Angiomotin information

AMOT
Identifiers
Aliases	AMOT, angiomotin
External IDs	OMIM: 300410; MGI: 108440; HomoloGene: 15778; GeneCards: AMOT; OMA:AMOT - orthologs
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	144,288,177 bp
RNA expression pattern
	Top expressed in
	middle frontal gyrus; ; Brodmann area 10; ; frontal pole; ; secondary oocyte; ; gastrocnemius muscle; ; amygdala; ; caudate nucleus; ; ganglionic eminence; ; nucleus accumbens; ; putamen;
	Top expressed in
	primitive streak; ; extraocular muscle; ; saccule; ; otic placode; ; digastric muscle; ; internal carotid artery; ; extensor digitorum longus muscle; ; soleus muscle; ; sternocleidomastoid muscle; ; vastus lateralis muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding; angiostatin binding; identical protein binding; signaling receptor activity;
Cellular component	cytoplasm; integral component of membrane; cytosol; ruffle; endocytic vesicle; stress fiber; cell surface; actin filament; COP9 signalosome; cytoplasmic vesicle; external side of plasma membrane; lamellipodium; bicellular tight junction; nucleus; cell junction;
Biological process	regulation of cell migration; blood vessel morphogenesis; blood vessel endothelial cell migration; gastrulation with mouth forming second; in utero embryonic development; hippo signaling; vasculogenesis; establishment of cell polarity involved in ameboidal cell migration; chemotaxis; negative regulation of GTPase activity; positive regulation of blood vessel endothelial cell migration; cell-cell junction assembly; positive regulation of cell size; negative regulation of angiogenesis; cell migration involved in gastrulation; positive regulation of embryonic development; regulation of small GTPase mediated signal transduction; positive regulation of stress fiber assembly; negative regulation of vascular permeability; actin cytoskeleton organization; angiogenesis;
	Sources:Amigo / QuickGO
Orthologs
	154796
	27494
	n/a
	ENSMUSG00000041688
	Q4VCS5
	Q8VHG2
	NM_001113490; NM_133265; NM_001386998; NM_001386999
	NM_001290274; NM_153319
	NP_001106962; NP_573572
NP_001277203; NP_695231; NP_001390315; NP_001390316; NP_001390317;
	NP_001390318
	Wikidata
View/Edit Human	View/Edit Mouse

Angiomotin (AMOT) is a protein that in humans is encoded by the AMOT gene.^[4]^[5]^[6]^[7] It belongs to the motin family of angiostatin binding proteins, which includes angiomotin, angiomotin-like 1 (AMOTL1) and angiomotin-like 2 (AMOTL2) characterized by coiled-coil domains at N-terminus and consensus PDZ-binding domain at the C-terminus.^[6] Angiomotin is expressed predominantly in endothelial cells of capillaries as well as angiogenic tissues such as placenta and solid tumor.^[8]

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000041688 – 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.
^ Troyanovsky B, Levchenko T, Månsson G, Matvijenko O, Holmgren L (March 2001). "Angiomotin: an angiostatin binding protein that regulates endothelial cell migration and tube formation". The Journal of Cell Biology. 152 (6): 1247–54. doi:10.1083/jcb.152.6.1247. PMC 2199208. PMID 11257124.
^ Bratt A, Birot O, Sinha I, Veitonmäki N, Aase K, Ernkvist M, Holmgren L (October 2005). "Angiomotin regulates endothelial cell-cell junctions and cell motility". The Journal of Biological Chemistry. 280 (41): 34859–69. doi:10.1074/jbc.M503915200. PMID 16043488.
^ ^a ^b Bratt A, Wilson WJ, Troyanovsky B, Aase K, Kessler R, Van Meir EG, Holmgren L, Meir EG (September 2002). "Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains". Gene. 298 (1): 69–77. doi:10.1016/S0378-1119(02)00928-9. PMID 12406577.
^ "Entrez Gene: AMOT angiomotin".
^ Zetter BR (March 2001). "Hold that line. Angiomotin regulates endothelial cell motility". The Journal of Cell Biology. 152 (6): F35-6. doi:10.1083/jcb.152.6.F35. PMC 2199203. PMID 11257132.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000041688 – Ensembl, May 2017

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

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

[Troyanovsky_2001-4] Troyanovsky B, Levchenko T, Månsson G, Matvijenko O, Holmgren L (March 2001). "Angiomotin: an angiostatin binding protein that regulates endothelial cell migration and tube formation". The Journal of Cell Biology. 152 (6): 1247–54. doi:10.1083/jcb.152.6.1247. PMC 2199208. PMID 11257124.

[Bratt_2005-5] Bratt A, Birot O, Sinha I, Veitonmäki N, Aase K, Ernkvist M, Holmgren L (October 2005). "Angiomotin regulates endothelial cell-cell junctions and cell motility". The Journal of Biological Chemistry. 280 (41): 34859–69. doi:10.1074/jbc.M503915200. PMID 16043488.

[Bratt_2002-6] Bratt A, Wilson WJ, Troyanovsky B, Aase K, Kessler R, Van Meir EG, Holmgren L, Meir EG (September 2002). "Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains". Gene. 298 (1): 69–77. doi:10.1016/S0378-1119(02)00928-9. PMID 12406577.

[entrez-7] "Entrez Gene: AMOT angiomotin".

[Zetter_2001-8] Zetter BR (March 2001). "Hold that line. Angiomotin regulates endothelial cell motility". The Journal of Cell Biology. 152 (6): F35-6. doi:10.1083/jcb.152.6.F35. PMC 2199203. PMID 11257132.

Angiomotin information

and 11 Related for: Angiomotin information

Angiomotin

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Wesley Sundquist

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MAP11