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Showing Protein Endoglin (HMDBP14526)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14526
Secondary Accession Numbers None
Name Endoglin
Synonyms
  1. Cell surface MJ7/18 antigen
Gene Name ENG
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:10625534). Required for normal structure and integrity of adult vasculature (By similarity). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (PubMed:10625534). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (PubMed:28530658). May play a role in the binding of endothelial cells to integrins. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:23300529). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
wound healing
cell chemotaxis
negative regulation of protein autophosphorylation
cell migration
cell adhesion
extracellular matrix disassembly
positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation
ventricular trabecula myocardium morphogenesis
positive regulation of pathway-restricted SMAD protein phosphorylation
positive regulation of collagen biosynthetic process
positive regulation of protein phosphorylation
negative regulation of nitric-oxide synthase activity
endocardial cushion morphogenesis
vascular associated smooth muscle cell development
heart development
epithelial to mesenchymal transition
epithelial to mesenchymal transition involved in endocardial cushion formation
angiogenesis
positive regulation of angiogenesis
artery morphogenesis
negative regulation of transcription from RNA polymerase II promoter
positive regulation of protein kinase B signaling cascade
positive regulation of transcription from RNA polymerase II promoter
negative regulation of endothelial cell proliferation
negative regulation of cell migration
heart looping
smooth muscle tissue development
vasculogenesis
positive regulation of BMP signaling pathway
outflow tract septum morphogenesis
regulation of transforming growth factor beta receptor signaling pathway
branching involved in blood vessel morphogenesis
transforming growth factor beta receptor signaling pathway
atrial cardiac muscle tissue morphogenesis
atrioventricular canal morphogenesis
cardiac atrium morphogenesis
cardiac ventricle morphogenesis
cell migration involved in endocardial cushion formation
positive regulation of gene expression
cell motility
central nervous system vasculogenesis
dorsal aorta morphogenesis
extracellular matrix constituent secretion
positive regulation of systemic arterial blood pressure
regulation of transcription, DNA-dependent
positive regulation of vascular associated smooth muscle cell differentiation
venous blood vessel morphogenesis
detection of hypoxia
response to hypoxia
negative regulation of gene expression
negative regulation of pathway-restricted SMAD protein phosphorylation
Cellular Component
cell surface
receptor complex
plasma membrane
extracellular space
external side of plasma membrane
endothelial microparticle
nuclear body
integral to membrane
Molecular Function
transforming growth factor beta binding
transforming growth factor beta-activated receptor activity
BMP binding
coreceptor activity
galactose binding
protein homodimerization activity
type II transforming growth factor beta receptor binding
identical protein binding
glycosaminoglycan binding
type I transforming growth factor beta receptor binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 653
Molecular Weight 70020.03
Theoretical pI 6.206
Pfam Domain Function
Signals
  • 1-26;
Transmembrane Regions
  • 582-606;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q63961
UniProtKB/Swiss-Prot Entry Name EGLN_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  3. Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP: Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol. 2009 May 5;7(5):e1000112. doi: 10.1371/journal.pbio.1000112. Epub 2009 May 26. [PubMed:19468303 ]
  4. Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV: Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10 via its orphan domain, inhibits blood vessel formation, and suppresses tumor growth. J Biol Chem. 2011 Aug 26;286(34):30034-46. doi: 10.1074/jbc.M111.260133. Epub 2011 Jul 7. [PubMed:21737454 ]
  5. Nolan-Stevaux O, Zhong W, Culp S, Shaffer K, Hoover J, Wickramasinghe D, Ruefli-Brasse A: Endoglin requirement for BMP9 signaling in endothelial cells reveals new mechanism of action for selective anti-endoglin antibodies. PLoS One. 2012;7(12):e50920. doi: 10.1371/journal.pone.0050920. Epub 2012 Dec 27. [PubMed:23300529 ]
  6. Lee NY, Blobe GC: The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells. J Biol Chem. 2007 Jul 20;282(29):21507-17. doi: 10.1074/jbc.M700176200. Epub 2007 May 31. [PubMed:17540773 ]
  7. Ge AZ, Butcher EC: Cloning and expression of a cDNA encoding mouse endoglin, an endothelial cell TGF-beta ligand. Gene. 1994 Jan 28;138(1-2):201-6. doi: 10.1016/0378-1119(94)90808-7. [PubMed:8125301 ]
  8. St-Jacques S, Cymerman U, Pece N, Letarte M: Molecular characterization and in situ localization of murine endoglin reveal that it is a transforming growth factor-beta binding protein of endothelial and stromal cells. Endocrinology. 1994 Jun;134(6):2645-57. doi: 10.1210/endo.134.6.8194490. [PubMed:8194490 ]
  9. Arthur HM, Ure J, Smith AJ, Renforth G, Wilson DI, Torsney E, Charlton R, Parums DV, Jowett T, Marchuk DA, Burn J, Diamond AG: Endoglin, an ancillary TGFbeta receptor, is required for extraembryonic angiogenesis and plays a key role in heart development. Dev Biol. 2000 Jan 1;217(1):42-53. doi: 10.1006/dbio.1999.9534. [PubMed:10625534 ]
  10. Sugden WW, Meissner R, Aegerter-Wilmsen T, Tsaryk R, Leonard EV, Bussmann J, Hamm MJ, Herzog W, Jin Y, Jakobsson L, Denz C, Siekmann AF: Endoglin controls blood vessel diameter through endothelial cell shape changes in response to haemodynamic cues. Nat Cell Biol. 2017 Jun;19(6):653-665. doi: 10.1038/ncb3528. Epub 2017 May 22. [PubMed:28530658 ]