ID ST32B_MOUSE Reviewed; 414 AA.
AC Q9JJX8; Q7TMD3; Q8C4E0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase 32B;
DE EC=2.7.11.1;
GN Name=Stk32b {ECO:0000312|MGI:MGI:1927552};
GN Synonyms=Stk32 {ECO:0000312|MGI:MGI:1927552};
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] {ECO:0000312|EMBL:CAB76566.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:CAB76566.1};
RX PubMed=10700184; DOI=10.1038/73508;
RA Ruiz-Perez V.L., Ide S.E., Strom T.M., Lorenz B., Wilson D., Woods K.,
RA King L., Francomano C., Freisinger P., Spranger S., Marino B.,
RA Dallapiccola B., Wright M., Meitinger T., Polymeropoulos M.H., Goodship J.;
RT "Mutations in a new gene in Ellis-van Creveld syndrome and Weyers
RT acrodental dysostosis.";
RL Nat. Genet. 24:283-286(2000).
RN [2] {ECO:0000312|EMBL:BAC38500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC38500.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC38500.1};
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 [3] {ECO:0000312|EMBL:AAH52404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52404.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH56396.1}, and
RC Fetal brain {ECO:0000312|EMBL:AAH52404.1};
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 -!- 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:0000250|UniProtKB:Q60592};
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:0000250|UniProtKB:Q60592};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ250840; CAB76566.1; -; mRNA.
DR EMBL; AK082468; BAC38500.1; -; mRNA.
DR EMBL; BC052404; AAH52404.1; -; mRNA.
DR EMBL; BC056396; AAH56396.1; -; mRNA.
DR EMBL; BC058412; AAH58412.1; -; mRNA.
DR CCDS; CCDS39076.1; -.
DR RefSeq; NP_071861.1; NM_022416.2.
DR AlphaFoldDB; Q9JJX8; -.
DR SMR; Q9JJX8; -.
DR STRING; 10090.ENSMUSP00000092432; -.
DR iPTMnet; Q9JJX8; -.
DR PhosphoSitePlus; Q9JJX8; -.
DR PaxDb; 10090-ENSMUSP00000092432; -.
DR ProteomicsDB; 254570; -.
DR Antibodypedia; 9281; 138 antibodies from 23 providers.
DR DNASU; 64293; -.
DR Ensembl; ENSMUST00000094836.6; ENSMUSP00000092432.5; ENSMUSG00000029123.9.
DR GeneID; 64293; -.
DR KEGG; mmu:64293; -.
DR UCSC; uc008xft.2; mouse.
DR AGR; MGI:1927552; -.
DR CTD; 55351; -.
DR MGI; MGI:1927552; Stk32b.
DR VEuPathDB; HostDB:ENSMUSG00000029123; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000160490; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q9JJX8; -.
DR OMA; QKCVERD; -.
DR OrthoDB; 2871850at2759; -.
DR PhylomeDB; Q9JJX8; -.
DR TreeFam; TF313395; -.
DR BioGRID-ORCS; 64293; 3 hits in 79 CRISPR screens.
DR ChiTaRS; Stk32b; mouse.
DR PRO; PR:Q9JJX8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JJX8; Protein.
DR Bgee; ENSMUSG00000029123; Expressed in cortical plate and 87 other cell types or tissues.
DR Genevisible; Q9JJX8; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05578; STKc_Yank1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24355:SF30; SERINE_THREONINE KINASE 32A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..414
FT /note="Serine/threonine-protein kinase 32B"
FT /id="PRO_0000232414"
FT DOMAIN 23..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 374..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 180
FT /note="M -> V (in Ref. 2; BAC38500)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="N -> D (in Ref. 1; CAB76566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 47916 MW; 3C394415790594F3 CRC64;
MGGNHSHKPP VFDENEEVNF DHFQILRAIG KGSFGKVCIV QKRDTKKMYA MKYMNKQKCV
ERDEVRNVFR ELQIMQGLEH PFLVNLWYSF QDEEDMFMVV DLLLGGDLRY HLQQNVHFTE
GTVKLYICEL ALALEYLQRY HIIHRDIKPD NILLDEHGHV HITDFNIATV LKGSEKASSM
AGTKPYMAPE VFQVYVDGGP GYSYPVDWWS LGVTAYELLR GWRPYEIHSA TPIDEILNMF
KVERVHYSST WCEGMVSLLK KLLTKDPESR LSSLRDIQSM TYLADMNWDA VFEKALMPGF
VPNKGRLNCD PTFELEEMIL ESKPLHKKKK RLAKHRSRDS TKDSCPLNGH LQQCLETVRK
EFIIFNREKL RRQQGHNGQL SDLDGRIGSQ TSSKLQDGRN NNILTHTCPR GCSS
//
