ID H2R6X6_PANTR Unreviewed; 526 AA.
AC H2R6X6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Serine/threonine-protein kinase Sgk1 {ECO:0000256|ARBA:ARBA00041082};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Serum/glucocorticoid-regulated kinase 1 {ECO:0000256|ARBA:ARBA00042467};
GN Name=SGK1 {ECO:0000313|Ensembl:ENSPTRP00000049596.4,
GN ECO:0000313|VGNC:VGNC:11250};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000049596.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000049596.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000049596.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; AACZ04054438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2R6X6; -.
DR Ensembl; ENSPTRT00000046204.5; ENSPTRP00000049596.4; ENSPTRG00000018626.6.
DR VGNC; VGNC:11250; SGK1.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000155726; -.
DR HOGENOM; CLU_000288_63_48_1; -.
DR TreeFam; TF320906; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018626; Expressed in Brodmann (1909) area 10 and 21 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05575; STKc_SGK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF184; SERINE_THREONINE-PROTEIN KINASE SGK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 193..450
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 451..526
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 161..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 526 AA; 59702 MW; 9DB4034233183BBA CRC64;
MVNKDMNGFP VKKCSAFQFF KKRVRRWIKS PMVSVDKHQS PSLKYTGSSI VHIPPGEPDF
ESSLCQTCLG EHAFQRGVLP QENESCSWET QSECEVSSLC VAPDVMKPSK RFFISPPSST
AFMKQRRMGL NDFIQKIANN SYACKHPEVQ SILKISQPQE PELMNANPSP PPSPSQQINL
GPSSNPHAKP SDFHFLKVIG KGSFGKVLLA RHKAEEVFYA VKVLQKKAIL KKKEEKHIMS
ERNVLLKNVK HPFLVGLHFS FQTADKLYFV LDYINGGELF YHLQRERCFL EPRARFYAAE
IASALGYLHS LNIVYRDLKP ENILLDSQGH IVLTDFGLCK ENIEHNSTTS TFCGTPEYLA
PEVLHKQPYD RTVDWWCLGA VLYEMLYGLP PFYSRNTAEM YDNILNKPLQ LKPNITNSAR
HLLEGLLQKD RTKRLGAKDD FMEIKSHVFF SLINWDDLIN KKITPPFNPN VSGPNDLRHF
DPEFTEEPVP NSIGKSPDSV LVTASVKEAA EAFLGFSYAP PTDSFL
//
