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Protein-tyrosine kinase 6 (EC 2.7.10.2) (SRC-related intestinal kinase)

 PTK6_MOUSE              Reviewed;         451 AA.
Q64434;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 164.
RecName: Full=Protein-tyrosine kinase 6;
EC=2.7.10.2;
AltName: Full=SRC-related intestinal kinase;
Name=Ptk6; Synonyms=Sik;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ, and ICR; TISSUE=Intestinal crypt;
PubMed=7838533;
Vasioukhin V., Serfas M.S., Siyanova E.Y., Polonskaia M.,
Costigan V.J., Liu B., Thomason A., Tyner A.L.;
"A novel intracellular epithelial cell tyrosine kinase is expressed in
the skin and gastrointestinal tract.";
Oncogene 10:349-357(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
STRAIN=BALB/cJ;
Siyanova E.Y.;
"Promoter region of the mouse sik gene.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH GAP-A.P65.
PubMed=9405638; DOI=10.1073/pnas.94.26.14477;
Vasioukhin V., Tyner A.L.;
"A role for the epithelial-cell-specific tyrosine kinase Sik during
keratinocyte differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 94:14477-14482(1997).
[4]
DEVELOPMENTAL STAGE.
PubMed=10430081;
Llor X., Serfas M.S., Bie W., Vasioukhin V., Polonskaia M., Derry J.,
Abbott C.M., Tyner A.L.;
"BRK/Sik expression in the gastrointestinal tract and in colon
tumors.";
Clin. Cancer Res. 5:1767-1777(1999).
[5]
INTERACTION WITH KHDRBS1, MUTAGENESIS OF TYR-447, SUBCELLULAR
LOCATION, ENZYME REGULATION, AND FUNCTION IN PHOSPHORYLATION OF
KHDRBS1.
PubMed=10913193; DOI=10.1128/MCB.20.16.6114-6126.2000;
Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V.,
Cochrane A.W., Chen T., Tyner A.L.;
"Sik (BRK) phosphorylates Sam68 in the nucleus and negatively
regulates its RNA binding ability.";
Mol. Cell. Biol. 20:6114-6126(2000).
[6]
SUBCELLULAR LOCATION.
PubMed=12833144; DOI=10.1038/sj.onc.1206465;
Derry J.J., Prins G.S., Ray V., Tyner A.L.;
"Altered localization and activity of the intracellular tyrosine
kinase BRK/Sik in prostate tumor cells.";
Oncogene 22:4212-4220(2003).
[7]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15471878; DOI=10.1074/jbc.M409579200;
Haegebarth A., Heap D., Bie W., Derry J.J., Richard S., Tyner A.L.;
"The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the
RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and
SLM-2.";
J. Biol. Chem. 279:54398-54404(2004).
[8]
DISRUPTION PHENOTYPE.
PubMed=16782882; DOI=10.1128/MCB.01901-05;
Haegebarth A., Bie W., Yang R., Crawford S.E., Vasioukhin V.,
Fuchs E., Tyner A.L.;
"Protein tyrosine kinase 6 negatively regulates growth and promotes
enterocyte differentiation in the small intestine.";
Mol. Cell. Biol. 26:4949-4957(2006).
[9]
FUNCTION IN APOPTOSIS.
PubMed=19501589; DOI=10.1053/j.gastro.2009.05.054;
Haegebarth A., Perekatt A.O., Bie W., Gierut J.J., Tyner A.L.;
"Induction of protein tyrosine kinase 6 in mouse intestinal crypt
epithelial cells promotes DNA damage-induced apoptosis.";
Gastroenterology 137:945-954(2009).
-!- FUNCTION: Non-receptor tyrosine-protein kinase implicated in the
regulation of a variety of signaling pathways that control the
differentiation and maintenance of normal epithelia, as well as
tumor growth. Function seems to be context dependent and differ
depending on cell type, as well as its intracellular localization.
A number of potential nuclear and cytoplasmic substrates have been
identified. These include the RNA-binding proteins: KHDRBS1/SAM68,
KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors:
STAT3 and STAT5A/B and a variety of signaling molecules:
ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates
also with a variety of proteins that are likely upstream of PTK6
in various signaling pathways, or for which PTK6 may play an
adapter-like role. These proteins include ADAM15, EGFR, ERBB2,
ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6
promotes cellular differentiation and apoptosis. In tumors PTK6
contributes to cancer progression by sensitizing cells to
mitogenic signals and enhancing proliferation, anchorage-
independent survival and migration/invasion. Association with
EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and
growth through enhancement of EGF-induced signaling via BTK/AKT
and PI3 kinase. Contributes to migration and proliferation by
contributing to EGF-mediated phosphorylation of
ARHGAP35/p190RhoGAP, which promotes association with
RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF
stimulation resulted in phosphorylation of PNX/Paxillin by PTK6
and activation of RAC1 via CRK/CrKII, thereby promoting migration
and invasion. PTK6 activates STAT3 and STAT5B to promote
proliferation. Nuclear PTK6 may be important for regulating growth
in normal epithelia, while cytoplasmic PTK6 might activate
oncogenic signaling pathways. {ECO:0000269|PubMed:10913193,
ECO:0000269|PubMed:15471878, ECO:0000269|PubMed:19501589}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Activated by EGF, NRG1 and IGF1. Inhibited by
SOCS3 to phosphorylate STAT3. Stabilized in the inactive form by
an association between the SH3 domain and the SH2-TK linker
region. Interaction between Trp-184 within SH2-TK linker region
and the catalytic domain appears essential for positive regulation
of kinase activity. {ECO:0000269|PubMed:10913193}.
-!- SUBUNIT: Interacts with KHDRBS1. Interacts with phosphorylated
IRS4 (By similarity). Interacts with GAP-A.p65. Interacts with
ADAM15 (By similarity). Interacts (via SH3 and SH2 domains) with
phosphorylated IRS4 (By similarity). Interacts (via SH3 domain)
with SFPQ (By similarity). Interacts with EGFR and ERBB2 (By
similarity). Interacts with STAP2 (By similarity). Interacts with
PNX (By similarity). Interacts with SFPQ (By similarity).
Interacts with PTK/ATK (By similarity). Interacts with CTNNB1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane. Cell
projection, ruffle {ECO:0000250}. Note=Also found to be membrane-
associated. Colocalizes with KHDRBS1, within the nucleus.
-!- TISSUE SPECIFICITY: Expressed only in epithelial tissues,
including the skin and lining of the alimentary canal. Restricted
to the cell layers immediately above the proliferative cell zone
in these epithelia. {ECO:0000269|PubMed:15471878}.
-!- DEVELOPMENTAL STAGE: First detected at day 15.5 of gestation in
the embryo, where it is expressed in the newly forming granular
layer of the skin. Is found in stomach at day 17.5.
{ECO:0000269|PubMed:10430081}.
-!- DOMAIN: The SH3 domain plays a major role in substrate
interactions. The SH2 domain of PTK6 plays a role in protein-
protein interactions, but is likely more important for the
regulation of catalytic activity (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated. Autophosphorylation of Tyr-342 leads to
an increase of kinase activity. Tyr-447 binds to the SH2 domain
when phosphorylated and negatively regulates kinase activity (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Deficient mice have an increased cell
turnover in the small intestine, which is accompanied by increased
villus length and crypt depth and delayed enterocyte
differentiation that is accompanied by increased PTK/AKT and WNT
signaling. {ECO:0000269|PubMed:16782882}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. BRK/PTK6/SIK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U16805; AAA67929.1; -; mRNA.
EMBL; AF016545; AAB94550.1; -; Genomic_DNA.
CCDS; CCDS17203.1; -.
RefSeq; NP_033210.1; NM_009184.2.
UniGene; Mm.4497; -.
ProteinModelPortal; Q64434; -.
SMR; Q64434; -.
IntAct; Q64434; 1.
MINT; Q64434; -.
STRING; 10090.ENSMUSP00000016511; -.
iPTMnet; Q64434; -.
PhosphoSitePlus; Q64434; -.
MaxQB; Q64434; -.
PaxDb; Q64434; -.
PRIDE; Q64434; -.
Ensembl; ENSMUST00000016511; ENSMUSP00000016511; ENSMUSG00000038751.
GeneID; 20459; -.
KEGG; mmu:20459; -.
UCSC; uc008olk.1; mouse.
CTD; 5753; -.
MGI; MGI:99683; Ptk6.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; Q64434; -.
KO; K08894; -.
OMA; VRHYKIW; -.
OrthoDB; EOG091G0596; -.
PhylomeDB; Q64434; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-MMU-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
Reactome; R-MMU-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-MMU-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-MMU-8849472; PTK6 Down-Regulation.
Reactome; R-MMU-8849474; PTK6 Activates STAT3.
Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
ChiTaRS; Nop58; mouse.
PRO; PR:Q64434; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000038751; -.
CleanEx; MM_PTK6; -.
ExpressionAtlas; Q64434; baseline and differential.
Genevisible; Q64434; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0060575; P:intestinal epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0045926; P:negative regulation of growth; IMP:UniProtKB.
GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
CDD; cd10358; SH2_PTK6_Brk; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR035846; PTK6_SH2.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
ATP-binding; Cell projection; Complete proteome; Cytoplasm; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
CHAIN 1 451 Protein-tyrosine kinase 6.
/FTId=PRO_0000088134.
DOMAIN 8 72 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 78 170 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 191 445 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 197 205 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 171 190 Linker.
ACT_SITE 312 312 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 219 219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 13 13 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 61 61 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 66 66 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 114 114 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 342 342 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 351 351 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882}.
MOD_RES 447 447 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q13882,
ECO:0000305}.
MUTAGEN 447 447 Y->F: Increase in the kinase activation
level. {ECO:0000269|PubMed:10913193}.
SEQUENCE 451 AA; 51972 MW; 8FBEC26025498DEC CRC64;
MVSWDKAHLG PKYVGLWDFK ARTDEELSFQ AGDLLHVTKK EELWWWATLL DAEGKALAEG
YVPHNYLAEK ETVESEPWFF GCISRSEAMH RLQAEDNSKG AFLIRVSQKP GADYVLSVRD
AQAVRHYRIW KNNEGRLHLN EAVSFSNLSE LVDYHKTQSL SHGLQLSMPC WKHKTEPLPH
WDDWERPREE FTLCKKLGAG YFGEVFEALW KGQVHVAVKV ISRDNLLHQH TFQAEIQAMK
KLRHKHILSL YAVATAGDPV YIITELMPKG NLLQLLRDSD EKALPILELV DFASQVAEGM
CYLESQNYIH RDLAARNVLV TENNLCKVGD FGLARLVKED IYLSHEHNVP YKWTAPEALS
RGHYSIKSDV WSFGVLLHEI FSRGQMPYPG MSNHETFLRV DAGYRMPCPL ECPPNIHKLM
LSCWSRDPKQ RPCFKDLCEK LTGITRYENL V


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