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Endoglin (CD antigen CD105)

 EGLN_HUMAN              Reviewed;         658 AA.
P17813; Q14248; Q14926; Q5T9C0;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
22-NOV-2017, entry version 190.
RecName: Full=Endoglin;
AltName: CD_antigen=CD105;
Flags: Precursor;
Name=ENG; Synonyms=END;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND ALTERNATIVE SPLICING.
PubMed=8370410; DOI=10.1002/eji.1830230943;
Bellon T., Corbi A., Lastres P., Cales C., Cebrian M., Vera S.,
Cheifetz S., Massague J., Letarte M., Bernabeu C.;
"Identification and expression of two forms of the human transforming
growth factor-beta-binding protein endoglin with distinct cytoplasmic
regions.";
Eur. J. Immunol. 23:2340-2345(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 14-658, PROTEIN SEQUENCE
OF 26-36 (ISOFORM LONG), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Umbilical vein;
PubMed=1692830;
Gougos A., Letarte M.;
"Primary structure of endoglin, an RGD-containing glycoprotein of
human endothelial cells.";
J. Biol. Chem. 265:8361-8364(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-378, FUNCTION, AND
INVOLVEMENT IN HHT1.
PubMed=7894484; DOI=10.1038/ng1294-345;
McAllister K.A., Grogg K.M., Johnson D.W., Gallione C.J.,
Baldwin M.A., Jackson C.E., Helmbold E.A., Markel D.S., McKinnon W.C.,
Murrell J., McCormick M.K., Pericak-Vance M.A., Heutink P.,
Oostra B.A., Haitjema T., Westerman C.J., Porteous M.E.,
Guttmacher A.E., Letarte M., Marchuk D.A.;
"Endoglin, a TGF-beta binding protein of endothelial cells, is the
gene for hereditary haemorrhagic telangiectasia type 1.";
Nat. Genet. 8:345-351(1994).
[6]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=1326540;
Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massague J.,
Letarte M.;
"Endoglin is a component of the transforming growth factor-beta
receptor system in human endothelial cells.";
J. Biol. Chem. 267:19027-19030(1992).
[7]
INTERACTION WITH TCTEX1D4.
PubMed=16982625; DOI=10.1074/jbc.M608614200;
Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T.,
McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.;
"Identification of Tctex2beta, a novel dynein light chain family
member that interacts with different transforming growth factor-beta
receptors.";
J. Biol. Chem. 281:37069-37080(2006).
[8]
INTERACTION WITH ARRB2, SUBCELLULAR LOCATION, FUNCTION, AND
MUTAGENESIS OF THR-650.
PubMed=17540773; DOI=10.1074/jbc.M700176200;
Lee N.Y., Blobe G.C.;
"The interaction of endoglin with beta-arrestin2 regulates
transforming growth factor-beta-mediated ERK activation and migration
in endothelial cells.";
J. Biol. Chem. 282:21507-21517(2007).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
FUNCTION, AND INTERACTION WITH GDF2 AND BMP10.
PubMed=21737454; DOI=10.1074/jbc.M111.260133;
Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W.,
Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J.,
Kumar R., Grinberg A.V.;
"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. 286:30034-30046(2011).
[11]
INTERACTION WITH GDF2 AND ACVRL1, AND SUBUNIT.
PubMed=22347366; DOI=10.1371/journal.pone.0029948;
Alt A., Miguel-Romero L., Donderis J., Aristorena M., Blanco F.J.,
Round A., Rubio V., Bernabeu C., Marina A.;
"Structural and functional insights into endoglin ligand recognition
and binding.";
PLoS ONE 7:E29948-E29948(2012).
[12]
FUNCTION.
PubMed=23300529; DOI=10.1371/journal.pone.0050920;
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 7:E50920-E50920(2012).
[13] {ECO:0000244|PDB:5HZV, ECO:0000244|PDB:5HZW, ECO:0000244|PDB:5I04}
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 26-337, X-RAY
CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 338-581, X-RAY CRYSTALLOGRAPHY
(4.45 ANGSTROMS) OF 26-337 IN COMPLEX WITH GDF2, INTERACTION WITH GDF2
AND ACVRL1, SUBUNIT, DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF
ASP-246; 270-GLN-ILE-271; TYR-277; SER-278; PHE-282; PHE-290; CYS-350;
CYS-382 AND CYS-516.
PubMed=28564608; DOI=10.1016/j.celrep.2017.05.011;
Saito T., Bokhove M., Croci R., Zamora-Caballero S., Han L.,
Letarte M., de Sanctis D., Jovine L.;
"Structural Basis of the Human Endoglin-BMP9 Interaction: Insights
into BMP Signaling and HHT1.";
Cell Rep. 19:1917-1928(2017).
[14]
VARIANT HHT1 192-ARG--PRO-198 DEL, AND VARIANT MET-5.
PubMed=9245986; DOI=10.1086/513906;
Shovlin C.L., Hughes J.M.B., Scott J., Seidman C.E., Seidman J.G.;
"Characterization of endoglin and identification of novel mutations in
hereditary hemorrhagic telangiectasia.";
Am. J. Hum. Genet. 61:68-79(1997).
[15]
VARIANT HHT1 ASP-160.
PubMed=9157574;
Yamaguchi H., Azuma H., Shigekiyo T., Inoue H., Saito S.;
"A novel missense mutation in the endoglin gene in hereditary
hemorrhagic telangiectasia.";
Thromb. Haemost. 77:243-247(1997).
[16]
VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-306.
PubMed=9554745;
DOI=10.1002/(SICI)1098-1004(1998)11:4<286::AID-HUMU6>3.3.CO;2-2;
Gallione C.J., Klaus D.J., Yeh E.Y., Stenzel T.T., Xue Y.,
Anthony K.B., McAllister K.A., Baldwin M.A., Berg J.N., Lux A.,
Smith J.D., Vary C.P.H., Craigen W.J., Westermann C.J.J., Warner M.L.,
Miller Y.E., Jackson C.E., Guttmacher A.E., Marchuk D.A.;
"Mutation and expression analysis of the endoglin gene in hereditary
hemorrhagic telangiectasia reveals null alleles.";
Hum. Mutat. 11:286-294(1998).
[17]
VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-221, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANTS HHT1 VAL-52; ARG-53;
CYS-149 AND PRO-221.
PubMed=10545596; DOI=10.1093/hmg/8.12.2171;
Pece-Barbara N., Cymerman U., Vera S., Marchuk D.A., Letarte M.;
"Expression analysis of four endoglin missense mutations suggests that
haploinsufficiency is the predominant mechanism for hereditary
hemorrhagic telangiectasia type 1.";
Hum. Mol. Genet. 8:2171-2181(1999).
[18]
VARIANT HHT1 VAL-413.
PubMed=10982033; DOI=10.1007/s004390000326;
Gallione C.J., Scheessele E.A., Reinhardt D., Duits A.J., Berg J.N.,
Westermann C.J.J., Marchuk D.A.;
"Two common endoglin mutations in families with hereditary hemorrhagic
telangiectasia in the Netherlands Antilles: evidence for a founder
effect.";
Hum. Genet. 107:40-44(2000).
[19]
VARIANT HHT1 ARG-53, AND TISSUE SPECIFICITY.
PubMed=10625079; DOI=10.1203/00006450-200001000-00008;
Cymerman U., Vera S., Pece-Barbara N., Bourdeau A., White R.I. Jr.,
Dunn J., Letarte M.;
"Identification of hereditary hemorrhagic telangiectasia type 1 in
newborns by protein expression and mutation analysis of endoglin.";
Pediatr. Res. 47:24-35(2000).
[20]
VARIANTS HHT1 PRO-8; PHE-49; ARG-107; CYS-207 DEL; THR-263;
ARG-232-233-THR DEL; ILE-263 DEL; SER-412 AND MET-504.
PubMed=15024723; DOI=10.1002/humu.20017;
French Rendu-Osler network;
Lesca G., Plauchu H., Coulet F., Lefebvre S., Plessis G., Odent S.,
Riviere S., Leheup B., Goizet C., Carette M.-F., Cordier J.-F.,
Pinson S., Soubrier F., Calender A., Giraud S.;
"Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary
hemorrhagic telangiectasia in France.";
Hum. Mutat. 23:289-299(2004).
[21]
VARIANTS HHT1 PRO-221; ILE-263 DEL AND LEU-615.
PubMed=15712270; DOI=10.1002/humu.9311;
Kuehl H.K.A., Caselitz M., Hasenkamp S., Wagner S., El-Harith E.-H.A.,
Manns M.P., Stuhrmann M.;
"Hepatic manifestation is associated with ALK1 in hereditary
hemorrhagic telangiectasia: identification of five novel ALK1 and one
novel ENG mutations.";
Hum. Mutat. 25:320-320(2005).
[22]
VARIANTS HHT1 ASP-11; ASP-105; GLU-175; THR-220; ASP-308; SER-363;
TRP-437; SER-490; HIS-529; PRO-547 AND ASP-604.
PubMed=16752392; DOI=10.1002/humu.20342;
Bossler A.D., Richards J., George C., Godmilow L., Ganguly A.;
"Novel mutations in ENG and ACVRL1 identified in a series of 200
individuals undergoing clinical genetic testing for hereditary
hemorrhagic telangiectasia (HHT): correlation of genotype with
phenotype.";
Hum. Mutat. 27:667-675(2006).
[23]
VARIANTS HHT1 193-THR-LEU-194 DELINS VAL-LEU-GLN AND ASP-545.
PubMed=16525724;
Argyriou L., Twelkemeyer S., Panchulidze I., Wehner L.E., Teske U.,
Engel W., Nayernia K.;
"Novel mutations in the ENG and ACVRL1 genes causing hereditary
hemorrhagic teleangiectasia.";
Int. J. Mol. Med. 17:655-659(2006).
[24]
VARIANTS PRO-150; PRO-205; MET-236; MET-315; GLU-374; ARG-414;
SER-545; TYR-549 AND ALA-561, AND VARIANTS HHT1 GLN-221; GLU-238;
SER-263; ARG-269; TYR-394; PRO-529 AND ARG-603.
PubMed=20414677; DOI=10.1007/s00439-010-0825-4;
Richards-Yutz J., Grant K., Chao E.C., Walther S.E., Ganguly A.;
"Update on molecular diagnosis of hereditary hemorrhagic
telangiectasia.";
Hum. Genet. 128:61-77(2010).
-!- FUNCTION: Vascular endothelium glycoprotein that plays an
important role in the regulation of angiogenesis (PubMed:21737454,
PubMed:23300529). Required for normal structure and integrity of
adult vasculature (PubMed:7894484). Regulates the migration of
vascular endothelial cells (PubMed:17540773). Required for normal
extraembryonic angiogenesis and for embryonic heart development
(By similarity). May play a critical role in the binding of
endothelial cells to integrins and/or other RGD receptors
(PubMed:1692830). 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:8370410,
PubMed:21737454, PubMed:22347366, PubMed:23300529). Required for
GDF2/BMP9 signaling through SMAD1 in endothelial cells and
modulates TGFB1 signaling through SMAD3 (PubMed:21737454,
PubMed:22347366, PubMed:23300529). {ECO:0000250|UniProtKB:Q63961,
ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:21737454,
ECO:0000269|PubMed:23300529, ECO:0000269|PubMed:7894484,
ECO:0000269|PubMed:8370410, ECO:0000305|PubMed:1692830}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:8370410,
PubMed:1326540, PubMed:21737454, PubMed:22347366,
PubMed:28564608). Forms a heteromeric complex with the signaling
receptors for transforming growth factor-beta: TGFBR1 and/or
TGFBR2 (PubMed:1326540). It is able to bind TGFB1 and TGFB2 with
high affinity, but not TGFB3 (PubMed:8370410, PubMed:1326540).
Interacts with GDF2, forming a heterotetramer with a 2:2
stoichiometry (PubMed:21737454, PubMed:22347366, PubMed:28564608).
Interacts with ACVRL1 (PubMed:22347366, PubMed:28564608). Can form
a heteromeric complex with GDF2 and ACVRL1 (PubMed:28564608).
Interacts with BMP10 (PubMed:21737454). Interacts with TCTEX1D4
(PubMed:16982625). Interacts with ARRB2 (PubMed:17540773).
{ECO:0000269|PubMed:1326540, ECO:0000269|PubMed:16982625,
ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:21737454,
ECO:0000269|PubMed:22347366, ECO:0000269|PubMed:28564608,
ECO:0000269|PubMed:8370410}.
-!- INTERACTION:
P08648:ITGA5; NbExp=4; IntAct=EBI-2834630, EBI-1382311;
P05556:ITGB1; NbExp=3; IntAct=EBI-2834630, EBI-703066;
P02750:LRG1; NbExp=4; IntAct=EBI-16065304, EBI-9083443;
P01137:TGFB1; NbExp=2; IntAct=EBI-2834630, EBI-779636;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10545596,
ECO:0000269|PubMed:1326540, ECO:0000269|PubMed:1692830,
ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:8370410}; Single-
pass type I membrane protein {ECO:0000305|PubMed:1692830,
ECO:0000305|PubMed:8370410}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P17813-1; Sequence=Displayed;
Name=Short;
IsoId=P17813-2; Sequence=VSP_004233;
-!- TISSUE SPECIFICITY: Detected on umbilical veil endothelial cells
(PubMed:10625079). Detected in placenta (at protein level)
(PubMed:1692830). Detected on endothelial cells (PubMed:1692830).
{ECO:0000269|PubMed:10625079, ECO:0000269|PubMed:1692830}.
-!- DOMAIN: The ZP domain mediates dimerization.
{ECO:0000269|PubMed:28564608}.
-!- DOMAIN: The N-terminal OR region is composed of two intertwined
domains (OR1 and OR2) with a common, novel fold. Each contains 12
beta-strands that form a parallel beta-helix-like structure, plus
a single alpha-helix. The OR1 region mediates interaction with
GDF2. {ECO:0000269|PubMed:28564608}.
-!- DISEASE: Telangiectasia, hereditary hemorrhagic, 1 (HHT1)
[MIM:187300]: A multisystemic vascular dysplasia leading to
dilation of permanent blood vessels and arteriovenous
malformations of skin, mucosa, and viscera. The disease is
characterized by recurrent epistaxis and gastro-intestinal
hemorrhage. Visceral involvement includes arteriovenous
malformations of the lung, liver, and brain.
{ECO:0000269|PubMed:10545596, ECO:0000269|PubMed:10625079,
ECO:0000269|PubMed:10982033, ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:15712270, ECO:0000269|PubMed:16525724,
ECO:0000269|PubMed:16752392, ECO:0000269|PubMed:20414677,
ECO:0000269|PubMed:7894484, ECO:0000269|PubMed:9157574,
ECO:0000269|PubMed:9245986, ECO:0000269|PubMed:9554745}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ENGID40452ch9q34.html";
-!- WEB RESOURCE: Name=Hereditary Hemorrhagic Telangiectasia and ENG;
URL="http://arup.utah.edu/database/ENG/ENG_welcome.php";
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EMBL; X72012; CAA50891.1; -; mRNA.
EMBL; AL157935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL162586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87702.1; -; Genomic_DNA.
EMBL; J05481; AAA35800.1; -; mRNA.
EMBL; U37439; AAC63386.1; -; Genomic_DNA.
EMBL; AF036969; AAC63386.1; JOINED; Genomic_DNA.
EMBL; U37447; AAC63386.1; JOINED; Genomic_DNA.
EMBL; AF036970; AAC63386.1; JOINED; Genomic_DNA.
EMBL; U37446; AAC63386.1; JOINED; Genomic_DNA.
EMBL; U37445; AAC63386.1; JOINED; Genomic_DNA.
EMBL; AF036971; AAC63386.1; JOINED; Genomic_DNA.
EMBL; U37442; AAC63386.1; JOINED; Genomic_DNA.
EMBL; U37441; AAC63386.1; JOINED; Genomic_DNA.
CCDS; CCDS48029.1; -. [P17813-1]
CCDS; CCDS6880.1; -. [P17813-2]
PIR; S50831; S50831.
RefSeq; NP_000109.1; NM_000118.3. [P17813-2]
RefSeq; NP_001108225.1; NM_001114753.2. [P17813-1]
RefSeq; NP_001265067.1; NM_001278138.1.
UniGene; Hs.76753; -.
PDB; 5HZV; X-ray; 2.70 A; A=338-581.
PDB; 5HZW; X-ray; 4.45 A; A=26-337.
PDB; 5I04; X-ray; 2.42 A; A=26-337.
PDBsum; 5HZV; -.
PDBsum; 5HZW; -.
PDBsum; 5I04; -.
ProteinModelPortal; P17813; -.
SMR; P17813; -.
BioGrid; 108337; 12.
CORUM; P17813; -.
DIP; DIP-6246N; -.
IntAct; P17813; 15.
MINT; MINT-4529566; -.
STRING; 9606.ENSP00000362299; -.
ChEMBL; CHEMBL3712885; -.
GuidetoPHARMACOLOGY; 2895; -.
iPTMnet; P17813; -.
PhosphoSitePlus; P17813; -.
SwissPalm; P17813; -.
DMDM; 3041681; -.
MaxQB; P17813; -.
PaxDb; P17813; -.
PeptideAtlas; P17813; -.
PRIDE; P17813; -.
DNASU; 2022; -.
Ensembl; ENST00000344849; ENSP00000341917; ENSG00000106991. [P17813-2]
Ensembl; ENST00000373203; ENSP00000362299; ENSG00000106991. [P17813-1]
GeneID; 2022; -.
KEGG; hsa:2022; -.
UCSC; uc004bsj.6; human. [P17813-1]
CTD; 2022; -.
DisGeNET; 2022; -.
EuPathDB; HostDB:ENSG00000106991.13; -.
GeneCards; ENG; -.
GeneReviews; ENG; -.
HGNC; HGNC:3349; ENG.
HPA; CAB000096; -.
HPA; CAB072873; -.
HPA; HPA011862; -.
HPA; HPA067440; -.
MalaCards; ENG; -.
MIM; 131195; gene.
MIM; 187300; phenotype.
neXtProt; NX_P17813; -.
OpenTargets; ENSG00000106991; -.
Orphanet; 231160; Familial cerebral saccular aneurysm.
Orphanet; 329971; Generalized juvenile polyposis/juvenile polyposis coli.
Orphanet; 774; Hereditary hemorrhagic telangiectasia.
PharmGKB; PA27785; -.
eggNOG; ENOG410IQ57; Eukaryota.
eggNOG; ENOG410YK9H; LUCA.
GeneTree; ENSGT00530000063861; -.
HOGENOM; HOG000112346; -.
HOVERGEN; HBG005573; -.
InParanoid; P17813; -.
KO; K06526; -.
OMA; DANHNMQ; -.
OrthoDB; EOG091G030O; -.
PhylomeDB; P17813; -.
TreeFam; TF337375; -.
SIGNOR; P17813; -.
ChiTaRS; ENG; human.
GeneWiki; Endoglin; -.
GenomeRNAi; 2022; -.
PRO; PR:P17813; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106991; -.
CleanEx; HS_ENG; -.
ExpressionAtlas; P17813; baseline and differential.
Genevisible; P17813; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0072563; C:endothelial microparticle; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IPI:BHF-UCL.
GO; GO:0070022; C:transforming growth factor beta receptor complex; IC:BHF-UCL.
GO; GO:0048185; F:activin binding; TAS:BHF-UCL.
GO; GO:0005534; F:galactose binding; IDA:BHF-UCL.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IPI:BHF-UCL.
GO; GO:0005072; F:transforming growth factor beta receptor, cytoplasmic mediator activity; IDA:BHF-UCL.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IDA:BHF-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:BHF-UCL.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:1905222; P:atrioventricular canal morphogenesis; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; TAS:BHF-UCL.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0003209; P:cardiac atrium morphogenesis; ISS:BHF-UCL.
GO; GO:0003208; P:cardiac ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; IMP:BHF-UCL.
GO; GO:0016477; P:cell migration; IMP:BHF-UCL.
GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IEA:Ensembl.
GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0022009; P:central nervous system vasculogenesis; IMP:BHF-UCL.
GO; GO:0001300; P:chronological cell aging; IEP:BHF-UCL.
GO; GO:0070483; P:detection of hypoxia; IDA:BHF-UCL.
GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0070278; P:extracellular matrix constituent secretion; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:BHF-UCL.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:BHF-UCL.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; ISS:BHF-UCL.
GO; GO:0030155; P:regulation of cell adhesion; TAS:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; TAS:BHF-UCL.
GO; GO:0042325; P:regulation of phosphorylation; TAS:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:HGNC.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:HGNC.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
GO; GO:0048745; P:smooth muscle tissue development; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0097084; P:vascular smooth muscle cell development; ISS:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
GO; GO:0048845; P:venous blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; IMP:BHF-UCL.
InterPro; IPR001507; ZP_dom.
Pfam; PF00100; Zona_pellucida; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Cell adhesion;
Cell membrane; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:1692830}.
CHAIN 26 658 Endoglin.
/FTId=PRO_0000021156.
TOPO_DOM 26 586 Extracellular. {ECO:0000255}.
TRANSMEM 587 611 Helical. {ECO:0000255}.
TOPO_DOM 612 658 Cytoplasmic. {ECO:0000255}.
DOMAIN 363 533 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375,
ECO:0000305|PubMed:28564608}.
REGION 26 337 Required for interaction with GDF2.
{ECO:0000269|PubMed:21737454,
ECO:0000269|PubMed:22347366,
ECO:0000269|PubMed:28564608}.
REGION 26 46 OR1, N-terminal part.
{ECO:0000269|PubMed:28564608}.
REGION 47 199 OR2. {ECO:0000269|PubMed:28564608}.
REGION 200 330 OR1, C-terminal part.
{ECO:0000269|PubMed:28564608}.
REGION 270 282 Essential for interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MOTIF 399 401 Cell attachment site. {ECO:0000255}.
COMPBIAS 336 576 Ser/Thr-rich.
MOD_RES 646 646 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q63961}.
MOD_RES 649 649 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:Q63961}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 207 {ECO:0000244|PDB:5HZW,
ECO:0000244|PDB:5I04,
ECO:0000269|PubMed:28564608}.
DISULFID 53 182 {ECO:0000244|PDB:5HZW,
ECO:0000244|PDB:5I04,
ECO:0000269|PubMed:28564608}.
DISULFID 242 330 {ECO:0000244|PDB:5HZW,
ECO:0000269|PubMed:28564608}.
DISULFID 350 382 {ECO:0000244|PDB:5HZV,
ECO:0000269|PubMed:28564608}.
DISULFID 363 442 {ECO:0000244|PDB:5HZV,
ECO:0000269|PubMed:28564608}.
DISULFID 394 412 {ECO:0000244|PDB:5HZV,
ECO:0000269|PubMed:28564608}.
DISULFID 493 549 {ECO:0000244|PDB:5HZV,
ECO:0000269|PubMed:28564608}.
DISULFID 516 516 Interchain.
{ECO:0000305|PubMed:28564608}.
VAR_SEQ 619 658 SPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA
-> EYPRPPQ (in isoform Short).
{ECO:0000303|PubMed:8370410}.
/FTId=VSP_004233.
VARIANT 5 5 T -> M (in dbSNP:rs35400405).
{ECO:0000269|PubMed:9245986}.
/FTId=VAR_005192.
VARIANT 8 8 L -> P (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026774.
VARIANT 11 11 A -> D (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070279.
VARIANT 49 49 V -> F (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026775.
VARIANT 52 52 G -> V (in HHT1; impairs protein folding;
abolishes expression at the cell
surface). {ECO:0000269|PubMed:10545596,
ECO:0000269|PubMed:9554745}.
/FTId=VAR_005193.
VARIANT 53 53 C -> R (in HHT1; impairs protein folding;
abolishes expression at the cell
surface). {ECO:0000269|PubMed:10545596,
ECO:0000269|PubMed:10625079,
ECO:0000269|PubMed:9554745}.
/FTId=VAR_005194.
VARIANT 105 105 V -> D (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070280.
VARIANT 107 107 L -> R (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026776.
VARIANT 149 149 W -> C (in HHT1; impairs protein folding;
nearly abolishes expression at the cell
surface; dbSNP:rs878853657).
{ECO:0000269|PubMed:10545596,
ECO:0000269|PubMed:9554745}.
/FTId=VAR_005195.
VARIANT 150 150 A -> P (found in a family with hereditary
hemorrhagic talagiectasia; unknown
pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070281.
VARIANT 160 160 A -> D (in HHT1).
{ECO:0000269|PubMed:9157574}.
/FTId=VAR_009120.
VARIANT 175 175 A -> E (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070282.
VARIANT 192 198 Missing (in HHT1).
{ECO:0000269|PubMed:9245986}.
/FTId=VAR_005196.
VARIANT 193 194 TL -> VLQ (in HHT1).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070283.
VARIANT 205 205 R -> P. {ECO:0000269|PubMed:20414677}.
/FTId=VAR_070284.
VARIANT 207 207 Missing (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026777.
VARIANT 220 220 I -> T (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070285.
VARIANT 221 221 L -> P (in HHT1; impairs protein folding;
strongly reduces expression at the cell
surface). {ECO:0000269|PubMed:10545596,
ECO:0000269|PubMed:15712270}.
/FTId=VAR_009121.
VARIANT 221 221 L -> Q (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070286.
VARIANT 232 233 Missing (in HHT1).
/FTId=VAR_026778.
VARIANT 236 236 V -> M (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance;
dbSNP:rs754136153).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070287.
VARIANT 238 238 V -> E (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070288.
VARIANT 263 263 I -> S (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070289.
VARIANT 263 263 I -> T (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026780.
VARIANT 263 263 Missing (in HHT1).
{ECO:0000269|PubMed:15024723,
ECO:0000269|PubMed:15712270}.
/FTId=VAR_026779.
VARIANT 269 269 M -> R (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070290.
VARIANT 306 306 L -> P (in HHT1).
{ECO:0000269|PubMed:9554745}.
/FTId=VAR_005197.
VARIANT 308 308 A -> D (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070291.
VARIANT 315 315 V -> M (found in a family with hereditary
hemorrhagic talagiectasia; unknown
pathological significance;
dbSNP:rs763508329).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070292.
VARIANT 363 363 C -> S (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070293.
VARIANT 366 366 D -> H (in dbSNP:rs1800956).
/FTId=VAR_014764.
VARIANT 374 374 K -> E (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070294.
VARIANT 394 394 C -> Y (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070295.
VARIANT 412 412 C -> S (in HHT1).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026781.
VARIANT 413 413 G -> V (in HHT1; dbSNP:rs121918401).
{ECO:0000269|PubMed:10982033}.
/FTId=VAR_037140.
VARIANT 414 414 M -> R (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070296.
VARIANT 437 437 R -> W (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070297.
VARIANT 490 490 L -> S (in HHT1; dbSNP:rs763475207).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070298.
VARIANT 504 504 V -> M (in HHT1; dbSNP:rs116330805).
{ECO:0000269|PubMed:15024723}.
/FTId=VAR_026782.
VARIANT 529 529 R -> H (in HHT1; dbSNP:rs863223538).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070299.
VARIANT 529 529 R -> P (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070300.
VARIANT 545 545 G -> D (in HHT1).
{ECO:0000269|PubMed:16525724}.
/FTId=VAR_070301.
VARIANT 545 545 G -> S (in dbSNP:rs142896669).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070302.
VARIANT 547 547 L -> P (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070303.
VARIANT 549 549 C -> Y (found in a patient with
hereditary hemorrhagic talagiectasia;
unknown pathological significance).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070304.
VARIANT 561 561 D -> A (in dbSNP:rs375965489).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070305.
VARIANT 603 603 G -> R (in HHT1).
{ECO:0000269|PubMed:20414677}.
/FTId=VAR_070306.
VARIANT 604 604 A -> D (in HHT1).
{ECO:0000269|PubMed:16752392}.
/FTId=VAR_070307.
VARIANT 615 615 S -> L (in HHT1; dbSNP:rs148002300).
{ECO:0000269|PubMed:15712270}.
/FTId=VAR_026783.
MUTAGEN 246 246 D->A: No effect on interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 269 269 M->A: Impairs protein folding, but does
not abolish interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 270 271 QI->AA: Loss of interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 277 277 Y->A: No effect on interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 278 278 S->P: Loss of interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 282 282 F->V: Loss of interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 290 290 F->A: No effect on interaction with GDF2.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 350 350 C->S: Impairs protein folding. Impairs
protein folding; when associated with C-
382. {ECO:0000269|PubMed:28564608}.
MUTAGEN 382 382 C->S: Impairs protein folding. Impairs
protein folding; when associated with C-
350. {ECO:0000269|PubMed:28564608}.
MUTAGEN 516 516 C->S: Loss of dimerization via ZP domain.
{ECO:0000269|PubMed:28564608}.
MUTAGEN 650 650 T->A: Loss of interaction with ARRB2.
{ECO:0000269|PubMed:17540773}.
CONFLICT 14 14 L -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 122 130 SSLVTFQEP -> FQPGHLPRA (in Ref. 5).
{ECO:0000305}.
TURN 37 39 {ECO:0000244|PDB:5I04}.
STRAND 40 54 {ECO:0000244|PDB:5I04}.
STRAND 61 70 {ECO:0000244|PDB:5I04}.
STRAND 76 83 {ECO:0000244|PDB:5I04}.
STRAND 94 103 {ECO:0000244|PDB:5I04}.
STRAND 105 111 {ECO:0000244|PDB:5I04}.
STRAND 116 120 {ECO:0000244|PDB:5I04}.
TURN 122 124 {ECO:0000244|PDB:5I04}.
STRAND 125 129 {ECO:0000244|PDB:5I04}.
STRAND 132 137 {ECO:0000244|PDB:5I04}.
HELIX 143 151 {ECO:0000244|PDB:5I04}.
STRAND 156 171 {ECO:0000244|PDB:5I04}.
STRAND 185 189 {ECO:0000244|PDB:5I04}.
STRAND 193 200 {ECO:0000244|PDB:5I04}.
STRAND 205 208 {ECO:0000244|PDB:5I04}.
STRAND 217 224 {ECO:0000244|PDB:5I04}.
STRAND 232 240 {ECO:0000244|PDB:5I04}.
STRAND 249 254 {ECO:0000244|PDB:5I04}.
STRAND 259 267 {ECO:0000244|PDB:5I04}.
STRAND 270 279 {ECO:0000244|PDB:5I04}.
HELIX 296 305 {ECO:0000244|PDB:5I04}.
STRAND 309 327 {ECO:0000244|PDB:5I04}.
HELIX 352 358 {ECO:0000244|PDB:5HZV}.
STRAND 360 363 {ECO:0000244|PDB:5HZV}.
STRAND 365 373 {ECO:0000244|PDB:5HZV}.
HELIX 374 379 {ECO:0000244|PDB:5HZV}.
STRAND 384 388 {ECO:0000244|PDB:5HZV}.
STRAND 400 408 {ECO:0000244|PDB:5HZV}.
STRAND 415 417 {ECO:0000244|PDB:5HZV}.
STRAND 420 431 {ECO:0000244|PDB:5HZV}.
STRAND 436 443 {ECO:0000244|PDB:5HZV}.
TURN 445 447 {ECO:0000244|PDB:5HZV}.
STRAND 448 459 {ECO:0000244|PDB:5HZV}.
STRAND 465 467 {ECO:0000244|PDB:5HZV}.
STRAND 473 481 {ECO:0000244|PDB:5HZV}.
STRAND 484 496 {ECO:0000244|PDB:5HZV}.
TURN 499 501 {ECO:0000244|PDB:5HZV}.
STRAND 503 508 {ECO:0000244|PDB:5HZV}.
STRAND 517 519 {ECO:0000244|PDB:5HZV}.
STRAND 524 526 {ECO:0000244|PDB:5HZV}.
STRAND 529 532 {ECO:0000244|PDB:5HZV}.
STRAND 538 540 {ECO:0000244|PDB:5HZV}.
STRAND 543 555 {ECO:0000244|PDB:5HZV}.
HELIX 560 562 {ECO:0000244|PDB:5HZV}.
STRAND 564 574 {ECO:0000244|PDB:5HZV}.
SEQUENCE 658 AA; 70578 MW; 49CA2CE013298D17 CRC64;
MDRGTLPLAV ALLLASCSLS PTSLAETVHC DLQPVGPERG EVTYTTSQVS KGCVAQAPNA
ILEVHVLFLE FPTGPSQLEL TLQASKQNGT WPREVLLVLS VNSSVFLHLQ ALGIPLHLAY
NSSLVTFQEP PGVNTTELPS FPKTQILEWA AERGPITSAA ELNDPQSILL RLGQAQGSLS
FCMLEASQDM GRTLEWRPRT PALVRGCHLE GVAGHKEAHI LRVLPGHSAG PRTVTVKVEL
SCAPGDLDAV LILQGPPYVS WLIDANHNMQ IWTTGEYSFK IFPEKNIRGF KLPDTPQGLL
GEARMLNASI VASFVELPLA SIVSLHASSC GGRLQTSPAP IQTTPPKDTC SPELLMSLIQ
TKCADDAMTL VLKKELVAHL KCTITGLTFW DPSCEAEDRG DKFVLRSAYS SCGMQVSASM
ISNEAVVNIL SSSSPQRKKV HCLNMDSLSF QLGLYLSPHF LQASNTIEPG QQSFVQVRVS
PSVSEFLLQL DSCHLDLGPE GGTVELIQGR AAKGNCVSLL SPSPEGDPRF SFLLHFYTVP
IPKTGTLSCT VALRPKTGSQ DQEVHRTVFM RLNIISPDLS GCTSKGLVLP AVLGITFGAF
LIGALLTAAL WYIYSHTRSP SKREPVVAVA APASSESSST NHSIGSTQST PCSTSSMA


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1P-298-T025 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 25 tests
11-298-C025 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 0.025 mg
11-298-C100 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 0.1 mg
1F-453-T100 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 100 tests
1F-453-T025 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 25 tests
1A-298-T100 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 100 tests
1A-298-T025 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 25 tests
PB-298-T100 Mouse Monoclonal to CD105 _ Endoglin Antigen CD105 Isotype IgG2a Antigen CD105 Isotype IgG2a 100 tests


 

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