Reviewed, UniProtKB/Swiss-Prot Q02763 (TIE2_HUMAN)

Names and origin

Protein names

Recommended name:
    Angiopoietin-1 receptor
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor TIE-2
      Short name=hTIE2
    Tyrosine-protein kinase receptor TEK
    Tunica interna endothelial cell kinase
    p140 TEK
    CD_antigen=CD202b

Gene names

Name:	TEK
Synonyms:	TIE2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1124 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This protein is a protein tyrosine-kinase transmembrane receptor for angiopoietin 1. It may constitute the earliest mammalian endothelial cell lineage marker. Probably regulates endothelial cell proliferation, differentiation and guides the proper patterning of endothelial cells during blood vessel formation.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with PTPRB. Ref.7
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Predominantly expressed in endothelial cells and their progenitors, the angioblasts. Has been directly found in placenta and lung, with a lower level in umbilical vein endothelial cells, brain and kidney.
Post-translational modification	Phosphorylated. Phosphorylation is induced by ANGPT1 and ANGPT2. ANGPT1-induced phosphorylation is impaired during hypoxia. Dephosphorylated by PTPRB. Ref.6
Involvement in disease	Defects in TEK are a cause of dominantly inherited venous malformations (VMCM) [MIM:600195]; an error of vascular morphogenesis characterized by dilated, serpiginous channels. Ref.9 Ref.10
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily. Contains 3 EGF-like domains. Contains 3 fibronectin type-III domains. Contains 2 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Immunoglobulin domain Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-cell signaling Ref.9 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of cell proliferation Inferred from electronic annotation. Source: InterPro transmembrane receptor protein tyrosine kinase signaling pathway Ref.9 Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.7 Inferred from physical interaction. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPN12	Q05209	1	EBI-2257090,EBI-2266035
PTPRB	P23467	1	EBI-2257090,EBI-1265766
PTPRC	P08575	1	EBI-2257090,EBI-1341
PTPRG	P23470	1	EBI-2257090,EBI-2258115
PTPRJ	Q12913	1	EBI-2257090,EBI-2264500
PTPRK	Q15262	1	EBI-2257090,EBI-474052
PTPRO	Q16827	1	EBI-2257090,EBI-723739

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.5

Chain

23 – 1124

1102

Angiopoietin-1 receptor

PRO_0000024474

Regions

Topological domain

23 – 745

723

Extracellular Potential

Transmembrane

746 – 770

25

Potential

Topological domain

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

Nucleotide binding

830 – 838

9

ATP By similarity

Sites

Active site

964

1

Proton acceptor By similarity

Binding site

855

1

ATP By similarity

Amino acid modifications

Modified residue

992

1

Phosphotyrosine; by autocatalysis

Glycosylation

140

1

N-linked (GlcNAc...) Potential

Glycosylation

158

1

N-linked (GlcNAc...) Potential

Glycosylation

399

1

N-linked (GlcNAc...) Potential

Glycosylation

438

1

N-linked (GlcNAc...) Potential

Glycosylation

464

1

N-linked (GlcNAc...) Potential

Glycosylation

560

1

N-linked (GlcNAc...) Potential

Glycosylation

596

1

N-linked (GlcNAc...) Ref.8

Glycosylation

649

1

N-linked (GlcNAc...) Potential

Glycosylation

691

1

N-linked (GlcNAc...) Potential

Disulfide bond

220 ↔ 233

By similarity

Disulfide bond

227 ↔ 240

By similarity

Disulfide bond

242 ↔ 251

By similarity

Natural variations

Natural variant

117

1

K → N in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.11 Ref.12

VAR_035714

Natural variant

148

1

I → T: dbSNP rs35969327. Ref.12

VAR_041855

Natural variant

226

1

A → V: dbSNP rs35814893. Ref.12

VAR_041856

Natural variant

346

1

Q → P: dbSNP rs682632. Ref.1 Ref.2 Ref.4

VAR_048002

Natural variant

391

1

T → I: dbSNP rs34032300.

VAR_048003

Natural variant

486

1

V → I: dbSNP rs1334811. Ref.12

VAR_024578

Natural variant

600

1

V → L: dbSNP rs35030851. Ref.12

VAR_041857

Natural variant

634

1

L → F: dbSNP rs35378598. Ref.12

VAR_041858

Natural variant

676

1

V → I: dbSNP rs56367117. Ref.12

VAR_041859

Natural variant

724

1

A → T: dbSNP rs4631561. Ref.12

VAR_041860

Natural variant

849

1

R → W in VMCM; activating effect. Ref.9 Ref.10

VAR_006352

Natural variant

883

1

P → A in an ovarian serous carcinoma sample; somatic mutation. Ref.12

VAR_041861

Natural variant

897

1

Y → S in VMCM; activating effect. Ref.10

VAR_008716

Natural variant

1124

1

A → V in a renal clear cell carcinoma sample; somatic mutation. Ref.12

VAR_041862

Experimental info

Sequence conflict

695

1

T → I in AAA61139. Ref.1

Secondary structure

1

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1124

Helix Strand Turn

Details...

Beta strand

26 – 29

4

Beta strand

33 – 35

3

Beta strand

40 – 46

7

Beta strand

56 – 59

4

Turn

61 – 63

3

Beta strand

64 – 66

3

Beta strand

74 – 76

3

Beta strand

80 – 88

9

Beta strand

98 – 106

9

Beta strand

109 – 119

11

Beta strand

123 – 125

3

Beta strand

127 – 133

7

Beta strand

139 – 145

7

Beta strand

153 – 157

5

Beta strand

160 – 165

6

Helix

167 – 169

3

Beta strand

172 – 178

7

Helix

183 – 185

3

Beta strand

187 – 193

7

Helix

198 – 200

3

Beta strand

202 – 208

7

Beta strand

215 – 217

3

Turn

235 – 237

3

Beta strand

246 – 248

3

Beta strand

259 – 261

3

Turn

271 – 276

6

Beta strand

279 – 281

3

Turn

282 – 285

4

Beta strand

286 – 288

3

Helix

296 – 298

3

Beta strand

322 – 324

3

Turn

325 – 327

3

Beta strand

328 – 330

3

Beta strand

361 – 366

6

Beta strand

369 – 373

5

Helix

380 – 382

3

Beta strand

383 – 386

4

Beta strand

396 – 400

5

Beta strand

405 – 408

4

Beta strand

411 – 414

4

Helix

416 – 418

3

Beta strand

420 – 428

9

Beta strand

431 – 439

9

Beta strand

816 – 818

3

Helix

821 – 823

3

Beta strand

825 – 831

7

Helix

833 – 835

3

Beta strand

837 – 845

9

Beta strand

848 – 858

11

Helix

868 – 876

9

Beta strand

888 – 894

7

Beta strand

897 – 902

6

Helix

910 – 915

6

Helix

919 – 922

4

Helix

924 – 929

6

Helix

938 – 957

20

Helix

967 – 969

3

Beta strand

970 – 972

3

Helix

974 – 976

3

Beta strand

978 – 980

3

Beta strand

986 – 989

4

Turn

1002 – 1004

3

Helix

1007 – 1012

6

Helix

1017 – 1032

16

Turn

1038 – 1041

4

Helix

1044 – 1050

7

Helix

1051 – 1053

3

Helix

1065 – 1074

10

Helix

1079 – 1081

3

Helix

1085 – 1097

13

Beta strand

1098 – 1100

3

Helix

1118 – 1120

3

Sequences

	Sequence		Length	Mass (Da)
	Q02763-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: E739DEC3E4FEB124	FASTA	1,124	125,830
	10 20 30 40 50 60 MDSLASLVLC GVSLLLSGTV EGAMDLILIN SLPLVSDAET SLTCIASGWR PHEPITIGRD 70 80 90 100 110 120 FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY FCEGRVRGEA IRIRTMKMRQ 130 140 150 160 170 180 QASFLPATLT MTVDKGDNVN ISFKKVLIKE EDAVIYKNGS FIHSVPRHEV PDILEVHLPH 190 200 210 220 230 240 AQPQDAGVYS ARYIGGNLFT SAFTRLIVRR CEAQKWGPEC NHLCTACMNN GVCHEDTGEC 250 260 270 280 290 300 ICPPGFMGRT CEKACELHTF GRTCKERCSG QEGCKSYVFC LPDPYGCSCA TGWKGLQCNE 310 320 330 340 350 360 ACHPGFYGPD CKLRCSCNNG EMCDRFQGCL CSPGWQGLQC EREGIQRMTP KIVDLPDHIE 370 380 390 400 410 420 VNSGKFNPIC KASGWPLPTN EEMTLVKPDG TVLHPKDFNH TDHFSVAIFT IHRILPPDSG 430 440 450 460 470 480 VWVCSVNTVA GMVEKPFNIS VKVLPKPLNA PNVIDTGHNF AVINISSEPY FGDGPIKSKK 490 500 510 520 530 540 LLYKPVNHYE AWQHIQVTNE IVTLNYLEPR TEYELCVQLV RRGEGGEGHP GPVRRFTTAS 550 560 570 580 590 600 IGLPPPRGLN LLPKSQTTLN LTWQPIFPSS EDDFYVEVER RSVQKSDQQN IKVPGNLTSV 610 620 630 640 650 660 LLNNLHPREQ YVVRARVNTK AQGEWSEDLT AWTLSDILPP QPENIKISNI THSSAVISWT 670 680 690 700 710 720 ILDGYSISSI TIRYKVQGKN EDQHVDVKIK NATITQYQLK GLEPETAYQV DIFAENNIGS 730 740 750 760 770 780 SNPAFSHELV TLPESQAPAD LGGGKMLLIA ILGSAGMTCL TVLLAFLIIL QLKRANVQRR 790 800 810 820 830 840 MAQAFQNVRE EPAVQFNSGT LALNRKVKNN PDPTIYPVLD WNDIKFQDVI GEGNFGQVLK 850 860 870 880 890 900 ARIKKDGLRM DAAIKRMKEY ASKDDHRDFA GELEVLCKLG HHPNIINLLG ACEHRGYLYL 910 920 930 940 950 960 AIEYAPHGNL LDFLRKSRVL ETDPAFAIAN STASTLSSQQ LLHFAADVAR GMDYLSQKQF 970 980 990 1000 1010 1020 IHRDLAARNI LVGENYVAKI ADFGLSRGQE VYVKKTMGRL PVRWMAIESL NYSVYTTNSD 1030 1040 1050 1060 1070 1080 VWSYGVLLWE IVSLGGTPYC GMTCAELYEK LPQGYRLEKP LNCDDEVYDL MRQCWREKPY 1090 1100 1110 1120 ERPSFAQILV SLNRMLEERK TYVNTTLYEK FTYAGIDCSA EEAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta." Ziegler S.F., Bird T.A., Schneringer J.A., Schooley K.A., Baum P.R. Oncogene 8:663-670(1993) [PubMed: 8382358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-346. Tissue: Placenta.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-346. Tissue: Placenta.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-346.
[5]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-37.
[6]	"Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human endothelial cells." Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., Jurasz P., Stewart D.J. Angiogenesis 12:25-33(2009) [PubMed: 19116766] [Abstract] Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRB.
[7]	"VE-PTP controls blood vessel development by balancing Tie-2 activity." Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F., Deutsch U., Nottebaum A.F., Vestweber D. J. Cell Biol. 185:657-671(2009) [PubMed: 19451274] [Abstract] Cited for: INTERACTION WITH PTPRB.
[8]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-596, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Vascular dysmorphogenesis caused by an activating mutation in the receptor tyrosine kinase TIE2." 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. Cell 87:1181-1190(1996) [PubMed: 8980225] [Abstract] Cited for: VARIANT VMCM TRP-849.
[10]	"Allelic and locus heterogeneity in inherited venous malformations." 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. Hum. Mol. Genet. 8:1279-1289(1999) [PubMed: 10369874] [Abstract] Cited for: VARIANTS VMCM TRP-849 AND SER-897.
[11]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-117.
[12]	"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: 17344846] [Abstract] Cited for: 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06139 mRNA. Translation: AAA61139.1.
AK291775 mRNA. Translation: BAF84464.1.
AL133411, AL355432, AL355433 Genomic DNA. Translation: CAI16055.1.
CH471071 Genomic DNA. Translation: EAW58571.1.

IPI

IPI00412829.

PIR

I58388.

RefSeq

NP_000450.2.

UniGene

Hs.89640

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FVR	X-ray	2.20	A/B	808-1124	[»]
2GY5	X-ray	2.90	A	23-445	[»]
2GY7	X-ray	3.70	B	23-445	[»]
2OO8	X-ray	2.20	X	808-1124	[»]
2OSC	X-ray	2.80	A	808-1124	[»]
2P4I	X-ray	2.50	A/B	808-1124	[»]
2WQB	X-ray	2.95	A	802-1124	[»]
3BEA	X-ray	2.02	A	917-935	[»]

SMR

Q02763. Positions 463-727.

ModBase

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Protein-protein interaction databases

DIP

DIP-6047N.

IntAct

Q02763. 7 interactions.

STRING

Q02763.

PTM databases

PhosphoSite

Q02763.

Proteomic databases

PRIDE

Q02763.

Genome annotation databases

Ensembl

ENST00000406359; ENSP00000383977; ENSG00000120156; Homo sapiens. [Genome view]

GeneID

7010.

KEGG

hsa:7010.

Organism-specific databases

CTD

7010.

GeneCards

GC09P027099.

H-InvDB

HIX0025697.

HGNC

HGNC:11724. TEK.

HPA

CAB010359.
HPA011738.

MIM

600195. phenotype.
600221. gene.

Orphanet

2451. Mucocutaneous venous malformations.

PharmGKB

PA36441.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG04502.

HOVERGEN

Q02763.

InParanoid

Q02763.

OMA

DAVIYKN.

OrthoDB

EOG97Q0RK.

PhylomeDB

Q02763.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.

Reactome

REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

Q02763.

Bgee

Q02763.

CleanEx

HS_TEK.

Genevestigator

Q02763.

GermOnline

ENSG00000120156. Homo sapiens.

Family and domain databases

InterPro

IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR018941. Tyr_kin_Tie2_Ig-like_dom-1_N.
IPR015781. Tyr_kinase_angiopoietin_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

PANTHER

PTHR23256:SF90. TieRTK. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.

Pfam

PF00041. fn3. 3 hits.
PF10430. Ig_Tie2_1. 1 hit.
[Graphical view]

SMART

SM00181. EGF. 2 hits.
SM00060. FN3. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS00022. EGF_1. 3 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 1 hit.
PS50853. FN3. 3 hits.
PS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

SOURCE

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Entry information

Entry name

TIE2_HUMAN

Accession

Primary (citable) accession number: Q02763
Secondary accession number(s): A8K6W0, Q5TCU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.