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UniProtKB/Swiss-Prot entry Q02763


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TIE2_HUMAN
Primary accession number Q02763
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 101)
Name and origin of the protein
Protein name Angiopoietin-1 receptor [Precursor]
Synonyms EC 2.7.10.1
Tyrosine-protein kinase receptor TIE-2
hTIE2
Tyrosine-protein kinase receptor TEK
Tunica interna endothelial cell kinase
p140 TEK
CD202b antigen
Gene name
Name: TEK
Synonyms: TIE2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8382358 [NCBI, ExPASy, EBI, Israel, Japan]
Ziegler S.F., Bird T.A., Schneringer J.A., Schooley K.A., Baum P.R.;
"Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta.";
Oncogene 8:663-670(1993).
[2]
PROTEIN SEQUENCE OF 23-37.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[3]
VARIANT VMCM TRP-849.
DOI=10.1016/S0092-8674(00)81814-0; PubMed=8980225 [NCBI, ExPASy, EBI, Israel, Japan]
Vikkula M., Boon L.M., Carraway K.L. III, Calvert J.T., Diamonti A.J., Goumnerov B., Pasyk K.A., Marchuk D.A., Warman M.L., Cantley L.C., Mulliken J.B., Olse B.R.;
"Vascular dysmorphogenesis caused by an activating mutation in the receptor tyrosine kinase TIE2.";
Cell 87:1181-1190(1996).
[4]
VARIANTS VMCM TRP-849 AND SER-897.
DOI=10.1093/hmg/8.7.1279; PubMed=10369874 [NCBI, ExPASy, EBI, Israel, Japan]
Calvert J.T., Riney T.J., Kontos C.D., Cha E.H., Prieto V.G., Shea C.R., Berg J.N., Nevin N.C., Simpson S.A., Pasyk K.A., Speer M.C., Peters K.G., Marchuk D.A.;
"Allelic and locus heterogeneity in inherited venous malformations.";
Hum. Mol. Genet. 8:1279-1289(1999).
[5]
VARIANT [LARGE SCALE ANALYSIS] ASN-117.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[6]
VARIANTS [LARGE SCALE ANALYSIS] ASN-117; THR-148; VAL-226; ILE-486; LEU-600; PHE-634; ILE-676; THR-724; ALA-883 AND VAL-1124.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L06139; AAA61139.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I58388; I58388.
UniGene Hs.89640
3D structure databases
PDB
1FVR; X-ray; 2.20 A; A/B=808-1124.[ExPASy / RCSB / EBI]
2GY5; X-ray; 2.90 A; A=23-445.[ExPASy / RCSB / EBI]
2GY7; X-ray; 3.70 A; B=23-445.[ExPASy / RCSB / EBI]
2OO8; X-ray; 2.20 A; X=808-1124.[ExPASy / RCSB / EBI]
2OSC; X-ray; 2.80 A; A=808-1124.[ExPASy / RCSB / EBI]
2P4I; X-ray; 2.50 A; A/B=808-1124.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FVR; -.
2GY5; -.
2GY7; -.
2OO8; -.
2OSC; -.
2P4I; -.
ModBase Q02763.
Protein-protein interaction databases
DIP DIP:6047N; -.
PTM databases
PhosphoSite Q02763; -.
Organism-specific databases
H-InvDB HIX0025697; -.
HGNC HGNC:11724; TEK.
GenAtlas TEK.
HPA CAB010359; -.
HPA011738; -.
MIM 600195; phenotype. [NCBI / EBI]
600221; gene. [NCBI / EBI]
Orphanet 2451; Mucocutaneous venous malformations.
PharmGKB PA36441; -.
GeneCards Q02763.
Gene expression databases
ArrayExpress Q02763; -.
CleanEx HS_TEK; -.
GermOnline ENSG00000120156; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004714; Molecular function: transmembrane receptor protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007169; Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006210; EGF.
IPR000742; EGF_3.
IPR013111; EGF_extracell.
IPR013032; EGF_like_reg_CS.
IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR015781; TieRTK.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:2.60.40.10; Ig-like_fold; 1.
PANTHER PTHR23256:SF90; TieRTK; 1.
Pfam PF07974; EGF_2; 2.
PF00041; fn3; 3.
PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.
PRINTS PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00181; EGF; 2.
SM00060; FN3; 3.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; 3.
PS01186; EGF_2; 3.
PS50026; EGF_3; 1.
PS50853; FN3; 3.
PS50835; IG_LIKE; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q02763.
Genome annotation databases
Ensembl ENSG00000120156; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN Q02763; -.
Other
SOURCE TEK; Homo sapiens.
ProtoNet Q02763.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Direct protein sequencing; Disease mutation; EGF-like domain; Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     22  22      
CHAIN   23   1124  1102     Angiopoietin-1 receptor. PRO_0000024474
TOPO_DOM   23    745  723     Extracellular (Potential). 
TRANSMEM   746    770  25     Potential. 
TOPO_DOM   771   1124  354     Cytoplasmic (Potential). 
DOMAIN   44    123  80     Ig-like C2-type 1. 
DOMAIN   210    252  43     EGF-like 1. 
DOMAIN   254    299  46     EGF-like 2. 
DOMAIN   301    341  41     EGF-like 3. 
DOMAIN   350    440  91     Ig-like C2-type 2. 
DOMAIN   445    537  93     Fibronectin type-III 1. 
DOMAIN   544    633  90     Fibronectin type-III 2. 
DOMAIN   639    730  92     Fibronectin type-III 3. 
DOMAIN   824   1096  273     Protein kinase. 
NP_BIND   830    838  9     ATP (By similarity). 
ACT_SITE   964    964        Proton acceptor (By similarity). 
BINDING   855    855        ATP (By similarity). 
MOD_RES   992    992        Phosphotyrosine; by autocatalysis. 
CARBOHYD   140    140        N-linked (GlcNAc...) (Potential). 
CARBOHYD   158    158        N-linked (GlcNAc...) (Potential). 
CARBOHYD   399    399        N-linked (GlcNAc...) (Potential). 
CARBOHYD   438    438        N-linked (GlcNAc...) (Potential). 
CARBOHYD   464    464        N-linked (GlcNAc...) (Potential). 
CARBOHYD   560    560        N-linked (GlcNAc...) (Potential). 
CARBOHYD   596    596        N-linked (GlcNAc...) (Potential). 
CARBOHYD   649    649        N-linked (GlcNAc...) (Potential). 
CARBOHYD   691    691        N-linked (GlcNAc...) (Potential). 
DISULFID   220    233        By similarity. 
DISULFID   227    240        By similarity. 
DISULFID   242    251        By similarity. 
VARIANT   117    117  1     K -> N (in breast cancer samples; infiltrating ductal carcinoma; somatic mutation). VAR_035714 
VARIANT   148    148  1     I -> T. VAR_041855 
VARIANT   226    226  1     A -> V. VAR_041856 
VARIANT   486    486  1     V -> I (in dbSNP:rs1334811 [NCBI]). VAR_024578 
VARIANT   600    600  1     V -> L. VAR_041857 
VARIANT   634    634  1     L -> F. VAR_041858 
VARIANT   676    676  1     V -> I. VAR_041859 
VARIANT   724    724  1     A -> T. VAR_041860 
VARIANT   849    849  1     R -> W (in VMCM; activating effect). VAR_006352 
VARIANT   883    883  1     P -> A (in an ovarian serous carcinoma sample; somatic mutation). VAR_041861 
VARIANT   897    897  1     Y -> S (in VMCM; activating effect). VAR_008716 
VARIANT   1124   1124  1     A -> V (in a renal clear cell carcinoma sample; somatic mutation). VAR_041862 
STRAND   26     29  4      
STRAND   33     35  3      
STRAND   40     46  7      
STRAND   56     59  4      
TURN   61     63  3      
STRAND   64     66  3      
STRAND   74     76  3      
STRAND   80     88  9      
STRAND   98    106  9      
STRAND   109    119  11      
STRAND   123    125  3      
STRAND   127    133  7      
STRAND   139    145  7      
STRAND   153    157  5      
STRAND   160    165  6      
HELIX   167    169  3      
STRAND   172    178  7      
HELIX   183    185  3      
STRAND   187    193  7      
HELIX   198    200  3      
STRAND   202    208  7      
STRAND   215    217  3      
TURN   235    237  3      
STRAND   246    248  3      
STRAND   259    261  3      
TURN   271    276  6      
STRAND   279    281  3      
TURN   282    285  4      
STRAND   286    288  3      
HELIX   296    298  3      
STRAND   322    324  3      
TURN   325    327  3      
STRAND   328    330  3      
STRAND   361    366  6      
STRAND   369    373  5      
HELIX   380    382  3      
STRAND   383    386  4      
STRAND   396    400  5      
STRAND   405    408  4      
STRAND   411    414  4      
HELIX   416    418  3      
STRAND   420    428  9      
STRAND   431    439  9      
STRAND   816    818  3      
HELIX   821    823  3      
STRAND   825    831  7      
HELIX   833    835  3      
STRAND   837    845  9      
STRAND   848    858  11      
HELIX   868    876  9      
STRAND   888    894  7      
STRAND   897    902  6      
HELIX   910    915  6      
HELIX   919    922  4      
HELIX   924    929  6      
HELIX   938    957  20      
HELIX   967    969  3      
STRAND   970    972  3      
HELIX   974    976  3  &nb