STK16_MOUSE
ID STK16_MOUSE Reviewed; 305 AA.
AC O88697; Q3UEG5; Q9JMJ0; Q9JMJ1; Q9QX00;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein kinase 16;
DE EC=2.7.11.1;
DE AltName: Full=Embryo-derived protein kinase;
DE Short=Edpk;
DE AltName: Full=Myristoylated and palmitoylated serine/threonine-protein kinase;
DE Short=MPSK;
DE AltName: Full=Protein kinase Krct;
DE AltName: Full=Protein kinase PKL12;
DE AltName: Full=TGF-beta-stimulated factor 1;
DE Short=TSF-1;
DE AltName: Full=Tyrosine-protein kinase STK16;
DE EC=2.7.10.2;
GN Name=Stk16; Synonyms=Edpk, Krct, Mpsk1, Pkl12, Tsf1;
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], SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=9712705; DOI=10.1006/bbrc.1998.9163;
RA Ligos J.M., Gerwin N., Fernandez P., Gutierrez-Ramos J.-C., Bernad A.;
RT "Cloning, expression analysis, and functional characterization of PKL12, a
RT member of a new subfamily of ser/thr kinases.";
RL Biochem. Biophys. Res. Commun. 249:380-384(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=9878782; DOI=10.1016/s0167-4781(98)00224-3;
RA Kurioka K., Nakagawa K., Denda K., Miyazawa K., Kitamura N.;
RT "Molecular cloning and characterization of a novel protein serine/threonine
RT kinase highly expressed in mouse embryo.";
RL Biochim. Biophys. Acta 1443:275-284(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/NJ; TISSUE=Mammary gland;
RX PubMed=9817935; DOI=10.1093/hmg/7.13.2157;
RA Stairs D.B., Perry Gardner H., Ha S.I., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Chodosh L.A.;
RT "Cloning and characterization of Krct, a member of a novel subfamily of
RT serine/threonine kinases.";
RL Hum. Mol. Genet. 7:2157-2166(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10364453; DOI=10.1006/bbrc.1999.0811;
RA Berson A.E., Young C., Morrison S.L., Fujii G.H., Sheung J., Wu B.,
RA Bolen J.B., Burkhardt A.L.;
RT "Identification and characterization of a myristylated and palmitylated
RT serine/threonine protein kinase.";
RL Biochem. Biophys. Res. Commun. 259:533-538(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=10947953; DOI=10.1042/bj3500395;
RA Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.;
RT "A novel transcriptional factor with Ser/Thr kinase activity involved in
RT the transforming growth factor (TGF)-beta signalling pathway.";
RL Biochem. J. 350:395-404(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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: Membrane-associated protein kinase that phosphorylates on
CC serine and threonine residues. In vitro substrates include DRG1, ENO1
CC and EIF4EBP1. Also autophosphorylates (By similarity). May be involved
CC in secretory vesicle trafficking or intracellular signaling. May have a
CC role in regulating stromal-epithelial interactions that occur during
CC ductal morphogenesis in the mammary gland. May be involved in TGF-beta
CC signaling. Able to autophosphorylate on Tyr residue; it is however
CC unclear whether it has tyrosine-protein kinase toward other proteins.
CC {ECO:0000250, ECO:0000269|PubMed:9878782}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Monomer. Interacts with DRG1 (via its N-terminal); the
CC interaction phosphorylates DRG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:9712705}. Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels. Relatively
CC higher levels in testis, kidney and liver. {ECO:0000269|PubMed:9712705,
CC ECO:0000269|PubMed:9878782}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of developing embryo.
CC {ECO:0000269|PubMed:9712705}.
CC -!- PTM: Mainly autophosphorylated on serine/threonine residues. Also
CC autophosphorylated on Tyr-198 (By similarity). {ECO:0000250}.
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; AJ005790; CAA06699.1; -; mRNA.
DR EMBL; AB017197; BAA74457.1; -; mRNA.
DR EMBL; AF089869; AAC98502.1; -; mRNA.
DR EMBL; AF062076; AAD02811.1; -; mRNA.
DR EMBL; AB022285; BAA89662.1; -; Genomic_DNA.
DR EMBL; AB022179; BAA89499.1; -; mRNA.
DR EMBL; AK149539; BAE28946.1; -; mRNA.
DR EMBL; CH466548; EDL00383.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00384.1; -; Genomic_DNA.
DR EMBL; CH466548; EDL00386.1; -; Genomic_DNA.
DR EMBL; BC028999; AAH28999.1; -; mRNA.
DR CCDS; CCDS15067.1; -.
DR RefSeq; NP_001264921.1; NM_001277992.1.
DR RefSeq; NP_035624.3; NM_011494.5.
DR RefSeq; XP_006496524.1; XM_006496461.1.
DR AlphaFoldDB; O88697; -.
DR SMR; O88697; -.
DR BioGRID; 203544; 3.
DR STRING; 10090.ENSMUSP00000027401; -.
DR PhosphoSitePlus; O88697; -.
DR SwissPalm; O88697; -.
DR EPD; O88697; -.
DR MaxQB; O88697; -.
DR PaxDb; O88697; -.
DR PeptideAtlas; O88697; -.
DR PRIDE; O88697; -.
DR ProteomicsDB; 257092; -.
DR Antibodypedia; 34316; 285 antibodies from 26 providers.
DR DNASU; 20872; -.
DR Ensembl; ENSMUST00000027401; ENSMUSP00000027401; ENSMUSG00000026201.
DR GeneID; 20872; -.
DR KEGG; mmu:20872; -.
DR UCSC; uc007boh.2; mouse.
DR CTD; 8576; -.
DR MGI; MGI:1313271; Stk16.
DR VEuPathDB; HostDB:ENSMUSG00000026201; -.
DR eggNOG; KOG2345; Eukaryota.
DR GeneTree; ENSGT00550000075037; -.
DR InParanoid; O88697; -.
DR OMA; MHQYKVK; -.
DR OrthoDB; 831026at2759; -.
DR PhylomeDB; O88697; -.
DR TreeFam; TF350433; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 20872; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Stk16; mouse.
DR PRO; PR:O88697; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88697; protein.
DR Bgee; ENSMUSG00000026201; Expressed in right kidney and 270 other tissues.
DR ExpressionAtlas; O88697; baseline and differential.
DR Genevisible; O88697; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:GO_Central.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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 ATP-binding; Cytoplasm; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT CHAIN 2..305
FT /note="Serine/threonine-protein kinase 16"
FT /id="PRO_0000086702"
FT DOMAIN 20..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 166..202
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 197
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT MOD_RES 198
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75716"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 8
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 25..28
FT /note="KLGE -> EIGG (in Ref. 5; BAA89662 and 6; BAA89499)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="T -> A (in Ref. 6; BAA89499)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..268
FT /note="QL -> HV (in Ref. 4; AAD02811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34382 MW; EB4725D26B210537 CRC64;
MGHALCVCSR GTVIIDNKRY LFVQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDQE
EAQREAEMHR LFQHPNILRL MAYSLKERGA KHEAWLLLPF FKKGTLWNEI ERLKDQGSFL
TEDQILPLLL GISRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIQVEGS
RQALALQDWA AQRCTISYRA PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ
KGDSVALAVQ NELSIPQSPR HSSALRQLLS SMMTVDPQQR PHIPVLLSQL EALQPPAPGQ
HTTQI
