| Tag | Content |
|---|
| CPLM ID | CPLM-021100 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase Sgk3 |
Protein Synonyms/Alias | Cytokine-independent survival kinase; Serum/glucocorticoid-regulated kinase 3; Serum/glucocorticoid-regulated kinase-like |
Gene Name | Sgk3 |
Gene Synonyms/Alias | Cisk; Sgkl |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 71 | QFPAMALKIPAKRIF | acetylation | [1] | | 71 | QFPAMALKIPAKRIF | succinylation | [1] | | 166 | PTDFDFLKVIGKGSF | ubiquitination | [2] |
|
Reference | [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways. Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y. Mol Cell. 2013 Jun 27;50(6):919-30. [ PMID: 23806337] [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional 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. |
Sequence Annotation | DOMAIN 12 124 PX.
DOMAIN 162 419 Protein kinase.
DOMAIN 420 496 AGC-kinase C-terminal.
NP_BIND 168 176 ATP (By similarity).
MOTIF 195 205 Nuclear localization signal (By
ACT_SITE 286 286 Proton acceptor (By similarity).
BINDING 191 191 ATP (By similarity).
MOD_RES 126 126 Phosphoserine.
MOD_RES 129 129 Phosphoserine.
MOD_RES 320 320 Phosphothreonine; by PDPK1 (By
MOD_RES 486 486 Phosphoserine (By similarity). |
Keyword | 3D-structure; ATP-binding; Complete proteome; Cytoplasmic vesicle; Endosome; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 496 AA |
Protein Sequence | MQRDCIMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNS 60
LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD 120
SPRHQSDPSE DEDERSTSKP HSTSRNINLG PTGNPHAKPT DFDFLKVIGK GSFGKVLLAK 180
RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL 240
DFVNGGELFF HLQRERSFPE PRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSMGHV 300
VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV LYEMLYGLPP 360
FYCRDVAEMY DNILHKPLNL RPGVSLTAWS ILEELLEKNR QNRLGAKEDF LEIQNHPFFE 420
SLSWTDLVQK KIPPPFNPNV AGPDDIRNFD AVFTEETVPY SVCVSSDYSI VNASVLEADD 480
AFVGFSYAPP SEDLFL 496 |
Gene Ontology | GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI. GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. GO:0007154; P:cell communication; IEA:InterPro. GO:0043066; P:negative regulation of apoptotic process; IDA:MGI. |
Interpro | |
Pfam | |
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PRINTS | |