTCTCT AATTAACTGG 1080 | GACGATCTCA TTAATAAGAA GATTACGCCT CCTTTTAACC CAAATGTTAG TGGCCCCAGC 1140 | GACCTGCGGC ACTTTGATCC CGAGTTTACC GAAGAGCCTG TCCCCAGCTC CATCGGCAGG 1200 | TCCCCTGACA GCATCCTCAT CACGGCCAGC GTCAAGGAAG CGGCCGAGGC CTTCCTCGGC 1260 | TTCTCCTACG CGCCACCCAT GGACTCCTTC CTCTGA 1296 |
|
Domain Profile | S: 1 fdflkvigkgsfgkvllakrkadekfyavkvlqkkailkkkeekhimaernvllknvkhp 60 | f+flkvigkgsfgkvlla++ka+e+fyavkvlqkkailkkkeekhim+ernvllknvkhp | Q: 98 FHFLKVIGKGSFGKVLLARHKAEEAFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHP 157 | 9*********************************************************** |
| S: 61 flvglhysfqtaeklyfvldyvnggelffhlqrersfleprarfyaaeiasalgylhsln 120 | flvglh+sfqta+klyfvldy+nggelf+hlqrer+fleprarfyaaeiasalgylhsln | Q: 158 FLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLN 217 | ************************************************************ |
| S: 121 ivyrdlkpenilldskghvvltdfglckeeieaedttstfcgtpeylapevlrkkpydrt 180 | ivyrdlkpenillds+gh+vltdfglcke+ie++ ttstfcgtpeylapevl+k+pydrt | Q: 218 IVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNGTTSTFCGTPEYLAPEVLHKQPYDRT 277 | ************************************************************ |
| S: 181 vdwwclgavlyemlyglppfysrdvaemydnilnkplqlkpgisvaalelleellekdrk 240 | vdwwclgavlyemlyglppfysr++aemydnilnkplqlkp+i+++a++lle+ll+kdr+ | Q: 278 VDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRT 337 | ************************************************************ |
| S: 241 krlgakedfleiknhvff 258 | krlgak+df+ei+nhvff | Q: 338 KRLGAKDDFMEIRNHVFF 355 | *****************9 |
|
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 EIRNHVFF 258 |
|
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 |