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Inactive tyrosine-protein kinase 7 (Colon carcinoma kinase 4) (CCK-4) (Protein-tyrosine kinase 7) (Pseudo tyrosine kinase receptor 7) (Tyrosine-protein kinase-like 7)

 PTK7_HUMAN              Reviewed;        1070 AA.
Q13308; A8K974; B7Z477; E9PFZ5; Q13417; Q5T650; Q6IQ54; Q8NFA5;
Q8NFA6; Q8NFA7; Q8NFA8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 174.
RecName: Full=Inactive tyrosine-protein kinase 7;
AltName: Full=Colon carcinoma kinase 4;
Short=CCK-4;
AltName: Full=Protein-tyrosine kinase 7;
AltName: Full=Pseudo tyrosine kinase receptor 7;
AltName: Full=Tyrosine-protein kinase-like 7;
Flags: Precursor;
Name=PTK7; Synonyms=CCK4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon carcinoma, and Placenta;
PubMed=7478540;
Mossie K., Jallal B., Alves F., Sures I., Plowman G.D., Ullrich A.;
"Colon carcinoma kinase-4 defines a new subclass of the receptor
tyrosine kinase family.";
Oncogene 11:2179-2184(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fibroblast;
PubMed=8882711; DOI=10.1093/oxfordjournals.jbchem.a021228;
Park S.-K., Lee H.-S., Lee S.-T.;
"Characterization of the human full-length PTK7 cDNA encoding a
receptor protein tyrosine kinase-like molecule closely related to
chick KLG.";
J. Biochem. 119:235-239(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NUCLEOTIDE SEQUENCE [MRNA]
(ISOFORMS 1; 2; 3; 4 AND 5).
TISSUE=Testis;
PubMed=12427550; DOI=10.1016/S0167-4781(02)00536-5;
Jung J.-W., Ji A.-R., Lee J., Kim U.-J., Lee S.-T.;
"Organization of the human PTK7 gene encoding a receptor protein
tyrosine kinase-like molecule and alternative splicing of its mRNA.";
Biochim. Biophys. Acta 1579:153-163(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6).
TISSUE=Testis, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
GLYCOSYLATION AT ASN-646.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-646.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
FUNCTION.
PubMed=18471990; DOI=10.1016/j.bbrc.2008.04.168;
Shin W.-S., Maeng Y.-S., Jung J.-W., Min J.-K., Kwon Y.-G., Lee S.-T.;
"Soluble PTK7 inhibits tube formation, migration, and invasion of
endothelial cells and angiogenesis.";
Biochem. Biophys. Res. Commun. 371:793-798(2008).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116; ASN-175; ASN-268 AND
ASN-283.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[12]
FUNCTION.
PubMed=20558616; DOI=10.1182/blood-2010-01-262352;
Prebet T., Lhoumeau A.-C., Arnoulet C., Aulas A., Marchetto S.,
Audebert S., Puppo F., Chabannon C., Sainty D., Santoni M.-J.,
Sebbagh M., Summerour V., Huon Y., Shin W.-S., Lee S.-T., Esterni B.,
Vey N., Borg J.-P.;
"The cell polarity PTK7 receptor acts as a modulator of the
chemotherapeutic response in acute myeloid leukemia and impairs
clinical outcome.";
Blood 116:2315-2323(2010).
[13]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, CLEAVAGE, AND MUTAGENESIS
OF LEU-622; MET-641 AND MET-701.
PubMed=20837484; DOI=10.1074/jbc.M110.165159;
Golubkov V.S., Chekanov A.V., Cieplak P., Aleshin A.E., Chernov A.V.,
Zhu W., Radichev I.A., Zhang D., Dong P.D., Strongin A.Y.;
"The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a
highly efficient proteolytic target of membrane type-1 matrix
metalloproteinase: implications in cancer and embryogenesis.";
J. Biol. Chem. 285:35740-35749(2010).
[14]
FUNCTION.
PubMed=21103379; DOI=10.1371/journal.pone.0014018;
Meng L., Sefah K., O'Donoghue M.B., Zhu G., Shangguan D., Noorali A.,
Chen Y., Zhou L., Tan W.;
"Silencing of PTK7 in colon cancer cells: caspase-10-dependent
apoptosis via mitochondrial pathway.";
PLoS ONE 5:E14018-E14018(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
FUNCTION, INTERACTION WITH CTNNB1, AND REGION.
PubMed=21132015; DOI=10.1038/embor.2010.185;
Puppo F., Thome V., Lhoumeau A.-C., Cibois M., Gangar A., Lembo F.,
Belotti E., Marchetto S., Lecine P., Prebet T., Sebbagh M.,
Shin W.-S., Lee S.-T., Kodjabachian L., Borg J.-P.;
"Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin
canonical signalling.";
EMBO Rep. 12:43-49(2011).
[17]
VARIANTS [LARGE SCALE ANALYSIS] HIS-276; SER-410; ASP-745; GLN-766;
VAL-777; ARG-783; VAL-933; THR-1029 AND GLN-1038.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Inactive tyrosine kinase involved in Wnt signaling
pathway. Component of both the non-canonical (also known as the
Wnt/planar cell polarity signaling) and the canonical Wnt
signaling pathway. Functions in cell adhesion, cell migration,
cell polarity, proliferation, actin cytoskeleton reorganization
and apoptosis. Has a role in embryogenesis, epithelial tissue
organization and angiogenesis. {ECO:0000269|PubMed:18471990,
ECO:0000269|PubMed:20558616, ECO:0000269|PubMed:20837484,
ECO:0000269|PubMed:21103379, ECO:0000269|PubMed:21132015}.
-!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:21132015}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=5; IntAct=EBI-2803245, EBI-491549;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20837484};
Single-pass type I membrane protein {ECO:0000269|PubMed:20837484}.
Cell junction {ECO:0000269|PubMed:20837484}. Note=Colocalizes with
MMP14 at cell junctions. Also localizes at the leading edge of
migrating cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=PTK7-1;
IsoId=Q13308-1; Sequence=Displayed;
Name=2; Synonyms=PTK7-2;
IsoId=Q13308-2; Sequence=VSP_037182;
Name=3; Synonyms=PTK7-3;
IsoId=Q13308-3; Sequence=VSP_037181;
Name=4; Synonyms=PTK7-4;
IsoId=Q13308-4; Sequence=VSP_037183;
Name=5; Synonyms=PTK7-5;
IsoId=Q13308-5; Sequence=VSP_037184, VSP_037185;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=6;
IsoId=Q13308-6; Sequence=VSP_044775;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in lung, liver, pancreas,
kidney, placenta and melanocytes. Weakly expressed in thyroid
gland, ovary, brain, heart and skeletal muscle. Also expressed in
erythroleukemia cells. But not expressed in colon.
-!- INDUCTION: Higher expression in cell lines established from normal
non-tumorigenic tissues compared to cell lines established from
highly metastatic invasive carcinomas (at protein level).
{ECO:0000269|PubMed:20837484}.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive.
-!- PTM: MMP14 cleaves PTK7 between Pro-621 and Leu-622 generating an
N-terminal soluble (70 kDa) fragment and a membrane C-terminal (50
kDa) fragment. Proteolysis by MMP14 regulates PTK7 function in
non-canonical Wnt signaling pathway.
{ECO:0000269|PubMed:20837484}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTK7ID41901ch6p21.html";
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EMBL; U33635; AAA87565.1; -; mRNA.
EMBL; U40271; AAC50484.2; -; mRNA.
EMBL; AF447176; AAL39062.1; -; Genomic_DNA.
EMBL; AF447157; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447158; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447162; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447164; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447167; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447170; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447171; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447173; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447174; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF447175; AAL39062.1; JOINED; Genomic_DNA.
EMBL; AF531868; AAN04862.1; -; mRNA.
EMBL; AF531869; AAN04863.1; -; mRNA.
EMBL; AF531870; AAN04864.1; -; mRNA.
EMBL; AF531871; AAN04865.1; -; mRNA.
EMBL; AF531872; AAN04866.1; -; mRNA.
EMBL; AK291016; BAF83705.1; -; mRNA.
EMBL; AK292589; BAF85278.1; -; mRNA.
EMBL; AK296953; BAH12463.1; -; mRNA.
EMBL; AL355385; CAI13783.1; -; Genomic_DNA.
EMBL; CH471081; EAX04154.1; -; Genomic_DNA.
EMBL; CH471081; EAX04155.1; -; Genomic_DNA.
EMBL; CH471081; EAX04156.1; -; Genomic_DNA.
EMBL; CH471081; EAX04158.1; -; Genomic_DNA.
EMBL; CH471081; EAX04160.1; -; Genomic_DNA.
EMBL; BC071557; AAH71557.1; -; mRNA.
CCDS; CCDS4884.1; -. [Q13308-1]
CCDS; CCDS4885.1; -. [Q13308-2]
CCDS; CCDS4886.1; -. [Q13308-3]
CCDS; CCDS4887.1; -. [Q13308-4]
CCDS; CCDS59021.1; -. [Q13308-6]
PIR; JC4593; JC4593.
RefSeq; NP_001257327.1; NM_001270398.1. [Q13308-6]
RefSeq; NP_002812.2; NM_002821.4. [Q13308-1]
RefSeq; NP_690619.1; NM_152880.3. [Q13308-2]
RefSeq; NP_690620.1; NM_152881.3. [Q13308-3]
RefSeq; NP_690621.1; NM_152882.3. [Q13308-4]
UniGene; Hs.90572; -.
ProteinModelPortal; Q13308; -.
SMR; Q13308; -.
BioGrid; 111721; 43.
IntAct; Q13308; 17.
MINT; MINT-4532536; -.
STRING; 9606.ENSP00000230419; -.
iPTMnet; Q13308; -.
PhosphoSitePlus; Q13308; -.
SwissPalm; Q13308; -.
UniCarbKB; Q13308; -.
BioMuta; PTK7; -.
DMDM; 116242736; -.
EPD; Q13308; -.
MaxQB; Q13308; -.
PaxDb; Q13308; -.
PeptideAtlas; Q13308; -.
PRIDE; Q13308; -.
TopDownProteomics; Q13308-3; -. [Q13308-3]
DNASU; 5754; -.
Ensembl; ENST00000230418; ENSP00000230418; ENSG00000112655. [Q13308-5]
Ensembl; ENST00000230419; ENSP00000230419; ENSG00000112655. [Q13308-1]
Ensembl; ENST00000345201; ENSP00000325992; ENSG00000112655. [Q13308-2]
Ensembl; ENST00000349241; ENSP00000325462; ENSG00000112655. [Q13308-3]
Ensembl; ENST00000352931; ENSP00000326029; ENSG00000112655. [Q13308-4]
Ensembl; ENST00000481273; ENSP00000418754; ENSG00000112655. [Q13308-6]
GeneID; 5754; -.
KEGG; hsa:5754; -.
UCSC; uc003oub.3; human. [Q13308-1]
CTD; 5754; -.
DisGeNET; 5754; -.
EuPathDB; HostDB:ENSG00000112655.15; -.
GeneCards; PTK7; -.
HGNC; HGNC:9618; PTK7.
HPA; HPA003222; -.
MIM; 601890; gene.
neXtProt; NX_Q13308; -.
OpenTargets; ENSG00000112655; -.
PharmGKB; PA33961; -.
eggNOG; KOG1026; Eukaryota.
eggNOG; KOG4475; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118818; -.
HOGENOM; HOG000115767; -.
HOVERGEN; HBG008320; -.
InParanoid; Q13308; -.
KO; K05127; -.
OrthoDB; EOG091G0BWE; -.
PhylomeDB; Q13308; -.
TreeFam; TF326835; -.
SIGNOR; Q13308; -.
ChiTaRS; PTK7; human.
GeneWiki; PTK7; -.
GenomeRNAi; 5754; -.
PRO; PR:Q13308; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112655; -.
CleanEx; HS_PTK7; -.
ExpressionAtlas; Q13308; baseline and differential.
Genevisible; Q13308; HS.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:1904929; F:coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0003401; P:axis elongation; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
GO; GO:0060026; P:convergent extension; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR033592; PTK7.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
PANTHER; PTHR26391:SF15; PTHR26391:SF15; 2.
Pfam; PF07679; I-set; 3.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00409; IG; 7.
SMART; SM00408; IGc2; 7.
SUPFAM; SSF48726; SSF48726; 7.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 7.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1070 Inactive tyrosine-protein kinase 7.
/FTId=PRO_0000016748.
TOPO_DOM 31 704 Extracellular. {ECO:0000255}.
TRANSMEM 705 725 Helical. {ECO:0000255}.
TOPO_DOM 726 1070 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 120 Ig-like C2-type 1.
DOMAIN 128 218 Ig-like C2-type 2.
DOMAIN 225 317 Ig-like C2-type 3.
DOMAIN 309 407 Ig-like C2-type 4.
DOMAIN 412 497 Ig-like C2-type 5.
DOMAIN 503 586 Ig-like C2-type 6.
DOMAIN 578 680 Ig-like C2-type 7.
DOMAIN 796 1066 Protein kinase; inactive.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 794 1070 Interaction with CTNNB1.
{ECO:0000269|PubMed:21132015}.
SITE 621 622 Cleavage; by MMP14.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BKG3}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
DISULFID 53 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 200 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 246 301 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 343 391 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 433 481 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 524 570 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 613 664 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 26 MGAARGSPARPRRLPLLSVLLLPLLG -> MGSFLSGEKRP
SAPTVGSAMEKKEFPTPPGRVGP (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044775.
VAR_SEQ 410 540 TVPSWLKKPQDSQLEEGKPGYLDCLTQATPKPTVVWYRNQM
LISEDSRFEVFKNGTLRINSVEVYDGTWYRCMSSTPAGSIE
AQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKP
TIKWERAD -> N (in isoform 3).
{ECO:0000303|PubMed:12427550}.
/FTId=VSP_037181.
VAR_SEQ 500 539 Missing (in isoform 2).
{ECO:0000303|PubMed:12427550,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_037182.
VAR_SEQ 627 682 Missing (in isoform 4).
{ECO:0000303|PubMed:12427550}.
/FTId=VSP_037183.
VAR_SEQ 804 816 KSEFGEVFLAKAQ -> RPQAVPEDFQEQG (in
isoform 5).
{ECO:0000303|PubMed:12427550}.
/FTId=VSP_037184.
VAR_SEQ 817 1070 Missing (in isoform 5).
{ECO:0000303|PubMed:12427550}.
/FTId=VSP_037185.
VARIANT 276 276 R -> H (in dbSNP:rs56188167).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041502.
VARIANT 410 410 T -> S (in dbSNP:rs34021075).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041503.
VARIANT 745 745 E -> D (in dbSNP:rs9472017).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041504.
VARIANT 766 766 E -> Q (in dbSNP:rs56216742).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041505.
VARIANT 777 777 A -> V (in dbSNP:rs34764696).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041506.
VARIANT 783 783 H -> R (in dbSNP:rs55820547).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041507.
VARIANT 933 933 A -> V (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041508.
VARIANT 1029 1029 P -> T (in dbSNP:rs55755163).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041509.
VARIANT 1038 1038 R -> Q (in dbSNP:rs34865794).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041510.
MUTAGEN 622 622 L->D: Prevents proteolysis by MMP14.
{ECO:0000269|PubMed:20837484}.
MUTAGEN 641 641 M->R: No impact on proteolysis by MMP14.
{ECO:0000269|PubMed:20837484}.
MUTAGEN 701 701 M->D: No impact on proteolysis by MMP14.
{ECO:0000269|PubMed:20837484}.
CONFLICT 87 87 F -> L (in Ref. 4; BAF85278).
{ECO:0000305}.
CONFLICT 92 92 R -> P (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 93 93 L -> P (in Ref. 7; AAH71557).
{ECO:0000305}.
CONFLICT 147 147 T -> K (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 207 207 G -> S (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 495 496 RV -> VL (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 515 515 E -> G (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 755 755 Q -> R (in Ref. 4; BAH12463).
{ECO:0000305}.
CONFLICT 799 799 I -> F (in Ref. 4; BAF85278).
{ECO:0000305}.
CONFLICT 881 881 G -> E (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 969 969 P -> A (in Ref. 1; AAA87565).
{ECO:0000305}.
CONFLICT 992 992 F -> S (in Ref. 1; AAA87565).
{ECO:0000305}.
SEQUENCE 1070 AA; 118392 MW; 304926A1774EB5F4 CRC64;
MGAARGSPAR PRRLPLLSVL LLPLLGGTQT AIVFIKQPSS QDALQGRRAL LRCEVEAPGP
VHVYWLLDGA PVQDTERRFA QGSSLSFAAV DRLQDSGTFQ CVARDDVTGE EARSANASFN
IKWIEAGPVV LKHPASEAEI QPQTQVTLRC HIDGHPRPTY QWFRDGTPLS DGQSNHTVSS
KERNLTLRPA GPEHSGLYSC CAHSAFGQAC SSQNFTLSIA DESFARVVLA PQDVVVARYE
EAMFHCQFSA QPPPSLQWLF EDETPITNRS RPPHLRRATV FANGSLLLTQ VRPRNAGIYR
CIGQGQRGPP IILEATLHLA EIEDMPLFEP RVFTAGSEER VTCLPPKGLP EPSVWWEHAG
VRLPTHGRVY QKGHELVLAN IAESDAGVYT CHAANLAGQR RQDVNITVAT VPSWLKKPQD
SQLEEGKPGY LDCLTQATPK PTVVWYRNQM LISEDSRFEV FKNGTLRINS VEVYDGTWYR
CMSSTPAGSI EAQARVQVLE KLKFTPPPQP QQCMEFDKEA TVPCSATGRE KPTIKWERAD
GSSLPEWVTD NAGTLHFARV TRDDAGNYTC IASNGPQGQI RAHVQLTVAV FITFKVEPER
TTVYQGHTAL LQCEAQGDPK PLIQWKGKDR ILDPTKLGPR MHIFQNGSLV IHDVAPEDSG
RYTCIAGNSC NIKHTEAPLY VVDKPVPEES EGPGSPPPYK MIQTIGLSVG AAVAYIIAVL
GLMFYCKKRC KAKRLQKQPE GEEPEMECLN GGPLQNGQPS AEIQEEVALT SLGSGPAATN
KRHSTSDKMH FPRSSLQPIT TLGKSEFGEV FLAKAQGLEE GVAETLVLVK SLQSKDEQQQ
LDFRRELEMF GKLNHANVVR LLGLCREAEP HYMVLEYVDL GDLKQFLRIS KSKDEKLKSQ
PLSTKQKVAL CTQVALGMEH LSNNRFVHKD LAARNCLVSA QRQVKVSALG LSKDVYNSEY
YHFRQAWVPL RWMSPEAILE GDFSTKSDVW AFGVLMWEVF THGEMPHGGQ ADDEVLADLQ
AGKARLPQPE GCPSKLYRLM QRCWALSPKD RPSFSEIASA LGDSTVDSKP


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