Protein detail

EGLN

Endoglin (CD antigen CD105)

Protein symbol
EGLN
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
1
Protein classification
Cancer-related genesCandidate cardiovascular disease genesCD markersDisease related genesHuman disease related genesPlasma proteinsPredicted membrane proteins
Basic Information
Protein Names
Endoglin (CD antigen CD105)
Protein Class
Cancer-related genesCandidate cardiovascular disease genesCD markersDisease related genesHuman disease related genesPlasma proteinsPredicted membrane proteins
Protein Function
  • CD markers
  • Candidate cardiovascular disease genes
  • Human disease related genes:Congenital malformations:Congenital malformations of the circulatory system
  • Cancer-related genes:Candidate cancer biomarkers
  • Disease related genes
Transmembrane
587..611; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
CD105ENDHHT1ORWORW1
Gene Description
Endoglin
Chromosome
9
Position
127815013-127854658
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Cell SpecificEarly spermatids
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

10 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ENGSRCP12931Y612phosphorylationPhosphoSite
ENGSRCP12931Y614phosphorylationPhosphoSite
ENGTGFBR2P37173S634phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGTGFBR2P37173S635phosphorylationPhosphoSite_MIMPMIMPProtMapperRLIMS-P_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:16785228
ENGACVRL1P37023S646phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGACVRL1P37023T640phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGACVRL1P37023T654phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGACVRL1P37023S649phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGTGFBR1P36897S646phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
ENGTGFBR1P36897S649phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper

Ligand-Receptor Signaling

37 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
extracellularextracellularDGIdbNoNoNoYesNo
extracellularextracellularOmniPathNoNoNoYesNo
intracellularintracellularLOCATENoNoNoYesNo
intracellularintracellularGO_IntercellNoNoNoYesNo
intracellularintracellularOmniPathNoNoNoYesNo
activating_cofactorreceptor_regulatorCellChatDBYesNoNoYesNo
receptor_regulatorreceptor_regulatorOmniPathYesNoNoYesNo
growth_factor_binderligand_regulatorGO_IntercellYesNoNoYesNo
ligand_regulatorligand_regulatorOmniPathYesNoNoYesNo
adhesionadhesionAdhesomeYesYesNoYesNo
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Regulatory Interaction Network

4 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
EGLNP17813GDF2Q9UK05YesYesNoWangSIGNORIntActIntAct:28564608SIGNOR:21737454
SRCP12931EGLNP17813YesNoYesPhosphoSite_norefSIGNORProtMapperPhosphoSitePhosphoSite_ProtMapperSIGNOR:25070888PhosphoSite:25070888
EGLNP17813BMP10O95393YesYesNoSIGNORSIGNOR:21737454
ACVL1P37023EGLNP17813YesNoNoPhosphoSite_MIMPMIMPPhosphoSite_norefiPTMnetProtMapperHINTInnateDBDIPWangPhosphoSitePhosphoSite_ProtMapperHINT:16785228PhosphoSite:16785228HINT:23868260PhosphoSite:20042635HINT:28564608InnateDB:18333754HINT:10767348HINT:18333754InnateDB:16785228DIP:10767348DIP:23868260InnateDB:15702480HINT:15702480

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationELISA3373224754130796838207106
Sequence, Structure & Domains

Sequences

Length
658
Mass
70,578
Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=Long; IsoId=P17813-1; Sequence=Displayed; Name=Short; IsoId=P17813-2; Sequence=VSP_004233
Alternative Sequence
619..658; SPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA -> EYPRPPQ (in isoform Short)

3D Structural Models

Turn
37..39; 122..124; 445..447; 499..501
Helix
143..151; 296..305; 352..358; 374..379; 560..562
Beta Strand
40..54; 61..70; 76..83; 94..103; 105..111; 116..120; 125..129; 132..137; 156..171; 185..189; 193..200; 205..208; 217..224; 232..240; 249..254; 259..267; 270..279; 309..327; 360..363; 365..373; 384..388; 400..408; 415..417; 420..431; 436..443; 448..459; 465..467; 473..481; 484..496; 503..508; 517..519; 524..526; 529..532; 538..540; 543..555; 564..574
3D Structure
X-ray crystallography (3)

Domain & Motif Annotations

Compositional Bias
626..639; Low complexity; 640..658; Polar residues
Motif
399..401; Cell attachment site
Domain (CC)
The ZP domain mediates dimerization.; 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..
Domain (FT)
363..533; ZP
Region
26..337; Required for interaction with GDF2; 26..46; OR1, N-terminal part; 47..199; OR2; 200..330; OR1, C-terminal part; 270..282; Essential for interaction with GDF2; 626..658; Disordered
Clinical Relevance