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Q13308

- PTK7_HUMAN

UniProt

Q13308 - PTK7_HUMAN

Protein

Inactive tyrosine-protein kinase 7

Gene

PTK7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei621 – 6222Cleavage; by MMP14

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. axis elongation Source: Ensembl
    3. canonical Wnt signaling pathway Source: UniProtKB
    4. cell adhesion Source: UniProtKB-KW
    5. cell migration Source: UniProtKB
    6. cellular response to retinoic acid Source: BHF-UCL
    7. cochlea morphogenesis Source: Ensembl
    8. convergent extension Source: Ensembl
    9. establishment of epithelial cell apical/basal polarity Source: Ensembl
    10. establishment of planar polarity Source: Ensembl
    11. lung-associated mesenchyme development Source: Ensembl
    12. neural tube closure Source: Ensembl
    13. peptidyl-tyrosine phosphorylation Source: GOC
    14. planar cell polarity pathway involved in neural tube closure Source: Ensembl
    15. positive regulation of neuron projection development Source: BHF-UCL
    16. signal transduction Source: ProtInc
    17. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Cell adhesion, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PTK7
    Synonyms:CCK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9618. PTK7.

    Subcellular locationi

    Membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junction 1 Publication
    Note: Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell junction, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi622 – 6221L → D: Prevents proteolysis by MMP14. 1 Publication
    Mutagenesisi641 – 6411M → R: No impact on proteolysis by MMP14. 1 Publication
    Mutagenesisi701 – 7011M → D: No impact on proteolysis by MMP14. 1 Publication

    Organism-specific databases

    PharmGKBiPA33961.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 10701040Inactive tyrosine-protein kinase 7PRO_0000016748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 101PROSITE-ProRule annotation
    Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication
    Disulfide bondi150 ↔ 200PROSITE-ProRule annotation
    Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi246 ↔ 301PROSITE-ProRule annotation
    Glycosylationi268 – 2681N-linked (GlcNAc...)1 Publication
    Glycosylationi283 – 2831N-linked (GlcNAc...)1 Publication
    Disulfide bondi343 ↔ 391PROSITE-ProRule annotation
    Glycosylationi405 – 4051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi433 ↔ 481PROSITE-ProRule annotation
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi524 ↔ 570PROSITE-ProRule annotation
    Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi613 ↔ 664PROSITE-ProRule annotation
    Glycosylationi646 – 6461N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13308.
    PaxDbiQ13308.
    PRIDEiQ13308.

    PTM databases

    PhosphoSiteiQ13308.

    Expressioni

    Tissue specificityi

    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.

    Inductioni

    Higher expression in cell lines established from normal non-tumorigenic tissues compared to cell lines established from highly metastatic invasive carcinomas (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ13308.
    BgeeiQ13308.
    CleanExiHS_PTK7.
    GenevestigatoriQ13308.

    Organism-specific databases

    HPAiHPA003222.

    Interactioni

    Subunit structurei

    Interacts with CTNNB1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352225EBI-2803245,EBI-491549

    Protein-protein interaction databases

    BioGridi111721. 2 interactions.
    IntActiQ13308. 3 interactions.
    MINTiMINT-4532536.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13308.
    SMRiQ13308. Positions 34-693, 759-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 704674ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini726 – 1070345CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei705 – 72521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 12090Ig-like C2-type 1Add
    BLAST
    Domaini128 – 21891Ig-like C2-type 2Add
    BLAST
    Domaini225 – 31793Ig-like C2-type 3Add
    BLAST
    Domaini309 – 40799Ig-like C2-type 4Add
    BLAST
    Domaini412 – 49786Ig-like C2-type 5Add
    BLAST
    Domaini503 – 58684Ig-like C2-type 6Add
    BLAST
    Domaini578 – 680103Ig-like C2-type 7Add
    BLAST
    Domaini796 – 1066271Protein kinase; inactivePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni794 – 1070277Interaction with CTNNB1Add
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG008320.
    InParanoidiQ13308.
    KOiK05127.
    OMAiDGTWYRC.
    OrthoDBiEOG790G1M.
    PhylomeDBiQ13308.
    TreeFamiTF326835.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    InterProiIPR007110. 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]
    PfamiPF07679. I-set. 6 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50835. IG_LIKE. 7 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13308-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGAARGSPAR PRRLPLLSVL LLPLLGGTQT AIVFIKQPSS QDALQGRRAL     50
    LRCEVEAPGP VHVYWLLDGA PVQDTERRFA QGSSLSFAAV DRLQDSGTFQ 100
    CVARDDVTGE EARSANASFN IKWIEAGPVV LKHPASEAEI QPQTQVTLRC 150
    HIDGHPRPTY QWFRDGTPLS DGQSNHTVSS KERNLTLRPA GPEHSGLYSC 200
    CAHSAFGQAC SSQNFTLSIA DESFARVVLA PQDVVVARYE EAMFHCQFSA 250
    QPPPSLQWLF EDETPITNRS RPPHLRRATV FANGSLLLTQ VRPRNAGIYR 300
    CIGQGQRGPP IILEATLHLA EIEDMPLFEP RVFTAGSEER VTCLPPKGLP 350
    EPSVWWEHAG VRLPTHGRVY QKGHELVLAN IAESDAGVYT CHAANLAGQR 400
    RQDVNITVAT VPSWLKKPQD SQLEEGKPGY LDCLTQATPK PTVVWYRNQM 450
    LISEDSRFEV FKNGTLRINS VEVYDGTWYR CMSSTPAGSI EAQARVQVLE 500
    KLKFTPPPQP QQCMEFDKEA TVPCSATGRE KPTIKWERAD GSSLPEWVTD 550
    NAGTLHFARV TRDDAGNYTC IASNGPQGQI RAHVQLTVAV FITFKVEPER 600
    TTVYQGHTAL LQCEAQGDPK PLIQWKGKDR ILDPTKLGPR MHIFQNGSLV 650
    IHDVAPEDSG RYTCIAGNSC NIKHTEAPLY VVDKPVPEES EGPGSPPPYK 700
    MIQTIGLSVG AAVAYIIAVL GLMFYCKKRC KAKRLQKQPE GEEPEMECLN 750
    GGPLQNGQPS AEIQEEVALT SLGSGPAATN KRHSTSDKMH FPRSSLQPIT 800
    TLGKSEFGEV FLAKAQGLEE GVAETLVLVK SLQSKDEQQQ LDFRRELEMF 850
    GKLNHANVVR LLGLCREAEP HYMVLEYVDL GDLKQFLRIS KSKDEKLKSQ 900
    PLSTKQKVAL CTQVALGMEH LSNNRFVHKD LAARNCLVSA QRQVKVSALG 950
    LSKDVYNSEY YHFRQAWVPL RWMSPEAILE GDFSTKSDVW AFGVLMWEVF 1000
    THGEMPHGGQ ADDEVLADLQ AGKARLPQPE GCPSKLYRLM QRCWALSPKD 1050
    RPSFSEIASA LGDSTVDSKP 1070
    Length:1,070
    Mass (Da):118,392
    Last modified:October 17, 2006 - v2
    Checksum:i304926A1774EB5F4
    GO
    Isoform 2 (identifier: Q13308-2) [UniParc]FASTAAdd to Basket

    Also known as: PTK7-2

    The sequence of this isoform differs from the canonical sequence as follows:
         500-539: Missing.

    Show »
    Length:1,030
    Mass (Da):113,805
    Checksum:i34501D254ED02C49
    GO
    Isoform 3 (identifier: Q13308-3) [UniParc]FASTAAdd to Basket

    Also known as: PTK7-3

    The sequence of this isoform differs from the canonical sequence as follows:
         410-540: TVPSWLKKPQ...KPTIKWERAD → N

    Show »
    Length:940
    Mass (Da):103,581
    Checksum:i33FEE51123972DA8
    GO
    Isoform 4 (identifier: Q13308-4) [UniParc]FASTAAdd to Basket

    Also known as: PTK7-4

    The sequence of this isoform differs from the canonical sequence as follows:
         627-682: Missing.

    Show »
    Length:1,014
    Mass (Da):112,261
    Checksum:iBCAA8FEBBF9909B8
    GO
    Isoform 5 (identifier: Q13308-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:816
    Mass (Da):89,764
    Checksum:i20405B0B94CA99EB
    GO
    Isoform 6 (identifier: Q13308-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MGAARGSPARPRRLPLLSVLLLPLLG → MGSFLSGEKRPSAPTVGSAMEKKEFPTPPGRVGP

    Note: No experimental confirmation available.

    Show »
    Length:1,078
    Mass (Da):119,197
    Checksum:iE5F3E9970734EAF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871F → L in BAF85278. (PubMed:14702039)Curated
    Sequence conflicti92 – 921R → P in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti93 – 931L → P in AAH71557. (PubMed:15489334)Curated
    Sequence conflicti147 – 1471T → K in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti207 – 2071G → S in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti495 – 4962RV → VL in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti515 – 5151E → G in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti755 – 7551Q → R in BAH12463. (PubMed:14702039)Curated
    Sequence conflicti799 – 7991I → F in BAF85278. (PubMed:14702039)Curated
    Sequence conflicti881 – 8811G → E in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti969 – 9691P → A in AAA87565. (PubMed:7478540)Curated
    Sequence conflicti992 – 9921F → S in AAA87565. (PubMed:7478540)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti276 – 2761R → H.1 Publication
    Corresponds to variant rs56188167 [ dbSNP | Ensembl ].
    VAR_041502
    Natural varianti410 – 4101T → S.1 Publication
    Corresponds to variant rs34021075 [ dbSNP | Ensembl ].
    VAR_041503
    Natural varianti745 – 7451E → D.1 Publication
    Corresponds to variant rs9472017 [ dbSNP | Ensembl ].
    VAR_041504
    Natural varianti766 – 7661E → Q.1 Publication
    Corresponds to variant rs56216742 [ dbSNP | Ensembl ].
    VAR_041505
    Natural varianti777 – 7771A → V.1 Publication
    Corresponds to variant rs34764696 [ dbSNP | Ensembl ].
    VAR_041506
    Natural varianti783 – 7831H → R.1 Publication
    Corresponds to variant rs55820547 [ dbSNP | Ensembl ].
    VAR_041507
    Natural varianti933 – 9331A → V in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041508
    Natural varianti1029 – 10291P → T.1 Publication
    Corresponds to variant rs55755163 [ dbSNP | Ensembl ].
    VAR_041509
    Natural varianti1038 – 10381R → Q.1 Publication
    Corresponds to variant rs34865794 [ dbSNP | Ensembl ].
    VAR_041510

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MGAAR…LPLLG → MGSFLSGEKRPSAPTVGSAM EKKEFPTPPGRVGP in isoform 6. 1 PublicationVSP_044775Add
    BLAST
    Alternative sequencei410 – 540131TVPSW…WERAD → N in isoform 3. 1 PublicationVSP_037181Add
    BLAST
    Alternative sequencei500 – 53940Missing in isoform 2. 2 PublicationsVSP_037182Add
    BLAST
    Alternative sequencei627 – 68256Missing in isoform 4. 1 PublicationVSP_037183Add
    BLAST
    Alternative sequencei804 – 81613KSEFG…LAKAQ → RPQAVPEDFQEQG in isoform 5. 1 PublicationVSP_037184Add
    BLAST
    Alternative sequencei817 – 1070254Missing in isoform 5. 1 PublicationVSP_037185Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33635 mRNA. Translation: AAA87565.1.
    U40271 mRNA. Translation: AAC50484.2.
    AF447176
    , 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.
    CCDSiCCDS4884.1. [Q13308-1]
    CCDS4885.1. [Q13308-2]
    CCDS4886.1. [Q13308-3]
    CCDS4887.1. [Q13308-4]
    CCDS59021.1. [Q13308-6]
    PIRiJC4593.
    RefSeqiNP_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]
    UniGeneiHs.90572.

    Genome annotation databases

    EnsembliENST00000230418; 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]
    GeneIDi5754.
    KEGGihsa:5754.
    UCSCiuc003oub.2. human. [Q13308-1]
    uc003ouc.2. human. [Q13308-4]
    uc003oud.2. human. [Q13308-2]
    uc003oue.2. human. [Q13308-3]

    Polymorphism databases

    DMDMi116242736.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33635 mRNA. Translation: AAA87565.1 .
    U40271 mRNA. Translation: AAC50484.2 .
    AF447176
    , 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 .
    CCDSi CCDS4884.1. [Q13308-1 ]
    CCDS4885.1. [Q13308-2 ]
    CCDS4886.1. [Q13308-3 ]
    CCDS4887.1. [Q13308-4 ]
    CCDS59021.1. [Q13308-6 ]
    PIRi JC4593.
    RefSeqi NP_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 ]
    UniGenei Hs.90572.

    3D structure databases

    ProteinModelPortali Q13308.
    SMRi Q13308. Positions 34-693, 759-1061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111721. 2 interactions.
    IntActi Q13308. 3 interactions.
    MINTi MINT-4532536.

    PTM databases

    PhosphoSitei Q13308.

    Polymorphism databases

    DMDMi 116242736.

    Proteomic databases

    MaxQBi Q13308.
    PaxDbi Q13308.
    PRIDEi Q13308.

    Protocols and materials databases

    DNASUi 5754.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230418 ; 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 ]
    GeneIDi 5754.
    KEGGi hsa:5754.
    UCSCi uc003oub.2. human. [Q13308-1 ]
    uc003ouc.2. human. [Q13308-4 ]
    uc003oud.2. human. [Q13308-2 ]
    uc003oue.2. human. [Q13308-3 ]

    Organism-specific databases

    CTDi 5754.
    GeneCardsi GC06P043044.
    HGNCi HGNC:9618. PTK7.
    HPAi HPA003222.
    MIMi 601890. gene.
    neXtProti NX_Q13308.
    PharmGKBi PA33961.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG008320.
    InParanoidi Q13308.
    KOi K05127.
    OMAi DGTWYRC.
    OrthoDBi EOG790G1M.
    PhylomeDBi Q13308.
    TreeFami TF326835.

    Miscellaneous databases

    ChiTaRSi PTK7. human.
    GeneWikii PTK7.
    GenomeRNAii 5754.
    NextBioi 22390.
    PROi Q13308.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13308.
    Bgeei Q13308.
    CleanExi HS_PTK7.
    Genevestigatori Q13308.

    Family and domain databases

    Gene3Di 2.60.40.10. 7 hits.
    InterProi IPR007110. 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 ]
    Pfami PF07679. I-set. 6 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50835. IG_LIKE. 7 hits.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. 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.
      , 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.

    Entry informationi

    Entry nameiPTK7_HUMAN
    AccessioniPrimary (citable) accession number: Q13308
    Secondary accession number(s): A8K974
    , B7Z477, E9PFZ5, Q13417, Q5T650, Q6IQ54, Q8NFA5, Q8NFA6, Q8NFA7, Q8NFA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3