Full text data of STK16
STK16
(MPSK1, PKL12, TSF1)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein kinase 16; 2.7.11.1 (Myristoylated and palmitoylated serine/threonine-protein kinase; MPSK; Protein kinase PKL12; TGF-beta-stimulated factor 1; TSF-1; Tyrosine-protein kinase STK16; 2.7.10.2; hPSK)
Serine/threonine-protein kinase 16; 2.7.11.1 (Myristoylated and palmitoylated serine/threonine-protein kinase; MPSK; Protein kinase PKL12; TGF-beta-stimulated factor 1; TSF-1; Tyrosine-protein kinase STK16; 2.7.10.2; hPSK)
UniProt
O75716
ID STK16_HUMAN Reviewed; 305 AA.
AC O75716; A8K9H9; Q5U0F8; Q96KI2; Q9BUH4; Q9UEN3; Q9UP78;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT PKL12, a 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
RP AND 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
RT palmitylated serine/threonine protein kinase.";
RL Biochem. Biophys. Res. Commun. 259:533-538(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10947953; DOI=10.1042/0264-6021:3500395;
RA Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.;
RT "A novel transcriptional factor with Ser/Thr kinase activity involved
RT in 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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
RP COMPLEX WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1,
RP AUTOPHOSPHORYLATION AT THR-185; SER-197 AND TYR-198, AND MASS
RP 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.,
RA Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.;
RT "Structure of the human protein kinase MPSK1 reveals an atypical
RT activation 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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC on serine and threonine residues. In vitro substrates include
CC DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved
CC in secretory vesicle trafficking or intracellular signaling. May
CC have a role in regulating stromal-epithelial interactions that
CC occur during ductal morphogenesis in the mammary gland. May be
CC involved in TGF-beta signaling. Able to autophosphorylate on Tyr
CC residue; it is however unclear whether it has tyrosine-protein
CC kinase toward other proteins.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
CC -!- SUBUNIT: Monomer. Interacts with DRG1 (via its N-terminal); the
CC interaction phosphorylates DRG1.
CC -!- INTERACTION:
CC Q6UY14:ADAMTSL4; NbExp=3; IntAct=EBI-749295, EBI-742002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane;
CC Lipid-anchor (By similarity). Note=Associates with Golgi and
CC Golgi-derived vesicles (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels.
CC -!- PTM: Mainly autophosphorylated on serine/threonine residues. Also
CC autophosphorylated on Tyr-198.
CC -!- PTM: It is uncertain whether palmitoylation is on Cys-6 and/or
CC Cys-8.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV38392.1; Type=Frameshift; Positions=305;
CC Sequence=CAA06700.1; Type=Frameshift; Positions=305;
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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 RefSeq; NP_001008910.1; NM_001008910.2.
DR UniGene; Hs.153003; -.
DR PDB; 2BUJ; X-ray; 2.60 A; A/B=13-304.
DR PDBsum; 2BUJ; -.
DR ProteinModelPortal; O75716; -.
DR SMR; O75716; 13-299.
DR DIP; DIP-29598N; -.
DR IntAct; O75716; 5.
DR MINT; MINT-3001680; -.
DR STRING; 9606.ENSP00000379964; -.
DR BindingDB; O75716; -.
DR ChEMBL; CHEMBL3938; -.
DR GuidetoPHARMACOLOGY; 2213; -.
DR PhosphoSite; O75716; -.
DR PaxDb; O75716; -.
DR PRIDE; O75716; -.
DR DNASU; 8576; -.
DR Ensembl; ENST00000396738; ENSP00000379964; ENSG00000115661.
DR Ensembl; ENST00000409638; ENSP00000386928; ENSG00000115661.
DR GeneID; 8576; -.
DR KEGG; hsa:8576; -.
DR UCSC; uc002vko.2; human.
DR CTD; 8576; -.
DR GeneCards; GC02P220110; -.
DR HGNC; HGNC:11394; STK16.
DR HPA; HPA029450; -.
DR MIM; 604719; gene.
DR neXtProt; NX_O75716; -.
DR PharmGKB; PA36202; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG054359; -.
DR KO; K08856; -.
DR OrthoDB; EOG7Z3F55; -.
DR BRENDA; 2.7.11.1; 2681.
DR SignaLink; O75716; -.
DR ChiTaRS; STK16; human.
DR EvolutionaryTrace; O75716; -.
DR GeneWiki; STK16; -.
DR GenomeRNAi; 8576; -.
DR NextBio; 32169; -.
DR PRO; PR:O75716; -.
DR ArrayExpress; O75716; -.
DR Bgee; O75716; -.
DR CleanEx; HS_STK16; -.
DR Genevestigator; O75716; -.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
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; Complete proteome; Cytoplasm; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Polymorphism; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 305 Serine/threonine-protein kinase 16.
FT /FTId=PRO_0000086701.
FT DOMAIN 20 293 Protein kinase.
FT NP_BIND 26 34 ATP (By similarity).
FT REGION 166 202 Activation loop.
FT ACT_SITE 148 148 Proton acceptor (By similarity).
FT BINDING 49 49 ATP (By similarity).
FT MOD_RES 185 185 Phosphothreonine; by autocatalysis.
FT MOD_RES 197 197 Phosphoserine; by autocatalysis.
FT MOD_RES 198 198 Phosphotyrosine; by autocatalysis.
FT LIPID 2 2 N-myristoyl glycine.
FT LIPID 6 6 S-palmitoyl cysteine (Probable).
FT LIPID 8 8 S-palmitoyl cysteine (Probable).
FT VARIANT 41 41 H -> R (in dbSNP:rs34799131).
FT /FTId=VAR_041140.
FT VARIANT 55 55 E -> K (in dbSNP:rs35947471).
FT /FTId=VAR_041141.
FT VARIANT 77 77 I -> V (in dbSNP:rs34282267).
FT /FTId=VAR_041142.
FT VARIANT 266 266 R -> W (in dbSNP:rs17849638).
FT /FTId=VAR_041143.
FT VARIANT 277 277 P -> L (in dbSNP:rs35454203).
FT /FTId=VAR_041144.
FT MUTAGEN 2 2 G->A: Loss of myristoylation.
FT MUTAGEN 6 6 C->S: Loss of palmitoylation.
FT MUTAGEN 8 8 C->S: Loss of palmitoylation.
FT CONFLICT 59 59 R -> L (in Ref. 6; AAV38392).
FT CONFLICT 180 180 S -> P (in Ref. 7; BAF85383).
FT CONFLICT 213 213 D -> G (in Ref. 1; CAA06700 and 4;
FT CAA09387).
FT CONFLICT 221 221 L -> F (in Ref. 2; AAC28337).
FT CONFLICT 222 222 G -> S (in Ref. 4; CAA09387).
FT STRAND 13 15
FT STRAND 18 27
FT STRAND 32 39
FT TURN 40 42
FT STRAND 45 55
FT HELIX 56 70
FT STRAND 82 88
FT STRAND 91 99
FT HELIX 106 114
FT TURN 115 117
FT HELIX 122 141
FT HELIX 151 153
FT STRAND 154 156
FT STRAND 162 164
FT STRAND 171 173
FT STRAND 175 179
FT HELIX 180 193
FT HELIX 196 198
FT HELIX 201 203
FT STRAND 208 212
FT HELIX 215 230
FT HELIX 236 240
FT HELIX 245 250
FT HELIX 263 272
FT HELIX 277 279
FT HELIX 283 292
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
//
ID STK16_HUMAN Reviewed; 305 AA.
AC O75716; A8K9H9; Q5U0F8; Q96KI2; Q9BUH4; Q9UEN3; Q9UP78;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT PKL12, a 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
RP AND 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
RT palmitylated serine/threonine protein kinase.";
RL Biochem. Biophys. Res. Commun. 259:533-538(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10947953; DOI=10.1042/0264-6021:3500395;
RA Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.;
RT "A novel transcriptional factor with Ser/Thr kinase activity involved
RT in 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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
RP COMPLEX WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1,
RP AUTOPHOSPHORYLATION AT THR-185; SER-197 AND TYR-198, AND MASS
RP 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.,
RA Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.;
RT "Structure of the human protein kinase MPSK1 reveals an atypical
RT activation 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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC on serine and threonine residues. In vitro substrates include
CC DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved
CC in secretory vesicle trafficking or intracellular signaling. May
CC have a role in regulating stromal-epithelial interactions that
CC occur during ductal morphogenesis in the mammary gland. May be
CC involved in TGF-beta signaling. Able to autophosphorylate on Tyr
CC residue; it is however unclear whether it has tyrosine-protein
CC kinase toward other proteins.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
CC -!- SUBUNIT: Monomer. Interacts with DRG1 (via its N-terminal); the
CC interaction phosphorylates DRG1.
CC -!- INTERACTION:
CC Q6UY14:ADAMTSL4; NbExp=3; IntAct=EBI-749295, EBI-742002;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane;
CC Lipid-anchor (By similarity). Note=Associates with Golgi and
CC Golgi-derived vesicles (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels.
CC -!- PTM: Mainly autophosphorylated on serine/threonine residues. Also
CC autophosphorylated on Tyr-198.
CC -!- PTM: It is uncertain whether palmitoylation is on Cys-6 and/or
CC Cys-8.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV38392.1; Type=Frameshift; Positions=305;
CC Sequence=CAA06700.1; Type=Frameshift; Positions=305;
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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 RefSeq; NP_001008910.1; NM_001008910.2.
DR UniGene; Hs.153003; -.
DR PDB; 2BUJ; X-ray; 2.60 A; A/B=13-304.
DR PDBsum; 2BUJ; -.
DR ProteinModelPortal; O75716; -.
DR SMR; O75716; 13-299.
DR DIP; DIP-29598N; -.
DR IntAct; O75716; 5.
DR MINT; MINT-3001680; -.
DR STRING; 9606.ENSP00000379964; -.
DR BindingDB; O75716; -.
DR ChEMBL; CHEMBL3938; -.
DR GuidetoPHARMACOLOGY; 2213; -.
DR PhosphoSite; O75716; -.
DR PaxDb; O75716; -.
DR PRIDE; O75716; -.
DR DNASU; 8576; -.
DR Ensembl; ENST00000396738; ENSP00000379964; ENSG00000115661.
DR Ensembl; ENST00000409638; ENSP00000386928; ENSG00000115661.
DR GeneID; 8576; -.
DR KEGG; hsa:8576; -.
DR UCSC; uc002vko.2; human.
DR CTD; 8576; -.
DR GeneCards; GC02P220110; -.
DR HGNC; HGNC:11394; STK16.
DR HPA; HPA029450; -.
DR MIM; 604719; gene.
DR neXtProt; NX_O75716; -.
DR PharmGKB; PA36202; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG054359; -.
DR KO; K08856; -.
DR OrthoDB; EOG7Z3F55; -.
DR BRENDA; 2.7.11.1; 2681.
DR SignaLink; O75716; -.
DR ChiTaRS; STK16; human.
DR EvolutionaryTrace; O75716; -.
DR GeneWiki; STK16; -.
DR GenomeRNAi; 8576; -.
DR NextBio; 32169; -.
DR PRO; PR:O75716; -.
DR ArrayExpress; O75716; -.
DR Bgee; O75716; -.
DR CleanEx; HS_STK16; -.
DR Genevestigator; O75716; -.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
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; Complete proteome; Cytoplasm; Kinase;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Polymorphism; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 305 Serine/threonine-protein kinase 16.
FT /FTId=PRO_0000086701.
FT DOMAIN 20 293 Protein kinase.
FT NP_BIND 26 34 ATP (By similarity).
FT REGION 166 202 Activation loop.
FT ACT_SITE 148 148 Proton acceptor (By similarity).
FT BINDING 49 49 ATP (By similarity).
FT MOD_RES 185 185 Phosphothreonine; by autocatalysis.
FT MOD_RES 197 197 Phosphoserine; by autocatalysis.
FT MOD_RES 198 198 Phosphotyrosine; by autocatalysis.
FT LIPID 2 2 N-myristoyl glycine.
FT LIPID 6 6 S-palmitoyl cysteine (Probable).
FT LIPID 8 8 S-palmitoyl cysteine (Probable).
FT VARIANT 41 41 H -> R (in dbSNP:rs34799131).
FT /FTId=VAR_041140.
FT VARIANT 55 55 E -> K (in dbSNP:rs35947471).
FT /FTId=VAR_041141.
FT VARIANT 77 77 I -> V (in dbSNP:rs34282267).
FT /FTId=VAR_041142.
FT VARIANT 266 266 R -> W (in dbSNP:rs17849638).
FT /FTId=VAR_041143.
FT VARIANT 277 277 P -> L (in dbSNP:rs35454203).
FT /FTId=VAR_041144.
FT MUTAGEN 2 2 G->A: Loss of myristoylation.
FT MUTAGEN 6 6 C->S: Loss of palmitoylation.
FT MUTAGEN 8 8 C->S: Loss of palmitoylation.
FT CONFLICT 59 59 R -> L (in Ref. 6; AAV38392).
FT CONFLICT 180 180 S -> P (in Ref. 7; BAF85383).
FT CONFLICT 213 213 D -> G (in Ref. 1; CAA06700 and 4;
FT CAA09387).
FT CONFLICT 221 221 L -> F (in Ref. 2; AAC28337).
FT CONFLICT 222 222 G -> S (in Ref. 4; CAA09387).
FT STRAND 13 15
FT STRAND 18 27
FT STRAND 32 39
FT TURN 40 42
FT STRAND 45 55
FT HELIX 56 70
FT STRAND 82 88
FT STRAND 91 99
FT HELIX 106 114
FT TURN 115 117
FT HELIX 122 141
FT HELIX 151 153
FT STRAND 154 156
FT STRAND 162 164
FT STRAND 171 173
FT STRAND 175 179
FT HELIX 180 193
FT HELIX 196 198
FT HELIX 201 203
FT STRAND 208 212
FT HELIX 215 230
FT HELIX 236 240
FT HELIX 245 250
FT HELIX 263 272
FT HELIX 277 279
FT HELIX 283 292
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
//
MIM
604719
*RECORD*
*FIELD* NO
604719
*FIELD* TI
*604719 SERINE/THREONINE PROTEIN KINASE 16; STK16
;;PKL12, MOUSE, HOMOLOG OF;;
TRANSFORMING GROWTH FACTOR-BETA-STIMULATED FACTOR 1; TSF1;;
read moreTGFB-STIMULATED FACTOR 1
*FIELD* TX
Protein kinases are a large family of proteins that share a homologous
catalytic domain of 250 to 300 amino acids, which can be subdivided into
11 subdomains. By screening a mouse fetal liver cDNA library with
primers from the catalytic domain of other serine/threonine protein
kinases, Ligos et al. (1998) characterized a new member of the ser/thr
kinase family, which they termed Pkl12 (protein kinase expressed in day
12 fetal liver). By in vitro kinase assay using enolase as substrate,
they showed that Pkl12 can phosphorylate enolase and promote
autophosphorylation, with a ser/thr specificity. They also constructed
the human homolog, STK16, using several human ESTs with sequence
similarity to the Pkl12 gene. The STK16 gene encodes a 310-amino acid
protein that shares 94% identity with the mouse homolog. Because its
size is very close to the minimal size for a core catalytic domain, the
authors suggested that STK16 may constitute the catalytic subunit of a
multisubunit kinase. By Northern blot analysis, Ligos et al. (1998)
showed that both STK16 and Pkl12 are ubiquitously expressed at very low
levels. Expression of an STK16 fusion protein showed that STK16 is
localized with Golgi and Golgi-derived vesicles. Overexpression of STK16
leads to disorganization of the Golgi apparatus into vesicular
structures, suggesting that STK16 is involved in the secretory pathway.
By sequence walking in the EST database, followed by PCR of a fetal
kidney cDNA library, Ohta et al. (2000) obtained a cDNA encoding STK16,
which they termed TSF1. Western blot analysis of a rat pituitary cell
line showed an increase of Tsf1 level after Tgfb (190180) treatment. Gel
shift analysis indicated that Tsf1 is a sequence-specific DNA-binding
factor that binds to GC-rich elements in vascular endothelial growth
factor (VEGF; 192240) and type C natriuretic peptide (NPPC; 600296)
promoters, independent of its kinase activity and Smad3 (603109) or
Smad4 (600993). Tsf1 could not directly activate the Smad-dependent
promoter of plasminogen activator inhibitor-1 (PAI1; 173360) but could
enhance the transactivation function of Smad3 and Smad4.
*FIELD* RF
1. Ligos, J. M.; Gerwin, N.; Fernandez, P.; Gutierrez-Ramos, J. C.;
Bernad, A.: Cloning, expression analysis, and functional characterization
of PKL12, a member of a new subfamily of ser/thr kinases. Biochem.
Biophys. Res. Commun. 249: 380-384, 1998.
2. Ohta, S.; Takeuchi, M.; Deguchi, M.; Tsuji, T.; Gahara, Y.; Nagata,
K.: A novel transcriptional factor with Ser/Thr kinase activity involved
in the transforming growth factor (TGF)-beta signalling pathway. Biochem.
J. 350: 395-404, 2000.
*FIELD* CN
Paul J. Converse - updated: 2/16/2001
*FIELD* CD
Yen-Pei C. Chang: 3/23/2000
*FIELD* ED
mgross: 02/21/2001
terry: 2/16/2001
carol: 3/23/2000
*RECORD*
*FIELD* NO
604719
*FIELD* TI
*604719 SERINE/THREONINE PROTEIN KINASE 16; STK16
;;PKL12, MOUSE, HOMOLOG OF;;
TRANSFORMING GROWTH FACTOR-BETA-STIMULATED FACTOR 1; TSF1;;
read moreTGFB-STIMULATED FACTOR 1
*FIELD* TX
Protein kinases are a large family of proteins that share a homologous
catalytic domain of 250 to 300 amino acids, which can be subdivided into
11 subdomains. By screening a mouse fetal liver cDNA library with
primers from the catalytic domain of other serine/threonine protein
kinases, Ligos et al. (1998) characterized a new member of the ser/thr
kinase family, which they termed Pkl12 (protein kinase expressed in day
12 fetal liver). By in vitro kinase assay using enolase as substrate,
they showed that Pkl12 can phosphorylate enolase and promote
autophosphorylation, with a ser/thr specificity. They also constructed
the human homolog, STK16, using several human ESTs with sequence
similarity to the Pkl12 gene. The STK16 gene encodes a 310-amino acid
protein that shares 94% identity with the mouse homolog. Because its
size is very close to the minimal size for a core catalytic domain, the
authors suggested that STK16 may constitute the catalytic subunit of a
multisubunit kinase. By Northern blot analysis, Ligos et al. (1998)
showed that both STK16 and Pkl12 are ubiquitously expressed at very low
levels. Expression of an STK16 fusion protein showed that STK16 is
localized with Golgi and Golgi-derived vesicles. Overexpression of STK16
leads to disorganization of the Golgi apparatus into vesicular
structures, suggesting that STK16 is involved in the secretory pathway.
By sequence walking in the EST database, followed by PCR of a fetal
kidney cDNA library, Ohta et al. (2000) obtained a cDNA encoding STK16,
which they termed TSF1. Western blot analysis of a rat pituitary cell
line showed an increase of Tsf1 level after Tgfb (190180) treatment. Gel
shift analysis indicated that Tsf1 is a sequence-specific DNA-binding
factor that binds to GC-rich elements in vascular endothelial growth
factor (VEGF; 192240) and type C natriuretic peptide (NPPC; 600296)
promoters, independent of its kinase activity and Smad3 (603109) or
Smad4 (600993). Tsf1 could not directly activate the Smad-dependent
promoter of plasminogen activator inhibitor-1 (PAI1; 173360) but could
enhance the transactivation function of Smad3 and Smad4.
*FIELD* RF
1. Ligos, J. M.; Gerwin, N.; Fernandez, P.; Gutierrez-Ramos, J. C.;
Bernad, A.: Cloning, expression analysis, and functional characterization
of PKL12, a member of a new subfamily of ser/thr kinases. Biochem.
Biophys. Res. Commun. 249: 380-384, 1998.
2. Ohta, S.; Takeuchi, M.; Deguchi, M.; Tsuji, T.; Gahara, Y.; Nagata,
K.: A novel transcriptional factor with Ser/Thr kinase activity involved
in the transforming growth factor (TGF)-beta signalling pathway. Biochem.
J. 350: 395-404, 2000.
*FIELD* CN
Paul J. Converse - updated: 2/16/2001
*FIELD* CD
Yen-Pei C. Chang: 3/23/2000
*FIELD* ED
mgross: 02/21/2001
terry: 2/16/2001
carol: 3/23/2000