STK40_PONAB
ID STK40_PONAB Reviewed; 435 AA.
AC Q5R667;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Serine/threonine-protein kinase 40;
DE EC=2.7.11.1;
GN Name=STK40;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be a negative regulator of NF-kappa-B and p53-mediated
CC gene transcription. {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; CR860629; CAH92749.1; -; mRNA.
DR RefSeq; NP_001126603.1; NM_001133131.1.
DR AlphaFoldDB; Q5R667; -.
DR SMR; Q5R667; -.
DR STRING; 9601.ENSPPYP00000001776; -.
DR GeneID; 100173600; -.
DR KEGG; pon:100173600; -.
DR CTD; 83931; -.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q5R667; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd13974; STKc_SHIK; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR024236; Ser/Thr_kinase_40.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR PANTHER; PTHR22961; PTHR22961; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..435
FT /note="Serine/threonine-protein kinase 40"
FT /id="PRO_0000252263"
FT DOMAIN 35..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 435 AA; 48985 MW; 9A6AE818AB50BF51 CRC64;
MKRRASDRGA GETSARAKAL GSGISGNNAK RAGPFILGPR LGNSPVPSIV QCLARKDGTD
DFYQLKILTL EERGDQGIES QEERQGKMLL HTEYSLLSLL HTQDGVVHHH GLFQDRTCEI
VEDTESSRMV KKMKKRICLV LDCLCAHDFS DKTADLINLQ HYVIKEKRLS ERETVVIFYD
VVRVVEALHQ KNIVHRDLKL GNMVLNKRTH RITITNFCLG KHPVSEGDLL KDQRGSPAYI
SPDVLSGRPY RGKPSDMWAL GVVLFTMLYG QFPFYDSIPQ ELFRKIKAAE YTIPEDGRVS
ENTVCLIRKL LVLDPQQRLA AADVLEALSA IIASWQSLSS LSGPLQVVPD IDDQMSNADS
SQEAKVTEEC SQYEFENYMR QQLLLAEEKS SIHDARSWVP KRQFGSAPPV RRLGHDAQPM
TSLDTAILAQ RYLRK