Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00595
Entry Name
UniProt Accession
Theoretical PI
6.67
Molecular Weight
118391.64
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Inactive tyrosine-protein kinase 7
Protein Synonyms/Alias
Colon carcinoma kinase 4; CCK-4; Protein-tyrosine kinase 7; Pseudo tyrosine kinase receptor 7; Tyrosine-protein kinase-like 7;
Gene Name
PTK7
Gene Synonyms/Alias
CCK4;
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
201
Canonical
HSGLYSCCAHSAFGQ
[1]
S-Palmitoylation
726
Canonical
VLGLMFYCKKRCKAK
[1]
S-Palmitoylation
730
Canonical
MFYCKKRCKAKRLQK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Topological domain: 31 704 Extracellular.
Transmembrane: 705 725 Helical.
Topological domain: 726 1070 Cytoplasmic.
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.
Region: 794 1070 Interaction with CTNNB1.
Functional site: 621 622 Cleavage; by MMP14.
Protein Length
1070 AA.
Protein Sequence
(Canonical)
MGAARGSPAR PRRLPLLSVL LLPLLGGTQT AIVFIKQPSS QDALQGRRAL LRCEVEAPGP  60
VHVYWLLDGA PVQDTERRFA QGSSLSFAAV DRLQDSGTFQ CVARDDVTGE EARSANASFN  120
IKWIEAGPVV LKHPASEAEI QPQTQVTLRC HIDGHPRPTY QWFRDGTPLS DGQSNHTVSS  180
KERNLTLRPA GPEHSGLYSC CAHSAFGQAC SSQNFTLSIA DESFARVVLA PQDVVVARYE  240
EAMFHCQFSA QPPPSLQWLF EDETPITNRS RPPHLRRATV FANGSLLLTQ VRPRNAGIYR  300
CIGQGQRGPP IILEATLHLA EIEDMPLFEP RVFTAGSEER VTCLPPKGLP EPSVWWEHAG  360
VRLPTHGRVY QKGHELVLAN IAESDAGVYT CHAANLAGQR RQDVNITVAT VPSWLKKPQD  420
SQLEEGKPGY LDCLTQATPK PTVVWYRNQM LISEDSRFEV FKNGTLRINS VEVYDGTWYR  480
CMSSTPAGSI EAQARVQVLE KLKFTPPPQP QQCMEFDKEA TVPCSATGRE KPTIKWERAD  540
GSSLPEWVTD NAGTLHFARV TRDDAGNYTC IASNGPQGQI RAHVQLTVAV FITFKVEPER  600
TTVYQGHTAL LQCEAQGDPK PLIQWKGKDR ILDPTKLGPR MHIFQNGSLV IHDVAPEDSG  660
RYTCIAGNSC NIKHTEAPLY VVDKPVPEES EGPGSPPPYK MIQTIGLSVG AAVAYIIAVL  720
GLMFYCKKRC KAKRLQKQPE GEEPEMECLN GGPLQNGQPS AEIQEEVALT SLGSGPAATN  780
KRHSTSDKMH FPRSSLQPIT TLGKSEFGEV FLAKAQGLEE GVAETLVLVK SLQSKDEQQQ  840
LDFRRELEMF GKLNHANVVR LLGLCREAEP HYMVLEYVDL GDLKQFLRIS KSKDEKLKSQ  900
PLSTKQKVAL CTQVALGMEH LSNNRFVHKD LAARNCLVSA QRQVKVSALG LSKDVYNSEY  960
YHFRQAWVPL RWMSPEAILE GDFSTKSDVW AFGVLMWEVF THGEMPHGGQ ADDEVLADLQ  1020
AGKARLPQPE GCPSKLYRLM QRCWALSPKD RPSFSEIASA LGDSTVDSKP             1070
FASTA
(Canonical)
>LipidDB-9606-00595|Q13308
MGAARGSPARPRRLPLLSVLLLPLLGGTQTAIVFIKQPSSQDALQGRRALLRCEVEAPGP
VHVYWLLDGAPVQDTERRFAQGSSLSFAAVDRLQDSGTFQCVARDDVTGEEARSANASFN
IKWIEAGPVVLKHPASEAEIQPQTQVTLRCHIDGHPRPTYQWFRDGTPLSDGQSNHTVSS
KERNLTLRPAGPEHSGLYSCCAHSAFGQACSSQNFTLSIADESFARVVLAPQDVVVARYE
EAMFHCQFSAQPPPSLQWLFEDETPITNRSRPPHLRRATVFANGSLLLTQVRPRNAGIYR
CIGQGQRGPPIILEATLHLAEIEDMPLFEPRVFTAGSEERVTCLPPKGLPEPSVWWEHAG
VRLPTHGRVYQKGHELVLANIAESDAGVYTCHAANLAGQRRQDVNITVATVPSWLKKPQD
SQLEEGKPGYLDCLTQATPKPTVVWYRNQMLISEDSRFEVFKNGTLRINSVEVYDGTWYR
CMSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKPTIKWERAD
GSSLPEWVTDNAGTLHFARVTRDDAGNYTCIASNGPQGQIRAHVQLTVAVFITFKVEPER
TTVYQGHTALLQCEAQGDPKPLIQWKGKDRILDPTKLGPRMHIFQNGSLVIHDVAPEDSG
RYTCIAGNSCNIKHTEAPLYVVDKPVPEESEGPGSPPPYKMIQTIGLSVGAAVAYIIAVL
GLMFYCKKRCKAKRLQKQPEGEEPEMECLNGGPLQNGQPSAEIQEEVALTSLGSGPAATN
KRHSTSDKMHFPRSSLQPITTLGKSEFGEVFLAKAQGLEEGVAETLVLVKSLQSKDEQQQ
LDFRRELEMFGKLNHANVVRLLGLCREAEPHYMVLEYVDLGDLKQFLRISKSKDEKLKSQ
PLSTKQKVALCTQVALGMEHLSNNRFVHKDLAARNCLVSAQRQVKVSALGLSKDVYNSEY
YHFRQAWVPLRWMSPEAILEGDFSTKSDVWAFGVLMWEVFTHGEMPHGGQADDEVLADLQ
AGKARLPQPEGCPSKLYRLMQRCWALSPKDRPSFSEIASALGDSTVDSKP
Gene Ontology
GO:0005911; C:cell-cell junction; IDA:UniProtKB
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005524; F:ATP binding; IEA:InterPro
GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc
GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB
GO:0003401; P:axis elongation; IEA:Ensembl
GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB
GO:0007155; P:cell adhesion; IEA:UniProtKB-KW
GO:0016477; P:cell migration; IMP:UniProtKB
GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL
GO:0090103; P:cochlea morphogenesis; IEA:Ensembl
GO:0060026; P:convergent extension; IEA:Ensembl
GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl
GO:0001736; P:establishment of planar polarity; IEA:Ensembl
GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl
GO:0001843; P:neural tube closure; IEA:Ensembl
GO:0018108; P:peptidyl-tyrosine phosphorylation; TAS:GOC
GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl
GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0042060; P:wound healing; IEA:Ensembl
Interpro
InterPro; IPR007110; Ig-like_dom
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
Pfam
Pfam; PF07679; I-set;
Pfam; PF07714; Pkinase_Tyr;
SMART
SMART; SM00409; IG;
SMART; SM00408; IGc2;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS50835; IG_LIKE;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PRINTS
PRINTS; PR00109; TYRKINASE;