STK40_MOUSE
ID STK40_MOUSE Reviewed; 435 AA.
AC Q7TNL3; B1AW01; Q3U3G3; Q811D6; Q8BKT1; Q9D7K3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase 40;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase lyk4;
GN Name=Stk40; Synonyms=Lyk4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of human, mouse, rat, chick and frog lyk4
RT gene.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=15893606; DOI=10.1016/j.molbrainres.2005.02.008;
RA Matsuki T., Hori G., Furuichi T.;
RT "Gene expression profiling during the embryonic development of mouse brain
RT using an oligonucleotide-based microarray system.";
RL Brain Res. Mol. Brain Res. 136:231-254(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, ICR, and NOD; TISSUE=Brain, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- INTERACTION:
CC Q7TNL3-1; Q8BP92: Rcn2; NbExp=3; IntAct=EBI-15828080, EBI-642694;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TNL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TNL3-2; Sequence=VSP_020901;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY336057; AAQ01591.1; -; mRNA.
DR EMBL; AB102946; BAC81568.1; -; mRNA.
DR EMBL; AK009154; BAB26110.2; -; mRNA.
DR EMBL; AK050808; BAC34419.2; -; mRNA.
DR EMBL; AK154780; BAE32823.1; -; mRNA.
DR EMBL; AL731780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046981; AAH46981.1; ALT_INIT; mRNA.
DR CCDS; CCDS51299.1; -. [Q7TNL3-2]
DR CCDS; CCDS51300.1; -. [Q7TNL3-1]
DR RefSeq; NP_001139299.1; NM_001145827.1. [Q7TNL3-2]
DR RefSeq; NP_083076.3; NM_028800.3. [Q7TNL3-1]
DR RefSeq; XP_006503504.1; XM_006503441.3. [Q7TNL3-2]
DR RefSeq; XP_006503505.1; XM_006503442.1. [Q7TNL3-1]
DR RefSeq; XP_017175903.1; XM_017320414.1. [Q7TNL3-1]
DR AlphaFoldDB; Q7TNL3; -.
DR SMR; Q7TNL3; -.
DR DIP; DIP-58526N; -.
DR IntAct; Q7TNL3; 1.
DR STRING; 10090.ENSMUSP00000092354; -.
DR iPTMnet; Q7TNL3; -.
DR PhosphoSitePlus; Q7TNL3; -.
DR EPD; Q7TNL3; -.
DR PaxDb; Q7TNL3; -.
DR PRIDE; Q7TNL3; -.
DR ProteomicsDB; 257454; -. [Q7TNL3-1]
DR ProteomicsDB; 257455; -. [Q7TNL3-2]
DR Antibodypedia; 2156; 168 antibodies from 29 providers.
DR DNASU; 74178; -.
DR Ensembl; ENSMUST00000094761; ENSMUSP00000092354; ENSMUSG00000042608. [Q7TNL3-1]
DR Ensembl; ENSMUST00000116286; ENSMUSP00000111990; ENSMUSG00000042608. [Q7TNL3-2]
DR GeneID; 74178; -.
DR KEGG; mmu:74178; -.
DR UCSC; uc008usl.2; mouse. [Q7TNL3-1]
DR UCSC; uc008usm.2; mouse. [Q7TNL3-2]
DR CTD; 83931; -.
DR MGI; MGI:1921428; Stk40.
DR VEuPathDB; HostDB:ENSMUSG00000042608; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00950000182986; -.
DR HOGENOM; CLU_035107_0_0_1; -.
DR InParanoid; Q7TNL3; -.
DR OMA; GRDAQPM; -.
DR OrthoDB; 1362510at2759; -.
DR PhylomeDB; Q7TNL3; -.
DR TreeFam; TF329785; -.
DR BioGRID-ORCS; 74178; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Stk40; mouse.
DR PRO; PR:Q7TNL3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TNL3; protein.
DR Bgee; ENSMUSG00000042608; Expressed in ileal epithelium and 224 other tissues.
DR ExpressionAtlas; Q7TNL3; baseline and differential.
DR Genevisible; Q7TNL3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0005977; P:glycogen metabolic process; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..435
FT /note="Serine/threonine-protein kinase 40"
FT /id="PRO_0000252262"
FT DOMAIN 35..332
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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"
FT VAR_SEQ 1
FT /note="M -> MKPYLRGASTQELRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020901"
FT CONFLICT 196
FT /note="R -> L (in Ref. 3; BAB26110)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="I -> V (in Ref. 3; BAB26110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48932 MW; 5AA58BA842CE2ACF CRC64;
MKRRASDRGA GETSANAKAL GTGIAGNNAK RAGPFVLGPR LGNSPVPSIV QCLARKDGTD
DFYQLKILTL EERGEQGIES QEERQGKMLL HTEYSLLSLL HTQDGVVHHH GLFQDRTCEA
VEDTESGRMV KKMKKRICLV LDCLCAHDFS DKTADLINLQ HYVIKEKRLS ERETVVIFYD
VVRVVEALHQ KNIVHRDLKL GNMVLNKRTH RITITNFCLG KHLVSEGDLL KDQRGSPAYI
SPDVLSGRPY RGKPSDMWAL GVVLFTMLYG QFPFYDSIPQ ELFRKIKAAE YTIPEDGRVS
ENTVCLIRKL LVLDPQQRLA AADVLEALSA IIASWQSLSS LSGPLQVVPD IDDQMSSSDS
SQEAKVTEEC SQYEFENYMR QQLLLAEEKS SIHEARAWVP KRQFGSMPPV RRLGHDAQPM
TSLDTAILAQ RYLRK
