ST17B_MOUSE
ID ST17B_MOUSE Reviewed; 372 AA.
AC Q8BG48; Q3TNG7; Q8BLV9; Q923E7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase 17B;
DE EC=2.7.11.1;
DE AltName: Full=DAP kinase-related apoptosis-inducing protein kinase 2;
GN Name=Stk17b; Synonyms=Drak2;
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 {ECO:0000312|EMBL:AAM18182.1};
RN [1] {ECO:0000312|EMBL:AAM18182.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM18182.1};
RA Walsh C.M., Wen B., Bain G., Kee B., Katayama C., Murre C., Hedrick S.M.;
RT "mDRAK2, a lymphoid-enriched apoptotic nuclear kinase, is activated during
RT thymocyte selection.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Bone marrow, Spleen, Testis, Thymus, Urinary bladder, and
RC Vein;
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:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a positive regulator of apoptosis. Phosphorylates
CC myosin light chains (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 Evidence={ECO:0000250|UniProtKB:Q9UEE5};
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:Q9UEE5};
CC -!- SUBUNIT: Interacts with CHP1; the interaction induces CHP1 to
CC translocate from the Golgi to the nucleus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250}. Note=Colocalizes with STK17B at the plasma membrane.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9UEE5}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. DAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AY092028; AAM18182.1; -; mRNA.
DR EMBL; AK035693; BAC29154.1; -; mRNA.
DR EMBL; AK041139; BAC30835.1; -; mRNA.
DR EMBL; AK076932; BAC36531.1; -; mRNA.
DR EMBL; AK083332; BAC38870.1; -; mRNA.
DR EMBL; AK153108; BAE31726.1; -; mRNA.
DR EMBL; AK165291; BAE38122.1; -; mRNA.
DR EMBL; BC006579; AAH06579.1; -; mRNA.
DR CCDS; CCDS14955.1; -.
DR RefSeq; NP_598571.2; NM_133810.3.
DR AlphaFoldDB; Q8BG48; -.
DR SMR; Q8BG48; -.
DR BioGRID; 221027; 2.
DR IntAct; Q8BG48; 1.
DR MINT; Q8BG48; -.
DR STRING; 10090.ENSMUSP00000027263; -.
DR iPTMnet; Q8BG48; -.
DR PhosphoSitePlus; Q8BG48; -.
DR EPD; Q8BG48; -.
DR MaxQB; Q8BG48; -.
DR PaxDb; Q8BG48; -.
DR PeptideAtlas; Q8BG48; -.
DR PRIDE; Q8BG48; -.
DR ProteomicsDB; 258629; -.
DR Antibodypedia; 19872; 436 antibodies from 44 providers.
DR DNASU; 98267; -.
DR Ensembl; ENSMUST00000027263; ENSMUSP00000027263; ENSMUSG00000026094.
DR GeneID; 98267; -.
DR KEGG; mmu:98267; -.
DR UCSC; uc007azj.2; mouse.
DR CTD; 9262; -.
DR MGI; MGI:2138162; Stk17b.
DR VEuPathDB; HostDB:ENSMUSG00000026094; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000154014; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q8BG48; -.
DR OMA; FYMLESK; -.
DR OrthoDB; 1156450at2759; -.
DR PhylomeDB; Q8BG48; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 98267; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Stk17b; mouse.
DR PRO; PR:Q8BG48; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BG48; protein.
DR Bgee; ENSMUSG00000026094; Expressed in peripheral lymph node and 233 other tissues.
DR ExpressionAtlas; Q8BG48; baseline and differential.
DR Genevisible; Q8BG48; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd14198; STKc_DRAK2; 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 InterPro; IPR042763; ST17B_STKc.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..372
FT /note="Serine/threonine-protein kinase 17B"
FT /id="PRO_0000086707"
FT DOMAIN 33..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 305..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 23
FT /note="I -> M (in Ref. 3; AAH06579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41983 MW; C858E175196E7A32 CRC64;
MSRRRFDCRS VSGLLTTTPQ TPIKTENFNN FYTLTPKELG RGKFAVVRQC ISKSTGQEYA
AKSLKKRRRG QDCRAEILHE IAVLELARSC PHVINLHEVY ENATEIILVL EYAAGGEIFN
LCLPELAEMV SENDVIRLIK QILEGVHYLH QNNIVHLDLK PQNILLSSIY PLGDIKIVDF
GMSRKIGNAS ELREIMGTPE YLAPEILNYD PITTATDMWN IGIIAYMLLT HTSPFVGEDN
QETYLNISQV NVDYSEEMFS SVSQLATDFI QSLLVKNPEK RPTAESCLSH SWLQQWDFGS
LFHPEETSGS SQIQDLTLRS SEEKTSKSSC NGSCGAREDK ENIPEDGSLV SKRFRFDDSL
PSPHELVPDL FC
