THC Science

Search for
Structures	Swiss-model
Domains	InterPro

tyrosine kinase with immunoglobulin-like and EGF-like domains 1
tyrosine kinase with immunoglobulin-like and EGF-like domains 1
Identifiers
Symbol	TIE1
Alt. symbols	TIE, JTK14
NCBI gene	7075
HGNC	11809
OMIM	600222
RefSeq	NM_005424
UniProt	P35590
Other data
EC number	2.7.1.112
Locus	Chr. 1 p34-p33
Structures
Search for
Structures	Swiss-model
Domains	InterPro

TIE1
Identifiers
Aliases	TIE1, JTK14, TIE, tyrosine kinase with immunoglobulin like and EGF like domains 1, LMPHM11
External IDs	OMIM: 600222; MGI: 99906; HomoloGene: 3957; GeneCards: TIE1; OMA:TIE1 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	43,323,108 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	118,347,258 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	n/a
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	7075
	21846
	ENSG00000066056
	ENSMUSG00000033191
	P35590
	Q06806
	NM_001253357; NM_005424
	NM_011587
	NP_001240286; NP_005415
	NP_035717
	Wikidata
View/Edit Human	View/Edit Mouse

Tyrosine kinase with immunoglobulin-like and EGF-like domains 1 also known as TIE1 is an angiopoietin receptor which in humans is encoded by the TIE1 gene.^[5]

Function[edit]

TIE1 is a cell surface protein expressed exclusively in endothelial cells, however it has also been shown to be expressed in immature hematopoietic cells^[6] and platelets.^[7] TIE1 upregulates the cell adhesion molecules (CAMs) VCAM-1, E-selectin, and ICAM-1 through a p38-dependent mechanism. Attachment of monocyte derived immune cells to endothelial cells is also enhanced by TIE1 expression. TIE1 has a proinflammatory effect and may play a role in the endothelial inflammatory diseases such as atherosclerosis.^[8]

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000066056 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033191 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Partanen J, Armstrong E, Mäkelä TP, Korhonen J, Sandberg M, Renkonen R, Knuutila S, Huebner K, Alitalo K (April 1992). "A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains". Molecular and Cellular Biology. 12 (4): 1698–707. doi:10.1128/mcb.12.4.1698. PMC 369613. PMID 1312667.
^ Rodewald HR, Sato TN (January 1996). "Tie1, a receptor tyrosine kinase essential for vascular endothelial cell integrity, is not critical for the development of hematopoietic cells". Oncogene. 12 (2): 397–404. PMID 8570217.
^ Tsiamis AC, Hayes P, Box H, Goodall AH, Bell PR, Brindle NP (2000). "Characterization and regulation of the receptor tyrosine kinase Tie-1 in platelets". Journal of Vascular Research. 37 (6): 437–42. doi:10.1159/000054075. PMID 11146396. S2CID 43509019.
^ Chan B, Yuan HT, Ananth Karumanchi S, Sukhatme VP (July 2008). "Receptor tyrosine kinase Tie-1 overexpression in endothelial cells upregulates adhesion molecules". Biochemical and Biophysical Research Communications. 371 (3): 475–9. doi:10.1016/j.bbrc.2008.04.091. PMID 18448073.

External links[edit]

Receptor,+TIE-1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000066056 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000033191 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1312667-5] Partanen J, Armstrong E, Mäkelä TP, Korhonen J, Sandberg M, Renkonen R, Knuutila S, Huebner K, Alitalo K (April 1992). "A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains". Molecular and Cellular Biology. 12 (4): 1698–707. doi:10.1128/mcb.12.4.1698. PMC 369613. PMID 1312667.

[6] Rodewald HR, Sato TN (January 1996). "Tie1, a receptor tyrosine kinase essential for vascular endothelial cell integrity, is not critical for the development of hematopoietic cells". Oncogene. 12 (2): 397–404. PMID 8570217.

[pmid11146396-7] Tsiamis AC, Hayes P, Box H, Goodall AH, Bell PR, Brindle NP (2000). "Characterization and regulation of the receptor tyrosine kinase Tie-1 in platelets". Journal of Vascular Research. 37 (6): 437–42. doi:10.1159/000054075. PMID 11146396. S2CID 43509019.

[pmid18448073-8] Chan B, Yuan HT, Ananth Karumanchi S, Sukhatme VP (July 2008). "Receptor tyrosine kinase Tie-1 overexpression in endothelial cells upregulates adhesion molecules". Biochemical and Biophysical Research Communications. 371 (3): 475–9. doi:10.1016/j.bbrc.2008.04.091. PMID 18448073.

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Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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