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Protein

Endoglin

Gene

ENG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication5 Publications

GO - Molecular functioni

  • activin binding Source: BHF-UCL
  • galactose binding Source: BHF-UCL
  • glycosaminoglycan binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • transforming growth factor beta-activated receptor activity Source: BHF-UCL
  • transforming growth factor beta binding Source: BHF-UCL
  • transforming growth factor beta receptor, cytoplasmic mediator activity Source: BHF-UCL
  • transmembrane signaling receptor activity Source: BHF-UCL
  • type II transforming growth factor beta receptor binding Source: BHF-UCL
  • type I transforming growth factor beta receptor binding Source: BHF-UCL

GO - Biological processi

  • artery morphogenesis Source: BHF-UCL
  • atrial cardiac muscle tissue morphogenesis Source: BHF-UCL
  • atrioventricular canal morphogenesis Source: BHF-UCL
  • BMP signaling pathway Source: BHF-UCL
  • bone development Source: Ensembl
  • branching involved in blood vessel morphogenesis Source: BHF-UCL
  • cardiac atrium morphogenesis Source: BHF-UCL
  • cardiac ventricle morphogenesis Source: BHF-UCL
  • cell adhesion Source: UniProtKB-KW
  • cell chemotaxis Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cell migration involved in endocardial cushion formation Source: Ensembl
  • cell motility Source: BHF-UCL
  • cellular response to mechanical stimulus Source: Ensembl
  • central nervous system vasculogenesis Source: BHF-UCL
  • chronological cell aging Source: BHF-UCL
  • detection of hypoxia Source: BHF-UCL
  • dorsal aorta morphogenesis Source: BHF-UCL
  • endocardial cushion morphogenesis Source: BHF-UCL
  • epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  • extracellular matrix constituent secretion Source: Ensembl
  • extracellular matrix disassembly Source: BHF-UCL
  • heart looping Source: BHF-UCL
  • negative regulation of cell migration Source: BHF-UCL
  • negative regulation of endothelial cell proliferation Source: BHF-UCL
  • negative regulation of gene expression Source: BHF-UCL
  • negative regulation of nitric-oxide synthase activity Source: BHF-UCL
  • negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • negative regulation of protein autophosphorylation Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • outflow tract septum morphogenesis Source: BHF-UCL
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of BMP signaling pathway Source: BHF-UCL
  • positive regulation of collagen biosynthetic process Source: Ensembl
  • positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of systemic arterial blood pressure Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of vascular smooth muscle cell differentiation Source: BHF-UCL
  • regulation of cell adhesion Source: BHF-UCL
  • regulation of cell proliferation Source: BHF-UCL
  • regulation of phosphorylation Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: HGNC
  • regulation of transforming growth factor beta receptor signaling pathway Source: HGNC
  • response to corticosteroid Source: Ensembl
  • response to drug Source: Ensembl
  • response to hypoxia Source: BHF-UCL
  • response to transforming growth factor beta Source: Ensembl
  • smooth muscle tissue development Source: BHF-UCL
  • transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • vascular smooth muscle cell development Source: BHF-UCL
  • vasculogenesis Source: BHF-UCL
  • venous blood vessel morphogenesis Source: BHF-UCL
  • ventricular trabecula myocardium morphogenesis Source: BHF-UCL
  • wound healing Source: BHF-UCL

Keywordsi

Biological processAngiogenesis, Cell adhesion

Enzyme and pathway databases

SIGNORiP17813.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglin
Alternative name(s):
CD_antigen: CD105
Gene namesi
Name:ENG
Synonyms:END
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000106991.13.
HGNCiHGNC:3349. ENG.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 586ExtracellularSequence analysisAdd BLAST561
Transmembranei587 – 611HelicalSequence analysisAdd BLAST25
Topological domaini612 – 658CytoplasmicSequence analysisAdd BLAST47

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Telangiectasia, hereditary hemorrhagic, 1 (HHT1)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:187300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0267748L → P in HHT1. 1 Publication1
Natural variantiVAR_07027911A → D in HHT1. 1 Publication1
Natural variantiVAR_02677549V → F in HHT1. 1 Publication1
Natural variantiVAR_00519352G → V in HHT1; impairs protein folding; abolishes expression at the cell surface. 2 Publications1
Natural variantiVAR_00519453C → R in HHT1; impairs protein folding; abolishes expression at the cell surface. 3 Publications1
Natural variantiVAR_070280105V → D in HHT1. 1 Publication1
Natural variantiVAR_026776107L → R in HHT1. 1 Publication1
Natural variantiVAR_005195149W → C in HHT1; impairs protein folding; nearly abolishes expression at the cell surface. 2 PublicationsCorresponds to variant dbSNP:rs878853657Ensembl.1
Natural variantiVAR_009120160A → D in HHT1. 1 Publication1
Natural variantiVAR_070282175A → E in HHT1. 1 Publication1
Natural variantiVAR_005196192 – 198Missing in HHT1. 1 Publication7
Natural variantiVAR_070283193 – 194TL → VLQ in HHT1. 1 Publication2
Natural variantiVAR_026777207Missing in HHT1. 1 Publication1
Natural variantiVAR_070285220I → T in HHT1. 1 Publication1
Natural variantiVAR_009121221L → P in HHT1; impairs protein folding; strongly reduces expression at the cell surface. 2 Publications1
Natural variantiVAR_070286221L → Q in HHT1. 1 Publication1
Natural variantiVAR_026778232 – 233Missing in HHT1. 2
Natural variantiVAR_070288238V → E in HHT1. 1 Publication1
Natural variantiVAR_070289263I → S in HHT1. 1 Publication1
Natural variantiVAR_026780263I → T in HHT1. 1 Publication1
Natural variantiVAR_026779263Missing in HHT1. 2 Publications1
Natural variantiVAR_070290269M → R in HHT1. 1 Publication1
Natural variantiVAR_005197306L → P in HHT1. 1 Publication1
Natural variantiVAR_070291308A → D in HHT1. 1 Publication1
Natural variantiVAR_070293363C → S in HHT1. 1 Publication1
Natural variantiVAR_070295394C → Y in HHT1. 1 Publication1
Natural variantiVAR_026781412C → S in HHT1. 1 Publication1
Natural variantiVAR_037140413G → V in HHT1. 1 PublicationCorresponds to variant dbSNP:rs121918401Ensembl.1
Natural variantiVAR_070297437R → W in HHT1. 1 Publication1
Natural variantiVAR_070298490L → S in HHT1. 1 PublicationCorresponds to variant dbSNP:rs763475207Ensembl.1
Natural variantiVAR_026782504V → M in HHT1. 1 PublicationCorresponds to variant dbSNP:rs116330805Ensembl.1
Natural variantiVAR_070299529R → H in HHT1. 1 PublicationCorresponds to variant dbSNP:rs863223538Ensembl.1
Natural variantiVAR_070300529R → P in HHT1. 1 Publication1
Natural variantiVAR_070301545G → D in HHT1. 1 Publication1
Natural variantiVAR_070303547L → P in HHT1. 1 Publication1
Natural variantiVAR_070306603G → R in HHT1. 1 Publication1
Natural variantiVAR_070307604A → D in HHT1. 1 Publication1
Natural variantiVAR_026783615S → L in HHT1. 1 PublicationCorresponds to variant dbSNP:rs148002300Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi246D → A: No effect on interaction with GDF2. 1 Publication1
Mutagenesisi269M → A: Impairs protein folding, but does not abolish interaction with GDF2. 1 Publication1
Mutagenesisi270 – 271QI → AA: Loss of interaction with GDF2. 1 Publication2
Mutagenesisi277Y → A: No effect on interaction with GDF2. 1 Publication1
Mutagenesisi278S → P: Loss of interaction with GDF2. 1 Publication1
Mutagenesisi282F → V: Loss of interaction with GDF2. 1 Publication1
Mutagenesisi290F → A: No effect on interaction with GDF2. 1 Publication1
Mutagenesisi350C → S: Impairs protein folding. Impairs protein folding; when associated with C-382. 1 Publication1
Mutagenesisi382C → S: Impairs protein folding. Impairs protein folding; when associated with C-350. 1 Publication1
Mutagenesisi516C → S: Loss of dimerization via ZP domain. 1 Publication1
Mutagenesisi650T → A: Loss of interaction with ARRB2. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2022.
GeneReviewsiENG.
MalaCardsiENG.
MIMi187300. phenotype.
OpenTargetsiENSG00000106991.
Orphaneti231160. Familial cerebral saccular aneurysm.
329971. Generalized juvenile polyposis/juvenile polyposis coli.
774. Hereditary hemorrhagic telangiectasia.
PharmGKBiPA27785.

Chemistry databases

ChEMBLiCHEMBL3712885.
GuidetoPHARMACOLOGYi2895.

Polymorphism and mutation databases

DMDMi3041681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000002115626 – 658EndoglinAdd BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 207Combined sources1 Publication
Disulfide bondi53 ↔ 182Combined sources1 Publication
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi102N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi121N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi134N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi242 ↔ 330Combined sources1 Publication
Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi350 ↔ 382Combined sources1 Publication
Disulfide bondi363 ↔ 442Combined sources1 Publication
Disulfide bondi394 ↔ 412Combined sources1 Publication
Disulfide bondi493 ↔ 549Combined sources1 Publication
Disulfide bondi516Interchain1 Publication
Modified residuei646Phosphoserine; by TGFBR1By similarity1
Modified residuei649Phosphoserine; by TGFBR1By similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP17813.
PaxDbiP17813.
PeptideAtlasiP17813.
PRIDEiP17813.

PTM databases

iPTMnetiP17813.
PhosphoSitePlusiP17813.
SwissPalmiP17813.

Expressioni

Tissue specificityi

Detected on umbilical veil endothelial cells (PubMed:10625079). Detected in placenta (at protein level) (PubMed:1692830). Detected on endothelial cells (PubMed:1692830).2 Publications

Gene expression databases

BgeeiENSG00000106991.
CleanExiHS_ENG.
ExpressionAtlasiP17813. baseline and differential.
GenevisibleiP17813. HS.

Organism-specific databases

HPAiCAB000096.
CAB072873.
HPA011862.
HPA067440.

Interactioni

Subunit structurei

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).7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • activin binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • transforming growth factor beta binding Source: BHF-UCL
  • type II transforming growth factor beta receptor binding Source: BHF-UCL
  • type I transforming growth factor beta receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108337. 12 interactors.
CORUMiP17813.
DIPiDIP-6246N.
IntActiP17813. 15 interactors.
MINTiMINT-4529566.
STRINGi9606.ENSP00000362299.

Structurei

Secondary structure

1658
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni37 – 39Combined sources3
Beta strandi40 – 54Combined sources15
Beta strandi61 – 70Combined sources10
Beta strandi76 – 83Combined sources8
Beta strandi94 – 103Combined sources10
Beta strandi105 – 111Combined sources7
Beta strandi116 – 120Combined sources5
Turni122 – 124Combined sources3
Beta strandi125 – 129Combined sources5
Beta strandi132 – 137Combined sources6
Helixi143 – 151Combined sources9
Beta strandi156 – 171Combined sources16
Beta strandi185 – 189Combined sources5
Beta strandi193 – 200Combined sources8
Beta strandi205 – 208Combined sources4
Beta strandi217 – 224Combined sources8
Beta strandi232 – 240Combined sources9
Beta strandi249 – 254Combined sources6
Beta strandi259 – 267Combined sources9
Beta strandi270 – 279Combined sources10
Helixi296 – 305Combined sources10
Beta strandi309 – 327Combined sources19
Helixi352 – 358Combined sources7
Beta strandi360 – 363Combined sources4
Beta strandi365 – 373Combined sources9
Helixi374 – 379Combined sources6
Beta strandi384 – 388Combined sources5
Beta strandi400 – 408Combined sources9
Beta strandi415 – 417Combined sources3
Beta strandi420 – 431Combined sources12
Beta strandi436 – 443Combined sources8
Turni445 – 447Combined sources3
Beta strandi448 – 459Combined sources12
Beta strandi465 – 467Combined sources3
Beta strandi473 – 481Combined sources9
Beta strandi484 – 496Combined sources13
Turni499 – 501Combined sources3
Beta strandi503 – 508Combined sources6
Beta strandi517 – 519Combined sources3
Beta strandi524 – 526Combined sources3
Beta strandi529 – 532Combined sources4
Beta strandi538 – 540Combined sources3
Beta strandi543 – 555Combined sources13
Helixi560 – 562Combined sources3
Beta strandi564 – 574Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HZVX-ray2.70A338-581[»]
5HZWX-ray4.45A26-337[»]
5I04X-ray2.42A26-337[»]
ProteinModelPortaliP17813.
SMRiP17813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini363 – 533ZPPROSITE-ProRule annotation1 PublicationAdd BLAST171

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 337Required for interaction with GDF23 PublicationsAdd BLAST312
Regioni26 – 46OR1, N-terminal part1 PublicationAdd BLAST21
Regioni47 – 199OR21 PublicationAdd BLAST153
Regioni200 – 330OR1, C-terminal part1 PublicationAdd BLAST131
Regioni270 – 282Essential for interaction with GDF21 PublicationAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi399 – 401Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi336 – 576Ser/Thr-richAdd BLAST241

Domaini

The ZP domain mediates dimerization.1 Publication
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 GDF2.1 Publication

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IQ57. Eukaryota.
ENOG410YK9H. LUCA.
GeneTreeiENSGT00530000063861.
HOGENOMiHOG000112346.
HOVERGENiHBG005573.
InParanoidiP17813.
KOiK06526.
OMAiDANHNMQ.
OrthoDBiEOG091G030O.
PhylomeDBiP17813.
TreeFamiTF337375.

Family and domain databases

InterProiView protein in InterPro
IPR001507. ZP_dom.
PfamiView protein in Pfam
PF00100. Zona_pellucida. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P17813-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDRGTLPLAV ALLLASCSLS PTSLAETVHC DLQPVGPERG EVTYTTSQVS
60 70 80 90 100
KGCVAQAPNA ILEVHVLFLE FPTGPSQLEL TLQASKQNGT WPREVLLVLS
110 120 130 140 150
VNSSVFLHLQ ALGIPLHLAY NSSLVTFQEP PGVNTTELPS FPKTQILEWA
160 170 180 190 200
AERGPITSAA ELNDPQSILL RLGQAQGSLS FCMLEASQDM GRTLEWRPRT
210 220 230 240 250
PALVRGCHLE GVAGHKEAHI LRVLPGHSAG PRTVTVKVEL SCAPGDLDAV
260 270 280 290 300
LILQGPPYVS WLIDANHNMQ IWTTGEYSFK IFPEKNIRGF KLPDTPQGLL
310 320 330 340 350
GEARMLNASI VASFVELPLA SIVSLHASSC GGRLQTSPAP IQTTPPKDTC
360 370 380 390 400
SPELLMSLIQ TKCADDAMTL VLKKELVAHL KCTITGLTFW DPSCEAEDRG
410 420 430 440 450
DKFVLRSAYS SCGMQVSASM ISNEAVVNIL SSSSPQRKKV HCLNMDSLSF
460 470 480 490 500
QLGLYLSPHF LQASNTIEPG QQSFVQVRVS PSVSEFLLQL DSCHLDLGPE
510 520 530 540 550
GGTVELIQGR AAKGNCVSLL SPSPEGDPRF SFLLHFYTVP IPKTGTLSCT
560 570 580 590 600
VALRPKTGSQ DQEVHRTVFM RLNIISPDLS GCTSKGLVLP AVLGITFGAF
610 620 630 640 650
LIGALLTAAL WYIYSHTRSP SKREPVVAVA APASSESSST NHSIGSTQST

PCSTSSMA
Length:658
Mass (Da):70,578
Last modified:July 15, 1998 - v2
Checksum:i49CA2CE013298D17
GO
Isoform Short (identifier: P17813-2) [UniParc]FASTAAdd to basket

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

Show »
Length:625
Mass (Da):67,542
Checksum:i8D8E510E5CB05812
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14L → G AA sequence (PubMed:1692830).Curated1
Sequence conflicti122 – 130SSLVTFQEP → FQPGHLPRA (PubMed:7894484).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0051925T → M1 PublicationCorresponds to variant dbSNP:rs35400405Ensembl.1
Natural variantiVAR_0267748L → P in HHT1. 1 Publication1
Natural variantiVAR_07027911A → D in HHT1. 1 Publication1
Natural variantiVAR_02677549V → F in HHT1. 1 Publication1
Natural variantiVAR_00519352G → V in HHT1; impairs protein folding; abolishes expression at the cell surface. 2 Publications1
Natural variantiVAR_00519453C → R in HHT1; impairs protein folding; abolishes expression at the cell surface. 3 Publications1
Natural variantiVAR_070280105V → D in HHT1. 1 Publication1
Natural variantiVAR_026776107L → R in HHT1. 1 Publication1
Natural variantiVAR_005195149W → C in HHT1; impairs protein folding; nearly abolishes expression at the cell surface. 2 PublicationsCorresponds to variant dbSNP:rs878853657Ensembl.1
Natural variantiVAR_070281150A → P Found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 Publication1
Natural variantiVAR_009120160A → D in HHT1. 1 Publication1
Natural variantiVAR_070282175A → E in HHT1. 1 Publication1
Natural variantiVAR_005196192 – 198Missing in HHT1. 1 Publication7
Natural variantiVAR_070283193 – 194TL → VLQ in HHT1. 1 Publication2
Natural variantiVAR_070284205R → P1 Publication1
Natural variantiVAR_026777207Missing in HHT1. 1 Publication1
Natural variantiVAR_070285220I → T in HHT1. 1 Publication1
Natural variantiVAR_009121221L → P in HHT1; impairs protein folding; strongly reduces expression at the cell surface. 2 Publications1
Natural variantiVAR_070286221L → Q in HHT1. 1 Publication1
Natural variantiVAR_026778232 – 233Missing in HHT1. 2
Natural variantiVAR_070287236V → M Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs754136153Ensembl.1
Natural variantiVAR_070288238V → E in HHT1. 1 Publication1
Natural variantiVAR_070289263I → S in HHT1. 1 Publication1
Natural variantiVAR_026780263I → T in HHT1. 1 Publication1
Natural variantiVAR_026779263Missing in HHT1. 2 Publications1
Natural variantiVAR_070290269M → R in HHT1. 1 Publication1
Natural variantiVAR_005197306L → P in HHT1. 1 Publication1
Natural variantiVAR_070291308A → D in HHT1. 1 Publication1
Natural variantiVAR_070292315V → M Found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763508329Ensembl.1
Natural variantiVAR_070293363C → S in HHT1. 1 Publication1
Natural variantiVAR_014764366D → H. Corresponds to variant dbSNP:rs1800956Ensembl.1
Natural variantiVAR_070294374K → E Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 Publication1
Natural variantiVAR_070295394C → Y in HHT1. 1 Publication1
Natural variantiVAR_026781412C → S in HHT1. 1 Publication1
Natural variantiVAR_037140413G → V in HHT1. 1 PublicationCorresponds to variant dbSNP:rs121918401Ensembl.1
Natural variantiVAR_070296414M → R Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 Publication1
Natural variantiVAR_070297437R → W in HHT1. 1 Publication1
Natural variantiVAR_070298490L → S in HHT1. 1 PublicationCorresponds to variant dbSNP:rs763475207Ensembl.1
Natural variantiVAR_026782504V → M in HHT1. 1 PublicationCorresponds to variant dbSNP:rs116330805Ensembl.1
Natural variantiVAR_070299529R → H in HHT1. 1 PublicationCorresponds to variant dbSNP:rs863223538Ensembl.1
Natural variantiVAR_070300529R → P in HHT1. 1 Publication1
Natural variantiVAR_070301545G → D in HHT1. 1 Publication1
Natural variantiVAR_070302545G → S1 PublicationCorresponds to variant dbSNP:rs142896669Ensembl.1
Natural variantiVAR_070303547L → P in HHT1. 1 Publication1
Natural variantiVAR_070304549C → Y Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance. 1 Publication1
Natural variantiVAR_070305561D → A1 PublicationCorresponds to variant dbSNP:rs375965489Ensembl.1
Natural variantiVAR_070306603G → R in HHT1. 1 Publication1
Natural variantiVAR_070307604A → D in HHT1. 1 Publication1
Natural variantiVAR_026783615S → L in HHT1. 1 PublicationCorresponds to variant dbSNP:rs148002300Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004233619 – 658SPSKR…TSSMA → EYPRPPQ in isoform Short. 1 PublicationAdd BLAST40

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72012 mRNA. Translation: CAA50891.1.
AL157935 Genomic DNA. No translation available.
AL162586 Genomic DNA. No translation available.
CH471090 Genomic DNA. Translation: EAW87702.1.
J05481 mRNA. Translation: AAA35800.1.
U37439
, AF036969, U37447, AF036970, U37446, U37445, AF036971, U37442, U37441 Genomic DNA. Translation: AAC63386.1.
CCDSiCCDS48029.1. [P17813-1]
CCDS6880.1. [P17813-2]
PIRiS50831.
RefSeqiNP_000109.1. NM_000118.3. [P17813-2]
NP_001108225.1. NM_001114753.2. [P17813-1]
NP_001265067.1. NM_001278138.1.
UniGeneiHs.76753.

Genome annotation databases

EnsembliENST00000344849; ENSP00000341917; ENSG00000106991. [P17813-2]
ENST00000373203; ENSP00000362299; ENSG00000106991. [P17813-1]
GeneIDi2022.
KEGGihsa:2022.
UCSCiuc004bsj.6. human. [P17813-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiEGLN_HUMAN
AccessioniPrimary (citable) accession number: P17813
Secondary accession number(s): Q14248, Q14926, Q5T9C0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 15, 1998
Last modified: November 22, 2017
This is version 190 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references