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Q13308 (PTK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inactive tyrosine-protein kinase 7
Alternative name(s):
Colon carcinoma kinase 4
Short name=CCK-4
Protein-tyrosine kinase 7
Pseudo tyrosine kinase receptor 7
Tyrosine-protein kinase-like 7
Gene names
Name:PTK7
Synonyms:CCK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1070 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.12 Ref.13 Ref.14 Ref.16

Subunit structure

Interacts with CTNNB1. Ref.16

Subcellular location

Membrane; Single-pass type I membrane protein. Cell junction. Note: Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells. Ref.13

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). Ref.13

Domain

The protein kinase domain is predicted to be catalytically inactive.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell adhesion
Wnt signaling pathway
   Cellular componentCell junction
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from mutant phenotype Ref.13. Source: UniProtKB

axis elongation

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.16. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype Ref.13. Source: UniProtKB

cellular response to retinoic acid

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

cochlea morphogenesis

Inferred from electronic annotation. Source: Ensembl

convergent extension

Inferred from electronic annotation. Source: Ensembl

establishment of epithelial cell apical/basal polarity

Inferred from electronic annotation. Source: Ensembl

establishment of planar polarity

Inferred from electronic annotation. Source: Ensembl

lung-associated mesenchyme development

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.2. Source: GOC

planar cell polarity pathway involved in neural tube closure

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

signal transduction

Traceable author statement Ref.1. Source: ProtInc

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.13. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352225EBI-2803245,EBI-491549

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13308-1)

Also known as: PTK7-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13308-2)

Also known as: PTK7-2;

The sequence of this isoform differs from the canonical sequence as follows:
     500-539: Missing.
Isoform 3 (identifier: Q13308-3)

Also known as: PTK7-3;

The sequence of this isoform differs from the canonical sequence as follows:
     410-540: TVPSWLKKPQ...KPTIKWERAD → N
Isoform 4 (identifier: Q13308-4)

Also known as: PTK7-4;

The sequence of this isoform differs from the canonical sequence as follows:
     627-682: Missing.
Isoform 5 (identifier: Q13308-5)

Also known as: PTK7-5;

The sequence of this isoform differs from the canonical sequence as follows:
     804-816: KSEFGEVFLAKAQ → RPQAVPEDFQEQG
     817-1070: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 6 (identifier: Q13308-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MGAARGSPARPRRLPLLSVLLLPLLG → MGSFLSGEKRPSAPTVGSAMEKKEFPTPPGRVGP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 10701040Inactive tyrosine-protein kinase 7
PRO_0000016748

Regions

Topological domain31 – 704674Extracellular Potential
Transmembrane705 – 72521Helical; Potential
Topological domain726 – 1070345Cytoplasmic Potential
Domain31 – 12090Ig-like C2-type 1
Domain128 – 21891Ig-like C2-type 2
Domain225 – 31793Ig-like C2-type 3
Domain309 – 40799Ig-like C2-type 4
Domain412 – 49786Ig-like C2-type 5
Domain503 – 58684Ig-like C2-type 6
Domain578 – 680103Ig-like C2-type 7
Domain796 – 1066271Protein kinase; inactive
Region794 – 1070277Interaction with CTNNB1

Sites

Site621 – 6222Cleavage; by MMP14

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...) Ref.11
Glycosylation1751N-linked (GlcNAc...) Ref.11
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Ref.11
Glycosylation2831N-linked (GlcNAc...) Ref.11
Glycosylation4051N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Ref.8 Ref.9
Disulfide bond53 ↔ 101 By similarity
Disulfide bond150 ↔ 200 By similarity
Disulfide bond246 ↔ 301 By similarity
Disulfide bond343 ↔ 391 By similarity
Disulfide bond433 ↔ 481 By similarity
Disulfide bond524 ↔ 570 By similarity
Disulfide bond613 ↔ 664 By similarity

Natural variations

Alternative sequence1 – 2626MGAAR…LPLLG → MGSFLSGEKRPSAPTVGSAM EKKEFPTPPGRVGP in isoform 6.
VSP_044775
Alternative sequence410 – 540131TVPSW…WERAD → N in isoform 3.
VSP_037181
Alternative sequence500 – 53940Missing in isoform 2.
VSP_037182
Alternative sequence627 – 68256Missing in isoform 4.
VSP_037183
Alternative sequence804 – 81613KSEFG…LAKAQ → RPQAVPEDFQEQG in isoform 5.
VSP_037184
Alternative sequence817 – 1070254Missing in isoform 5.
VSP_037185
Natural variant2761R → H. Ref.17
Corresponds to variant rs56188167 [ dbSNP | Ensembl ].
VAR_041502
Natural variant4101T → S. Ref.17
Corresponds to variant rs34021075 [ dbSNP | Ensembl ].
VAR_041503
Natural variant7451E → D. Ref.17
Corresponds to variant rs9472017 [ dbSNP | Ensembl ].
VAR_041504
Natural variant7661E → Q. Ref.17
Corresponds to variant rs56216742 [ dbSNP | Ensembl ].
VAR_041505
Natural variant7771A → V. Ref.17
Corresponds to variant rs34764696 [ dbSNP | Ensembl ].
VAR_041506
Natural variant7831H → R. Ref.17
Corresponds to variant rs55820547 [ dbSNP | Ensembl ].
VAR_041507
Natural variant9331A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.17
VAR_041508
Natural variant10291P → T. Ref.17
Corresponds to variant rs55755163 [ dbSNP | Ensembl ].
VAR_041509
Natural variant10381R → Q. Ref.17
Corresponds to variant rs34865794 [ dbSNP | Ensembl ].
VAR_041510

Experimental info

Mutagenesis6221L → D: Prevents proteolysis by MMP14. Ref.13
Mutagenesis6411M → R: No impact on proteolysis by MMP14. Ref.13
Mutagenesis7011M → D: No impact on proteolysis by MMP14. Ref.13
Sequence conflict871F → L in BAF85278. Ref.4
Sequence conflict921R → P in AAA87565. Ref.1
Sequence conflict931L → P in AAH71557. Ref.7
Sequence conflict1471T → K in AAA87565. Ref.1
Sequence conflict2071G → S in AAA87565. Ref.1
Sequence conflict495 – 4962RV → VL in AAA87565. Ref.1
Sequence conflict5151E → G in AAA87565. Ref.1
Sequence conflict7551Q → R in BAH12463. Ref.4
Sequence conflict7991I → F in BAF85278. Ref.4
Sequence conflict8811G → E in AAA87565. Ref.1
Sequence conflict9691P → A in AAA87565. Ref.1
Sequence conflict9921F → S in AAA87565. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PTK7-1) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 304926A1774EB5F4

FASTA1,070118,392
        10         20         30         40         50         60 
MGAARGSPAR PRRLPLLSVL LLPLLGGTQT AIVFIKQPSS QDALQGRRAL LRCEVEAPGP 

        70         80         90        100        110        120 
VHVYWLLDGA PVQDTERRFA QGSSLSFAAV DRLQDSGTFQ CVARDDVTGE EARSANASFN 

       130        140        150        160        170        180 
IKWIEAGPVV LKHPASEAEI QPQTQVTLRC HIDGHPRPTY QWFRDGTPLS DGQSNHTVSS 

       190        200        210        220        230        240 
KERNLTLRPA GPEHSGLYSC CAHSAFGQAC SSQNFTLSIA DESFARVVLA PQDVVVARYE 

       250        260        270        280        290        300 
EAMFHCQFSA QPPPSLQWLF EDETPITNRS RPPHLRRATV FANGSLLLTQ VRPRNAGIYR 

       310        320        330        340        350        360 
CIGQGQRGPP IILEATLHLA EIEDMPLFEP RVFTAGSEER VTCLPPKGLP EPSVWWEHAG 

       370        380        390        400        410        420 
VRLPTHGRVY QKGHELVLAN IAESDAGVYT CHAANLAGQR RQDVNITVAT VPSWLKKPQD 

       430        440        450        460        470        480 
SQLEEGKPGY LDCLTQATPK PTVVWYRNQM LISEDSRFEV FKNGTLRINS VEVYDGTWYR 

       490        500        510        520        530        540 
CMSSTPAGSI EAQARVQVLE KLKFTPPPQP QQCMEFDKEA TVPCSATGRE KPTIKWERAD 

       550        560        570        580        590        600 
GSSLPEWVTD NAGTLHFARV TRDDAGNYTC IASNGPQGQI RAHVQLTVAV FITFKVEPER 

       610        620        630        640        650        660 
TTVYQGHTAL LQCEAQGDPK PLIQWKGKDR ILDPTKLGPR MHIFQNGSLV IHDVAPEDSG 

       670        680        690        700        710        720 
RYTCIAGNSC NIKHTEAPLY VVDKPVPEES EGPGSPPPYK MIQTIGLSVG AAVAYIIAVL 

       730        740        750        760        770        780 
GLMFYCKKRC KAKRLQKQPE GEEPEMECLN GGPLQNGQPS AEIQEEVALT SLGSGPAATN 

       790        800        810        820        830        840 
KRHSTSDKMH FPRSSLQPIT TLGKSEFGEV FLAKAQGLEE GVAETLVLVK SLQSKDEQQQ 

       850        860        870        880        890        900 
LDFRRELEMF GKLNHANVVR LLGLCREAEP HYMVLEYVDL GDLKQFLRIS KSKDEKLKSQ 

       910        920        930        940        950        960 
PLSTKQKVAL CTQVALGMEH LSNNRFVHKD LAARNCLVSA QRQVKVSALG LSKDVYNSEY 

       970        980        990       1000       1010       1020 
YHFRQAWVPL RWMSPEAILE GDFSTKSDVW AFGVLMWEVF THGEMPHGGQ ADDEVLADLQ 

      1030       1040       1050       1060       1070 
AGKARLPQPE GCPSKLYRLM QRCWALSPKD RPSFSEIASA LGDSTVDSKP 

« Hide

Isoform 2 (PTK7-2) [UniParc].

Checksum: 34501D254ED02C49
Show »

FASTA1,030113,805
Isoform 3 (PTK7-3) [UniParc].

Checksum: 33FEE51123972DA8
Show »

FASTA940103,581
Isoform 4 (PTK7-4) [UniParc].

Checksum: BCAA8FEBBF9909B8
Show »

FASTA1,014112,261
Isoform 5 (PTK7-5) [UniParc].

Checksum: 20405B0B94CA99EB
Show »

FASTA81689,764
Isoform 6 [UniParc].

Checksum: E5F3E9970734EAF8
Show »

FASTA1,078119,197

References

« Hide 'large scale' references
[1]"Colon carcinoma kinase-4 defines a new subclass of the receptor tyrosine kinase family."
Mossie K., Jallal B., Alves F., Sures I., Plowman G.D., Ullrich A.
Oncogene 11:2179-2184(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon carcinoma and Placenta.
[2]"Characterization of the human full-length PTK7 cDNA encoding a receptor protein tyrosine kinase-like molecule closely related to chick KLG."
Park S.-K., Lee H.-S., Lee S.-T.
J. Biochem. 119:235-239(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fibroblast.
[3]"Organization of the human PTK7 gene encoding a receptor protein tyrosine kinase-like molecule and alternative splicing of its mRNA."
Jung J.-W., Ji A.-R., Lee J., Kim U.-J., Lee S.-T.
Biochim. Biophys. Acta 1579:153-163(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
Tissue: Testis.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 6).
Tissue: Testis and Tongue.
[5]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[8]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-646.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-646.
Tissue: Liver.
[10]"Soluble PTK7 inhibits tube formation, migration, and invasion of endothelial cells and angiogenesis."
Shin W.-S., Maeng Y.-S., Jung J.-W., Min J.-K., Kwon Y.-G., Lee S.-T.
Biochem. Biophys. Res. Commun. 371:793-798(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116; ASN-175; ASN-268 AND ASN-283.
Tissue: Leukemic T-cell.
[12]"The cell polarity PTK7 receptor acts as a modulator of the chemotherapeutic response in acute myeloid leukemia and impairs clinical outcome."
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.
Blood 116:2315-2323(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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."
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.
J. Biol. Chem. 285:35740-35749(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, CLEAVAGE, MUTAGENESIS OF LEU-622; MET-641 AND MET-701.
[14]"Silencing of PTK7 in colon cancer cells: caspase-10-dependent apoptosis via mitochondrial pathway."
Meng L., Sefah K., O'Donoghue M.B., Zhu G., Shangguan D., Noorali A., Chen Y., Zhou L., Tan W.
PLoS ONE 5:E14018-E14018(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Protein tyrosine kinase 7 has a conserved role in Wnt/beta-catenin canonical signalling."
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.
EMBO Rep. 12:43-49(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1, REGION.
[17]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-276; SER-410; ASP-745; GLN-766; VAL-777; ARG-783; VAL-933; THR-1029 AND GLN-1038.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33635 mRNA. Translation: AAA87565.1.
U40271 mRNA. Translation: AAC50484.2.
AF447176 expand/collapse EMBL AC list , AF447157, AF447158, AF447162, AF447164, AF447167, AF447170, AF447171, AF447173, AF447174, AF447175 Genomic DNA. Translation: AAL39062.1.
AF531868 mRNA. Translation: AAN04862.1.
AF531869 mRNA. Translation: AAN04863.1.
AF531870 mRNA. Translation: AAN04864.1.
AF531871 mRNA. Translation: AAN04865.1.
AF531872 mRNA. Translation: AAN04866.1.
AK291016 mRNA. Translation: BAF83705.1.
AK292589 mRNA. Translation: BAF85278.1.
AK296953 mRNA. Translation: BAH12463.1.
AL355385 Genomic DNA. Translation: CAI13783.1.
CH471081 Genomic DNA. Translation: EAX04154.1.
CH471081 Genomic DNA. Translation: EAX04155.1.
CH471081 Genomic DNA. Translation: EAX04156.1.
CH471081 Genomic DNA. Translation: EAX04158.1.
CH471081 Genomic DNA. Translation: EAX04160.1.
BC071557 mRNA. Translation: AAH71557.1.
CCDSCCDS4884.1. [Q13308-1]
CCDS4885.1. [Q13308-2]
CCDS4886.1. [Q13308-3]
CCDS4887.1. [Q13308-4]
CCDS59021.1. [Q13308-6]
PIRJC4593.
RefSeqNP_001257327.1. NM_001270398.1. [Q13308-6]
NP_002812.2. NM_002821.4. [Q13308-1]
NP_690619.1. NM_152880.3. [Q13308-2]
NP_690620.1. NM_152881.3. [Q13308-3]
NP_690621.1. NM_152882.3. [Q13308-4]
UniGeneHs.90572.

3D structure databases

ProteinModelPortalQ13308.
SMRQ13308. Positions 34-693, 759-1061.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111721. 2 interactions.
IntActQ13308. 3 interactions.
MINTMINT-4532536.

PTM databases

PhosphoSiteQ13308.

Polymorphism databases

DMDM116242736.

Proteomic databases

MaxQBQ13308.
PaxDbQ13308.
PRIDEQ13308.

Protocols and materials databases

DNASU5754.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230418; ENSP00000230418; ENSG00000112655. [Q13308-5]
ENST00000230419; ENSP00000230419; ENSG00000112655. [Q13308-1]
ENST00000345201; ENSP00000325992; ENSG00000112655. [Q13308-2]
ENST00000349241; ENSP00000325462; ENSG00000112655. [Q13308-3]
ENST00000352931; ENSP00000326029; ENSG00000112655. [Q13308-4]
ENST00000481273; ENSP00000418754; ENSG00000112655. [Q13308-6]
GeneID5754.
KEGGhsa:5754.
UCSCuc003oub.2. human. [Q13308-1]
uc003ouc.2. human. [Q13308-4]
uc003oud.2. human. [Q13308-2]
uc003oue.2. human. [Q13308-3]

Organism-specific databases

CTD5754.
GeneCardsGC06P043044.
HGNCHGNC:9618. PTK7.
HPAHPA003222.
MIM601890. gene.
neXtProtNX_Q13308.
PharmGKBPA33961.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG008320.
InParanoidQ13308.
KOK05127.
OMADGTWYRC.
OrthoDBEOG790G1M.
PhylomeDBQ13308.
TreeFamTF326835.

Gene expression databases

ArrayExpressQ13308.
BgeeQ13308.
CleanExHS_PTK7.
GenevestigatorQ13308.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07679. I-set. 6 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 7 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTK7. human.
GeneWikiPTK7.
GenomeRNAi5754.
NextBio22390.
PROQ13308.
SOURCESearch...

Entry information

Entry namePTK7_HUMAN
AccessionPrimary (citable) accession number: Q13308
Secondary accession number(s): A8K974 expand/collapse secondary AC list , B7Z477, E9PFZ5, Q13417, Q5T650, Q6IQ54, Q8NFA5, Q8NFA6, Q8NFA7, Q8NFA8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM