STK38_BOVIN
ID STK38_BOVIN Reviewed; 465 AA.
AC A2VDV2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Serine/threonine-protein kinase 38;
DE EC=2.7.11.1;
GN Name=STK38;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2
CC from its phosphorylated form to its non-phosphorylated form and
CC inhibits autophosphorylation of MAP3K2 (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by binding of S100B which releases
CC autoinhibitory N-lobe interactions, enabling ATP to bind and the
CC autophosphorylation of Ser-281. Thr-444 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-444 and the N-lobe promote additional structural
CC changes that complete the activation of the kinase. Autoinhibition is
CC also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N-
CC terminal of STK38 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38. Interacts with
CC MOB1 and MOB2. Interacts with MAP3K1 and MAP3K2 (via the kinase
CC domain). Forms a tripartite complex with MOBKL1B and STK3/MST2.
CC Interacts with MICAL1; leading to inhibit the protein kinase activity
CC by antagonizing activation by MST1/STK4. {ECO:0000250|UniProtKB:Q15208,
CC ECO:0000250|UniProtKB:Q91VJ4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC133417; AAI33418.1; -; mRNA.
DR RefSeq; NP_001075071.1; NM_001081602.1.
DR AlphaFoldDB; A2VDV2; -.
DR BMRB; A2VDV2; -.
DR SMR; A2VDV2; -.
DR STRING; 9913.ENSBTAP00000015663; -.
DR PaxDb; A2VDV2; -.
DR PRIDE; A2VDV2; -.
DR Ensembl; ENSBTAT00000015663; ENSBTAP00000015663; ENSBTAG00000011126.
DR GeneID; 533677; -.
DR KEGG; bta:533677; -.
DR CTD; 11329; -.
DR VEuPathDB; HostDB:ENSBTAG00000011126; -.
DR VGNC; VGNC:35399; STK38.
DR eggNOG; KOG0605; Eukaryota.
DR GeneTree; ENSGT00940000153544; -.
DR InParanoid; A2VDV2; -.
DR OMA; YTYKKSD; -.
DR OrthoDB; 759391at2759; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000011126; Expressed in blood and 105 other tissues.
DR ExpressionAtlas; A2VDV2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
FT CHAIN 2..465
FT /note="Serine/threonine-protein kinase 38"
FT /id="PRO_0000297526"
FT DOMAIN 89..382
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 383..455
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 62..87
FT /note="Interaction with S100B"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 95..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
FT MOD_RES 281
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
FT MOD_RES 444
FT /note="Phosphothreonine; by STK24/MST3"
FT /evidence="ECO:0000250|UniProtKB:Q15208"
SQ SEQUENCE 465 AA; 54176 MW; C1BD09EB19C693D9 CRC64;
MAMTGSTPCS SMSSHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK VMEEEGLKDE
EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL
RKADMLEKEQ VGHIRAERDI LVEADSLWVV KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK
KDTLTEEETQ FYIAETVLAI DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA
HRTEFYRNLN HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN
KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS EKAKDLILRF
CCEWEHRIGA PGVEEIKNNS FFEGVDWEHI RERPAAISIE IKSIDDTSNF DEFPESDILK
PTVATSNHPD TDYKNKDWVF INYTYKRFEG LTARGAIPSY MKAAK
