STK16_HUMAN
ID STK16_HUMAN Reviewed; 305 AA.
AC O75716; A8K9H9; Q5U0F8; Q96KI2; Q9BUH4; Q9UEN3; Q9UP78;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Serine/threonine-protein kinase 16;
DE EC=2.7.11.1;
DE AltName: Full=Myristoylated and palmitoylated serine/threonine-protein kinase;
DE Short=MPSK;
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;
DE AltName: Full=hPSK;
GN Name=STK16; Synonyms=MPSK1, PKL12, TSF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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, FUNCTION,
RP AUTOPHOSPHORYLATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-6 AND
RP CYS-8, AND MUTAGENESIS OF GLY-2; CYS-6 AND CYS-8.
RC TISSUE=Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Wabakken T.K., Aasheim H.-C.;
RT "Characterization of a ubiquitous expressed human serine/threonine
RT kinase.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Stairs D.B., Ha S.I., Chodosh L.A.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-266.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-266.
RC TISSUE=Colon, and Lymph;
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 13-304 OF WILD TYPE AND IN COMPLEX
RP WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1, PHOSPHORYLATION AT
RP THR-185; SER-197 AND TYR-198, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18184589; DOI=10.1016/j.str.2007.10.026;
RA Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E., Sobott F.,
RA Parker S.A., Najmanovich R., Turk B.E., Knapp S.;
RT "Structure of the human protein kinase MPSK1 reveals an atypical activation
RT loop architecture.";
RL Structure 16:115-124(2008).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-41; LYS-55; VAL-77; TRP-266 AND
RP LEU-277.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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. May be involved in secretory
CC vesicle trafficking or intracellular signaling. May have a role in
CC regulating stromal-epithelial interactions that occur during ductal
CC 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:0000269|PubMed:10364453}.
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:0000269|PubMed:18184589}.
CC -!- INTERACTION:
CC O75716; Q6UY14: ADAMTSL4; NbExp=3; IntAct=EBI-749295, EBI-742002;
CC O75716; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-749295, EBI-10173507;
CC O75716; O95994: AGR2; NbExp=3; IntAct=EBI-749295, EBI-712648;
CC O75716; A0A087WVE9: ARNT2; NbExp=3; IntAct=EBI-749295, EBI-12808086;
CC O75716; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-749295, EBI-12811889;
CC O75716; Q7RTU4: BHLHA9; NbExp=3; IntAct=EBI-749295, EBI-17508719;
CC O75716; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-749295, EBI-739580;
CC O75716; Q13185: CBX3; NbExp=3; IntAct=EBI-749295, EBI-78176;
CC O75716; P27918: CFP; NbExp=3; IntAct=EBI-749295, EBI-9038570;
CC O75716; O43186: CRX; NbExp=3; IntAct=EBI-749295, EBI-748171;
CC O75716; A8MUP2: CSKMT; NbExp=3; IntAct=EBI-749295, EBI-12842046;
CC O75716; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-749295, EBI-3867333;
CC O75716; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-749295, EBI-742054;
CC O75716; Q96EY1-2: DNAJA3; NbExp=3; IntAct=EBI-749295, EBI-3952284;
CC O75716; Q9Y295: DRG1; NbExp=3; IntAct=EBI-749295, EBI-719554;
CC O75716; O95967: EFEMP2; NbExp=6; IntAct=EBI-749295, EBI-743414;
CC O75716; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-749295, EBI-2349927;
CC O75716; Q96Q35: FLACC1; NbExp=3; IntAct=EBI-749295, EBI-750451;
CC O75716; O43559: FRS3; NbExp=3; IntAct=EBI-749295, EBI-725515;
CC O75716; P51114-2: FXR1; NbExp=3; IntAct=EBI-749295, EBI-11022345;
CC O75716; Q06546: GABPA; NbExp=3; IntAct=EBI-749295, EBI-638925;
CC O75716; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-749295, EBI-747204;
CC O75716; Q0VD86: INCA1; NbExp=6; IntAct=EBI-749295, EBI-6509505;
CC O75716; Q9BQ13: KCTD14; NbExp=4; IntAct=EBI-749295, EBI-10189448;
CC O75716; Q9BQ13-2: KCTD14; NbExp=3; IntAct=EBI-749295, EBI-12278688;
CC O75716; Q8N5Z5: KCTD17; NbExp=9; IntAct=EBI-749295, EBI-743960;
CC O75716; Q8N5Z5-2: KCTD17; NbExp=3; IntAct=EBI-749295, EBI-10189368;
CC O75716; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-749295, EBI-10693436;
CC O75716; Q5T749: KPRP; NbExp=3; IntAct=EBI-749295, EBI-10981970;
CC O75716; Q15323: KRT31; NbExp=3; IntAct=EBI-749295, EBI-948001;
CC O75716; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-749295, EBI-11959885;
CC O75716; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-749295, EBI-11749135;
CC O75716; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-749295, EBI-10172150;
CC O75716; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-749295, EBI-10172290;
CC O75716; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-749295, EBI-10171774;
CC O75716; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-749295, EBI-10172052;
CC O75716; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-749295, EBI-1052037;
CC O75716; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-749295, EBI-11953846;
CC O75716; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-749295, EBI-3957672;
CC O75716; P50222: MEOX2; NbExp=3; IntAct=EBI-749295, EBI-748397;
CC O75716; Q7Z3K6-2: MIER3; NbExp=3; IntAct=EBI-749295, EBI-12224671;
CC O75716; Q5JXC2: MIIP; NbExp=4; IntAct=EBI-749295, EBI-2801965;
CC O75716; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-749295, EBI-742948;
CC O75716; Q93015-2: NAA80; NbExp=5; IntAct=EBI-749295, EBI-12126220;
CC O75716; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-749295, EBI-740897;
CC O75716; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-749295, EBI-945833;
CC O75716; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-749295, EBI-22310682;
CC O75716; Q92824: PCSK5; NbExp=3; IntAct=EBI-749295, EBI-751290;
CC O75716; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-749295, EBI-2692890;
CC O75716; O15496: PLA2G10; NbExp=3; IntAct=EBI-749295, EBI-726466;
CC O75716; O15162: PLSCR1; NbExp=3; IntAct=EBI-749295, EBI-740019;
CC O75716; Q9NRY6: PLSCR3; NbExp=6; IntAct=EBI-749295, EBI-750734;
CC O75716; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-749295, EBI-11320284;
CC O75716; P31321: PRKAR1B; NbExp=3; IntAct=EBI-749295, EBI-2805516;
CC O75716; Q03431: PTH1R; NbExp=3; IntAct=EBI-749295, EBI-2860297;
CC O75716; Q04864: REL; NbExp=3; IntAct=EBI-749295, EBI-307352;
CC O75716; Q04864-2: REL; NbExp=3; IntAct=EBI-749295, EBI-10829018;
CC O75716; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-749295, EBI-746118;
CC O75716; P49247: RPIA; NbExp=4; IntAct=EBI-749295, EBI-744831;
CC O75716; Q2I0M5: RSPO4; NbExp=3; IntAct=EBI-749295, EBI-12821217;
CC O75716; Q8IYX7: SAXO1; NbExp=6; IntAct=EBI-749295, EBI-3957636;
CC O75716; P12757: SKIL; NbExp=3; IntAct=EBI-749295, EBI-2902468;
CC O75716; O14508: SOCS2; NbExp=3; IntAct=EBI-749295, EBI-617737;
CC O75716; O43597: SPRY2; NbExp=3; IntAct=EBI-749295, EBI-742487;
CC O75716; Q99081: TCF12; NbExp=3; IntAct=EBI-749295, EBI-722877;
CC O75716; P15884: TCF4; NbExp=3; IntAct=EBI-749295, EBI-533224;
CC O75716; Q08117: TLE5; NbExp=3; IntAct=EBI-749295, EBI-717810;
CC O75716; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-749295, EBI-2505861;
CC O75716; O43734: TRAF3IP2; NbExp=3; IntAct=EBI-749295, EBI-744798;
CC O75716; P14373: TRIM27; NbExp=3; IntAct=EBI-749295, EBI-719493;
CC O75716; Q8IWZ5: TRIM42; NbExp=6; IntAct=EBI-749295, EBI-5235829;
CC O75716; Q15654: TRIP6; NbExp=3; IntAct=EBI-749295, EBI-742327;
CC O75716; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-749295, EBI-11975223;
CC O75716; Q9Y3S2: ZNF330; NbExp=6; IntAct=EBI-749295, EBI-373456;
CC O75716; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-749295, EBI-10252492;
CC O75716; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-749295, EBI-10251462;
CC O75716; P32233: Drg1; Xeno; NbExp=4; IntAct=EBI-749295, EBI-8429215;
CC O75716; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-749295, EBI-6480811;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi
CC and Golgi-derived vesicles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels.
CC {ECO:0000269|PubMed:10364453}.
CC -!- PTM: Mainly autophosphorylated on serine/threonine residues. Also
CC autophosphorylated on Tyr-198. {ECO:0000269|PubMed:18184589}.
CC -!- PTM: It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8.
CC {ECO:0000269|PubMed:10364453}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV38392.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA06700.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ005791; CAA06700.1; ALT_FRAME; mRNA.
DR EMBL; AF060798; AAC28337.1; -; mRNA.
DR EMBL; AB020739; BAB16311.1; -; mRNA.
DR EMBL; AJ010872; CAA09387.1; -; mRNA.
DR EMBL; AF203910; AAG23728.1; -; mRNA.
DR EMBL; BT019585; AAV38392.1; ALT_FRAME; mRNA.
DR EMBL; AK292694; BAF85383.1; -; mRNA.
DR EMBL; CR407675; CAG28603.1; -; mRNA.
DR EMBL; BC002618; AAH02618.1; -; mRNA.
DR EMBL; BC053998; AAH53998.1; -; mRNA.
DR CCDS; CCDS42822.1; -.
DR RefSeq; NP_001008910.1; NM_001008910.3.
DR RefSeq; NP_001317142.1; NM_001330213.1.
DR PDB; 2BUJ; X-ray; 2.60 A; A/B=13-305.
DR PDBsum; 2BUJ; -.
DR AlphaFoldDB; O75716; -.
DR SMR; O75716; -.
DR BioGRID; 114144; 158.
DR DIP; DIP-29598N; -.
DR IntAct; O75716; 99.
DR MINT; O75716; -.
DR STRING; 9606.ENSP00000386928; -.
DR BindingDB; O75716; -.
DR ChEMBL; CHEMBL3938; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O75716; -.
DR GuidetoPHARMACOLOGY; 2213; -.
DR GlyGen; O75716; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75716; -.
DR PhosphoSitePlus; O75716; -.
DR SwissPalm; O75716; -.
DR BioMuta; STK16; -.
DR EPD; O75716; -.
DR jPOST; O75716; -.
DR MassIVE; O75716; -.
DR PaxDb; O75716; -.
DR PeptideAtlas; O75716; -.
DR PRIDE; O75716; -.
DR ProteomicsDB; 50174; -.
DR Antibodypedia; 34316; 285 antibodies from 26 providers.
DR DNASU; 8576; -.
DR Ensembl; ENST00000396738.7; ENSP00000379964.2; ENSG00000115661.14.
DR Ensembl; ENST00000409638.7; ENSP00000386928.3; ENSG00000115661.14.
DR GeneID; 8576; -.
DR KEGG; hsa:8576; -.
DR MANE-Select; ENST00000396738.7; ENSP00000379964.2; NM_001330213.2; NP_001317142.1.
DR UCSC; uc002vko.3; human.
DR CTD; 8576; -.
DR DisGeNET; 8576; -.
DR GeneCards; STK16; -.
DR HGNC; HGNC:11394; STK16.
DR HPA; ENSG00000115661; Low tissue specificity.
DR MIM; 604719; gene.
DR neXtProt; NX_O75716; -.
DR OpenTargets; ENSG00000115661; -.
DR PharmGKB; PA36202; -.
DR VEuPathDB; HostDB:ENSG00000115661; -.
DR eggNOG; KOG2345; Eukaryota.
DR GeneTree; ENSGT00550000075037; -.
DR InParanoid; O75716; -.
DR OMA; MHQYKVK; -.
DR OrthoDB; 831026at2759; -.
DR PhylomeDB; O75716; -.
DR TreeFam; TF350433; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; O75716; -.
DR SignaLink; O75716; -.
DR SIGNOR; O75716; -.
DR BioGRID-ORCS; 8576; 12 hits in 1112 CRISPR screens.
DR ChiTaRS; STK16; human.
DR EvolutionaryTrace; O75716; -.
DR GeneWiki; STK16; -.
DR GenomeRNAi; 8576; -.
DR Pharos; O75716; Tchem.
DR PRO; PR:O75716; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75716; protein.
DR Bgee; ENSG00000115661; Expressed in mucosa of transverse colon and 115 other tissues.
DR ExpressionAtlas; O75716; baseline and differential.
DR Genevisible; O75716; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; 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 3D-structure; ATP-binding; Cytoplasm; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..305
FT /note="Serine/threonine-protein kinase 16"
FT /id="PRO_0000086701"
FT DOMAIN 20..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 166..202
FT /note="Activation loop"
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 185
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18184589"
FT MOD_RES 197
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18184589"
FT MOD_RES 198
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18184589"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10364453"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10364453"
FT LIPID 8
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10364453"
FT VARIANT 41
FT /note="H -> R (in dbSNP:rs34799131)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041140"
FT VARIANT 55
FT /note="E -> K (in dbSNP:rs35947471)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041141"
FT VARIANT 77
FT /note="I -> V (in dbSNP:rs34282267)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041142"
FT VARIANT 266
FT /note="R -> W (in dbSNP:rs17849638)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.8"
FT /id="VAR_041143"
FT VARIANT 277
FT /note="P -> L (in dbSNP:rs35454203)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041144"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:10364453"
FT MUTAGEN 6
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:10364453"
FT MUTAGEN 8
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:10364453"
FT CONFLICT 59
FT /note="R -> L (in Ref. 6; AAV38392)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> P (in Ref. 7; BAF85383)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="D -> G (in Ref. 1; CAA06700 and 4; CAA09387)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> F (in Ref. 2; AAC28337)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="G -> S (in Ref. 4; CAA09387)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:2BUJ"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:2BUJ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2BUJ"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2BUJ"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:2BUJ"
SQ SEQUENCE 305 AA; 34656 MW; 593B2AEB8505009C CRC64;
MGHALCVCSR GTVIIDNKRY LFIQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDRE
EAQREADMHR LFNHPNILRL VAYCLRERGA KHEAWLLLPF FKRGTLWNEI ERLKDKGNFL
TEDQILWLLL GICRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIHVEGS
RQALTLQDWA AQRCTISYRA PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ
KGDSVALAVQ NQLSIPQSPR HSSALRQLLN SMMTVDPHQR PHIPLLLSQL EALQPPAPGQ
HTTQI
