STYK1_MOUSE
ID STYK1_MOUSE Reviewed; 429 AA.
AC Q6J9G1; Q8BZH6; Q8BZT1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tyrosine-protein kinase STYK1;
DE EC=2.7.10.2;
DE AltName: Full=Novel oncogene with kinase domain;
DE Short=mNOK;
DE AltName: Full=Serine/threonine/tyrosine kinase 1;
GN Name=Styk1; Synonyms=Nok;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=KM; TISSUE=Colon;
RX PubMed=15150103; DOI=10.1158/0008-5472.can-03-2106;
RA Liu L., Yu X.-Z., Li T.-S., Song L.-X., Chen P.-L., Suo T.-L., Li Y.-H.,
RA Wang S.-D., Chen Y., Ren Y.-M., Zhang S.-P., Chang Z.-J., Fu X.-Y.;
RT "A novel protein tyrosine kinase NOK that shares homology with platelet-
RT derived growth factor/fibroblast growth factor receptors induces
RT tumorigenesis and metastasis in nude mice.";
RL Cancer Res. 64:3491-3499(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Urinary bladder;
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).
CC -!- FUNCTION: Probable tyrosine protein-kinase, which has strong
CC transforming capabilities on a variety of cell lines including NIH 3T3
CC fibroblasts and on athymic nude mice. When overexpressed, it can also
CC induce tumor cell invasion as well as metastasis in distant organs. May
CC act by activating both MAP kinase and phosphatidylinositol 3'-kinases
CC (PI3K) pathways. {ECO:0000269|PubMed:15150103}.
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:PRU10028};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6J9G1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6J9G1-2; Sequence=VSP_013427;
CC -!- TISSUE SPECIFICITY: Highly expressed in colon and small intestine.
CC Weakly or not expressed in spleen, skeletal muscle, liver, kidney,
CC heart and brain. Expressed in transformed kidney cell lines (COS-1 and
CC HEK293T). {ECO:0000269|PubMed:15150103}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY563053; AAT01225.1; -; mRNA.
DR EMBL; AK033606; BAC28386.1; -; mRNA.
DR EMBL; AK035247; BAC29000.1; -; mRNA.
DR CCDS; CCDS20604.1; -. [Q6J9G1-1]
DR RefSeq; NP_766479.1; NM_172891.2. [Q6J9G1-1]
DR RefSeq; XP_006506194.1; XM_006506131.3. [Q6J9G1-1]
DR RefSeq; XP_006506195.1; XM_006506132.3. [Q6J9G1-1]
DR AlphaFoldDB; Q6J9G1; -.
DR SMR; Q6J9G1; -.
DR STRING; 10090.ENSMUSP00000044098; -.
DR iPTMnet; Q6J9G1; -.
DR PhosphoSitePlus; Q6J9G1; -.
DR MaxQB; Q6J9G1; -.
DR PaxDb; Q6J9G1; -.
DR PRIDE; Q6J9G1; -.
DR ProteomicsDB; 258668; -. [Q6J9G1-1]
DR ProteomicsDB; 258669; -. [Q6J9G1-2]
DR Antibodypedia; 23371; 328 antibodies from 34 providers.
DR DNASU; 243659; -.
DR Ensembl; ENSMUST00000049150; ENSMUSP00000044098; ENSMUSG00000032899. [Q6J9G1-1]
DR Ensembl; ENSMUST00000121078; ENSMUSP00000112900; ENSMUSG00000032899. [Q6J9G1-2]
DR GeneID; 243659; -.
DR KEGG; mmu:243659; -.
DR UCSC; uc009eir.1; mouse. [Q6J9G1-1]
DR UCSC; uc012eub.1; mouse. [Q6J9G1-2]
DR CTD; 55359; -.
DR MGI; MGI:2141396; Styk1.
DR VEuPathDB; HostDB:ENSMUSG00000032899; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000157871; -.
DR HOGENOM; CLU_000288_7_7_1; -.
DR InParanoid; Q6J9G1; -.
DR OMA; TFLWTCR; -.
DR OrthoDB; 1068299at2759; -.
DR PhylomeDB; Q6J9G1; -.
DR TreeFam; TF316675; -.
DR BioGRID-ORCS; 243659; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q6J9G1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6J9G1; protein.
DR Bgee; ENSMUSG00000032899; Expressed in animal zygote and 123 other tissues.
DR Genevisible; Q6J9G1; MM.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW Proto-oncogene; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..429
FT /note="Tyrosine-protein kinase STYK1"
FT /id="PRO_0000088164"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 119..390
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 125..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 67..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013427"
FT CONFLICT 24
FT /note="R -> Q (in Ref. 1; AAT01225)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="M -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="T -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48121 MW; 480130D319551F61 CRC64;
MGEKGHLSRV LLECSLSDKL CVVREKQYEV IIVPALLVGG FLILLAIILW LFIRGQRSQR
QSPGPRGTAS VPASRGRSQE AAGHGEKVLL PLKETSVEGF LRAATPRLAK LQVPREQLLE
VLEQIHSGSC GTLYHATMTT KDHPKPKSVV LKALEDPVGL QEVQDFIGRI QFYQYLGKHK
NLVQLEGCCT ERLPLYMMLE DVVPGDLLSF LWTCRRDVMT MDGLLYDLTE KQIYHIGKQI
LLALEFLQEK HLFHGDVAAR NILIQSDLTP KLCHLGLAYE VHAHGAISSA RSSTIPLKWL
APERLLLRPA SIRGDIWSFG ILLYEMVTLG APPYPEVPPT SILQYLQRKK IMKRPSSCSH
AMYNIMKCCW RWSEDSRPLL GQLLQRLEAA SRSADDKAVL QVPELVVPEL YADVAGIRAE
SISYSFSVL
