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P17813 (EGLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglin
Alternative name(s):
CD_antigen=CD105
Gene names
Name:ENG
Synonyms:END
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major glycoprotein of vascular endothelium. Involved in the regulation of angiogenesis. May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGF-beta1 signaling through SMAD3. Ref.9 Ref.11

Subunit structure

Homodimer that forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and/or TGFBR2. It is able to bind TGF-beta 1, and 3 efficiently and TGF-beta 2 less efficiently. Interacts with TCTEX1D4. Interacts with ARRB2. Interacts with GDF2. Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Endoglin is restricted to endothelial cells in all tissues except bone marrow.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement PubMed 11382917. Source: BHF-UCL

artery morphogenesis

Inferred from sequence or structural similarity PubMed 8194490. Source: BHF-UCL

bone development

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell chemotaxis

Inferred from mutant phenotype PubMed 18223685. Source: BHF-UCL

cell migration

Inferred from mutant phenotype PubMed 18223685. Source: BHF-UCL

cell migration involved in endocardial cushion formation

Inferred from electronic annotation. Source: Ensembl

cell motility

Inferred from mutant phenotype PubMed 18223685. Source: BHF-UCL

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

central nervous system vasculogenesis

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

chronological cell aging

Inferred from electronic annotation. Source: Ensembl

detection of hypoxia

Inferred from direct assay PubMed 18156205PubMed 18156205. Source: BHF-UCL

extracellular matrix constituent secretion

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Inferred from mutant phenotype PubMed 18223685. Source: BHF-UCL

heart looping

Inferred from sequence or structural similarity PubMed 8194490. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay PubMed 12015308. Source: GOC

negative regulation of cell migration

Inferred from direct assay PubMed 19736306. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 18974388. Source: BHF-UCL

negative regulation of nitric-oxide synthase activity

Inferred from mutant phenotype PubMed 18974388. Source: BHF-UCL

negative regulation of pathway-restricted SMAD protein phosphorylation

Inferred from mutant phenotype PubMed 18974388. Source: BHF-UCL

negative regulation of protein autophosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18974388PubMed 18974388. Source: BHF-UCL

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement PubMed 11382917PubMed 11382917. Source: BHF-UCL

patterning of blood vessels

Inferred from sequence or structural similarity PubMed 8194490. Source: BHF-UCL

positive regulation of BMP signaling pathway

Inferred from direct assay PubMed 17068149. Source: BHF-UCL

positive regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

positive regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 18974388. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18974388PubMed 18974388. Source: BHF-UCL

regulation of cell adhesion

Traceable author statement PubMed 11382917PubMed 11382917. Source: BHF-UCL

regulation of cell proliferation

Traceable author statement PubMed 11382917PubMed 11382917. Source: BHF-UCL

regulation of phosphorylation

Traceable author statement PubMed 11382917PubMed 11382917. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 15702480. Source: HGNC

regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 15702480. Source: HGNC

response to corticosteroid

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from direct assay PubMed 18156205PubMed 18156205. Source: BHF-UCL

response to statin

Inferred from electronic annotation. Source: Ensembl

response to transforming growth factor beta

Inferred from electronic annotation. Source: Ensembl

smooth muscle tissue development

Inferred from sequence or structural similarity PubMed 8194490. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 18223685. Source: BHF-UCL

vasculogenesis

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

venous blood vessel morphogenesis

Inferred from sequence or structural similarity PubMed 8194490. Source: BHF-UCL

wound healing

Inferred from mutant phenotype PubMed 18223685. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 18223685PubMed 18223685. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

endothelial microparticle

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay PubMed 1537377. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 19004009. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: HPA

transforming growth factor beta receptor homodimeric complex

Inferred by curator PubMed 1326540. Source: BHF-UCL

   Molecular_functionactivin binding

Traceable author statement PubMed 11382917. Source: BHF-UCL

galactose binding

Inferred from direct assay PubMed 3262645. Source: BHF-UCL

glycosaminoglycan binding

Inferred from direct assay PubMed 3262645. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 20856203PubMed 22940691. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: BHF-UCL

transforming growth factor beta binding

Inferred from physical interaction PubMed 1326540Ref.1. Source: BHF-UCL

transforming growth factor beta receptor, cytoplasmic mediator activity

Inferred from direct assay PubMed 12015308. Source: BHF-UCL

transforming growth factor beta-activated receptor activity

Inferred from direct assay PubMed 18223685. Source: BHF-UCL

transmembrane signaling receptor activity

Non-traceable author statement PubMed 18974388. Source: BHF-UCL

type I transforming growth factor beta receptor binding

Inferred from physical interaction PubMed 12015308PubMed 18974388PubMed 18974388. Source: BHF-UCL

type II transforming growth factor beta receptor binding

Inferred from physical interaction PubMed 12015308. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P17813-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P17813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     619-658: SPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA → EYPRPPQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.4
Chain26 – 658633Endoglin
PRO_0000021156

Regions

Topological domain26 – 586561Extracellular Potential
Transmembrane587 – 61125Helical; Potential
Topological domain612 – 65847Cytoplasmic Potential
Region26 – 337312Required for interaction with EGL
Motif399 – 4013Cell attachment site Potential
Compositional bias336 – 576241Ser/Thr-rich

Amino acid modifications

Modified residue6461Phosphoserine; by TGFBR1 By similarity
Modified residue6491Phosphoserine; by TGFBR1 By similarity
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Ref.8
Glycosylation3071N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence619 – 65840SPSKR…TSSMA → EYPRPPQ in isoform Short.
VSP_004233
Natural variant51T → M. Ref.12
Corresponds to variant rs35400405 [ dbSNP | Ensembl ].
VAR_005192
Natural variant81L → P in HHT1. Ref.18
VAR_026774
Natural variant111A → D in HHT1. Ref.20
VAR_070279
Natural variant491V → F in HHT1. Ref.18
VAR_026775
Natural variant521G → V in HHT1. Ref.14 Ref.15
VAR_005193
Natural variant531C → R in HHT1. Ref.14 Ref.15 Ref.17
VAR_005194
Natural variant1051V → D in HHT1. Ref.20
VAR_070280
Natural variant1071L → R in HHT1. Ref.18
VAR_026776
Natural variant1491W → C in HHT1. Ref.14 Ref.15
VAR_005195
Natural variant1501A → P Found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070281
Natural variant1601A → D in HHT1. Ref.13
VAR_009120
Natural variant1751A → E in HHT1. Ref.20
VAR_070282
Natural variant192 – 1987Missing in HHT1.
VAR_005196
Natural variant193 – 1942TL → VLQ in HHT1.
VAR_070283
Natural variant2051R → P. Ref.22
VAR_070284
Natural variant2071Missing in HHT1. Ref.18
VAR_026777
Natural variant2201I → T in HHT1. Ref.20
VAR_070285
Natural variant2211L → P in HHT1. Ref.15 Ref.19
VAR_009121
Natural variant2211L → Q in HHT1. Ref.22
VAR_070286
Natural variant232 – 2332Missing in HHT1.
VAR_026778
Natural variant2361V → M Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070287
Natural variant2381V → E in HHT1. Ref.22
VAR_070288
Natural variant2631I → S in HHT1. Ref.22
VAR_070289
Natural variant2631I → T in HHT1. Ref.18
VAR_026780
Natural variant2631Missing in HHT1. Ref.18 Ref.19
VAR_026779
Natural variant2691M → R in HHT1. Ref.22
VAR_070290
Natural variant3061L → P in HHT1. Ref.14
VAR_005197
Natural variant3081A → D in HHT1. Ref.20
VAR_070291
Natural variant3151V → M Found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070292
Natural variant3631C → S in HHT1. Ref.20
VAR_070293
Natural variant3661D → H.
Corresponds to variant rs1800956 [ dbSNP | Ensembl ].
VAR_014764
Natural variant3741K → E Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070294
Natural variant3941C → Y in HHT1. Ref.22
VAR_070295
Natural variant4121C → S in HHT1. Ref.18
VAR_026781
Natural variant4131G → V in HHT1. Ref.16
VAR_037140
Natural variant4141M → R Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070296
Natural variant4371R → W in HHT1. Ref.20
VAR_070297
Natural variant4901L → S in HHT1. Ref.20
VAR_070298
Natural variant5041V → M in HHT1. Ref.18
Corresponds to variant rs116330805 [ dbSNP | Ensembl ].
VAR_026782
Natural variant5291R → H in HHT1. Ref.20
VAR_070299
Natural variant5291R → P in HHT1. Ref.22
VAR_070300
Natural variant5451G → D in HHT1. Ref.21
VAR_070301
Natural variant5451G → S. Ref.22
VAR_070302
Natural variant5471L → P in HHT1. Ref.20
VAR_070303
Natural variant5491C → Y Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. Ref.22
VAR_070304
Natural variant5611D → A. Ref.22
VAR_070305
Natural variant6031G → R in HHT1. Ref.22
VAR_070306
Natural variant6041A → D in HHT1. Ref.20
VAR_070307
Natural variant6151S → L in HHT1. Ref.19
VAR_026783

Experimental info

Sequence conflict141L → G AA sequence Ref.4
Sequence conflict122 – 1309SSLVTFQEP → FQPGHLPRA Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 49CA2CE013298D17

FASTA65870,578
        10         20         30         40         50         60 
MDRGTLPLAV ALLLASCSLS PTSLAETVHC DLQPVGPERG EVTYTTSQVS KGCVAQAPNA 

        70         80         90        100        110        120 
ILEVHVLFLE FPTGPSQLEL TLQASKQNGT WPREVLLVLS VNSSVFLHLQ ALGIPLHLAY 

       130        140        150        160        170        180 
NSSLVTFQEP PGVNTTELPS FPKTQILEWA AERGPITSAA ELNDPQSILL RLGQAQGSLS 

       190        200        210        220        230        240 
FCMLEASQDM GRTLEWRPRT PALVRGCHLE GVAGHKEAHI LRVLPGHSAG PRTVTVKVEL 

       250        260        270        280        290        300 
SCAPGDLDAV LILQGPPYVS WLIDANHNMQ IWTTGEYSFK IFPEKNIRGF KLPDTPQGLL 

       310        320        330        340        350        360 
GEARMLNASI VASFVELPLA SIVSLHASSC GGRLQTSPAP IQTTPPKDTC SPELLMSLIQ 

       370        380        390        400        410        420 
TKCADDAMTL VLKKELVAHL KCTITGLTFW DPSCEAEDRG DKFVLRSAYS SCGMQVSASM 

       430        440        450        460        470        480 
ISNEAVVNIL SSSSPQRKKV HCLNMDSLSF QLGLYLSPHF LQASNTIEPG QQSFVQVRVS 

       490        500        510        520        530        540 
PSVSEFLLQL DSCHLDLGPE GGTVELIQGR AAKGNCVSLL SPSPEGDPRF SFLLHFYTVP 

       550        560        570        580        590        600 
IPKTGTLSCT VALRPKTGSQ DQEVHRTVFM RLNIISPDLS GCTSKGLVLP AVLGITFGAF 

       610        620        630        640        650 
LIGALLTAAL WYIYSHTRSP SKREPVVAVA APASSESSST NHSIGSTQST PCSTSSMA 

« Hide

Isoform Short [UniParc].

Checksum: 8D8E510E5CB05812
Show »

FASTA62567,542

References

« Hide 'large scale' references
[1]"Identification and expression of two forms of the human transforming growth factor-beta-binding protein endoglin with distinct cytoplasmic regions."
Bellon T., Corbi A., Lastres P., Cales C., Cebrian M., Vera S., Cheifetz S., Massague J., Letarte M., Bernabeu C.
Eur. J. Immunol. 23:2340-2345(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Primary structure of endoglin, an RGD-containing glycoprotein of human endothelial cells."
Gougos A., Letarte M.
J. Biol. Chem. 265:8361-8364(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 14-658, PROTEIN SEQUENCE OF 26-36 (ISOFORM LONG).
Tissue: Umbilical vein.
[5]"Endoglin, a TGF-beta binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1."
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.
Nat. Genet. 8:345-351(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-378.
[6]"Identification of Tctex2beta, a novel dynein light chain family member that interacts with different transforming growth factor-beta receptors."
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.
J. Biol. Chem. 281:37069-37080(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TCTEX1D4.
[7]"The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells."
Lee N.Y., Blobe G.C.
J. Biol. Chem. 282:21507-21517(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134.
Tissue: Liver.
[9]"Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10 via its orphan domain, inhibits blood vessel formation, and suppresses tumor growth."
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.
J. Biol. Chem. 286:30034-30046(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GDF2.
[10]"Structural and functional insights into endoglin ligand recognition and binding."
Alt A., Miguel-Romero L., Donderis J., Aristorena M., Blanco F.J., Round A., Rubio V., Bernabeu C., Marina A.
PLoS ONE 7:E29948-E29948(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GDF2.
[11]"Endoglin requirement for BMP9 signaling in endothelial cells reveals new mechanism of action for selective anti-endoglin antibodies."
Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J., Wickramasinghe D., Ruefli-Brasse A.
PLoS ONE 7:E50920-E50920(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Characterization of endoglin and identification of novel mutations in hereditary hemorrhagic telangiectasia."
Shovlin C.L., Hughes J.M.B., Scott J., Seidman C.E., Seidman J.G.
Am. J. Hum. Genet. 61:68-79(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHT1 192-ARG--PRO-198 DEL, VARIANT MET-5.
[13]"A novel missense mutation in the endoglin gene in hereditary hemorrhagic telangiectasia."
Yamaguchi H., Azuma H., Shigekiyo T., Inoue H., Saito S.
Thromb. Haemost. 77:243-247(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHT1 ASP-160.
[14]"Mutation and expression analysis of the endoglin gene in hereditary hemorrhagic telangiectasia reveals null alleles."
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.
Hum. Mutat. 11:286-294(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-306.
[15]"Expression analysis of four endoglin missense mutations suggests that haploinsufficiency is the predominant mechanism for hereditary hemorrhagic telangiectasia type 1."
Pece-Barbara N., Cymerman U., Vera S., Marchuk D.A., Letarte M.
Hum. Mol. Genet. 8:2171-2181(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHT1 VAL-52; ARG-53; CYS-149 AND PRO-221.
[16]"Two common endoglin mutations in families with hereditary hemorrhagic telangiectasia in the Netherlands Antilles: evidence for a founder effect."
Gallione C.J., Scheessele E.A., Reinhardt D., Duits A.J., Berg J.N., Westermann C.J.J., Marchuk D.A.
Hum. Genet. 107:40-44(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHT1 VAL-413.
[17]"Identification of hereditary hemorrhagic telangiectasia type 1 in newborns by protein expression and mutation analysis of endoglin."
Cymerman U., Vera S., Pece-Barbara N., Bourdeau A., White R.I. Jr., Dunn J., Letarte M.
Pediatr. Res. 47:24-35(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HHT1 ARG-53.
[18]"Molecular screening of ALK1/ACVRL1 and ENG genes in hereditary hemorrhagic telangiectasia in France."
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.
Hum. Mutat. 23:289-299(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[19]"Hepatic manifestation is associated with ALK1 in hereditary hemorrhagic telangiectasia: identification of five novel ALK1 and one novel ENG mutations."
Kuehl H.K.A., Caselitz M., Hasenkamp S., Wagner S., El-Harith E.-H.A., Manns M.P., Stuhrmann M.
Hum. Mutat. 25:320-320(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHT1 PRO-221; ILE-263 DEL AND LEU-615.
[20]"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."
Bossler A.D., Richards J., George C., Godmilow L., Ganguly A.
Hum. Mutat. 27:667-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[21]"Novel mutations in the ENG and ACVRL1 genes causing hereditary hemorrhagic teleangiectasia."
Argyriou L., Twelkemeyer S., Panchulidze I., Wehner L.E., Teske U., Engel W., Nayernia K.
Int. J. Mol. Med. 17:655-659(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHT1 193-THR-LEU-194 DELINS VAL-LEU-GLN AND ASP-545.
[22]"Update on molecular diagnosis of hereditary hemorrhagic telangiectasia."
Richards-Yutz J., Grant K., Chao E.C., Walther S.E., Ganguly A.
Hum. Genet. 128:61-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-150; PRO-205; MET-236; MET-315; GLU-374; ARG-414; SER-545; TYR-549 AND ALA-561, VARIANTS HHT1 GLN-221; GLU-238; SER-263; ARG-269; TYR-394; PRO-529 AND ARG-603.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72012 mRNA. Translation: CAA50891.1.
AL157935, AL162586 Genomic DNA. Translation: CAI12604.1.
AL162586, AL157935 Genomic DNA. Translation: CAI39764.1.
CH471090 Genomic DNA. Translation: EAW87702.1.
J05481 mRNA. Translation: AAA35800.1.
U37439 expand/collapse EMBL AC list , AF036969, U37447, AF036970, U37446, U37445, AF036971, U37442, U37441 Genomic DNA. Translation: AAC63386.1.
CCDSCCDS48029.1. [P17813-1]
CCDS6880.1. [P17813-2]
PIRS50831.
RefSeqNP_000109.1. NM_000118.3. [P17813-2]
NP_001108225.1. NM_001114753.2. [P17813-1]
NP_001265067.1. NM_001278138.1.
UniGeneHs.76753.

3D structure databases

ProteinModelPortalP17813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108337. 12 interactions.
DIPDIP-6246N.
IntActP17813. 8 interactions.
MINTMINT-4529566.
STRING9606.ENSP00000362299.

PTM databases

PhosphoSiteP17813.

Polymorphism databases

DMDM3041681.

Proteomic databases

MaxQBP17813.
PaxDbP17813.
PRIDEP17813.

Protocols and materials databases

DNASU2022.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344849; ENSP00000341917; ENSG00000106991. [P17813-2]
ENST00000373203; ENSP00000362299; ENSG00000106991. [P17813-1]
GeneID2022.
KEGGhsa:2022.
UCSCuc004bsj.5. human. [P17813-1]

Organism-specific databases

CTD2022.
GeneCardsGC09M130577.
GeneReviewsENG.
HGNCHGNC:3349. ENG.
HPACAB000096.
HPA011862.
MIM131195. gene.
187300. phenotype.
neXtProtNX_P17813.
Orphanet231160. Familial cerebral saccular aneurysm.
329971. Generalized juvenile polyposis/juvenile polyposis coli.
774. Hereditary hemorrhagic telangiectasia.
PharmGKBPA27785.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46276.
HOGENOMHOG000112346.
HOVERGENHBG005573.
InParanoidP17813.
KOK06526.
OMAHCDLQPV.
OrthoDBEOG70S754.
PhylomeDBP17813.
TreeFamTF337375.

Gene expression databases

ArrayExpressP17813.
BgeeP17813.
CleanExHS_ENG.
GenevestigatorP17813.

Family and domain databases

InterProIPR001507. ZP_dom.
[Graphical view]
PfamPF00100. Zona_pellucida. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENG. human.
GeneWikiEndoglin.
GenomeRNAi2022.
NextBio8193.
PROP17813.
SOURCESearch...

Entry information

Entry nameEGLN_HUMAN
AccessionPrimary (citable) accession number: P17813
Secondary accession number(s): Q14248, Q14926, Q5T9C0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries