Q9ULI3 · HEG1_HUMAN

  • Protein
    Protein HEG homolog 1
  • Gene
    HEG1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell-cell junction
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Biological Processcardiac atrium morphogenesis
Biological Processcardiac muscle tissue growth
Biological Processcell-cell junction organization
Biological Processendothelial cell morphogenesis
Biological Processheart development
Biological Processin utero embryonic development
Biological Processlung development
Biological Processlymph circulation
Biological Processlymph vessel development
Biological Processmulticellular organism growth
Biological Processnegative regulation of membrane permeability
Biological Processnegative regulation of Rho protein signal transduction
Biological Processnegative regulation of Rho-dependent protein serine/threonine kinase activity
Biological Processpericardium development
Biological Processpositive regulation of fibroblast growth factor production
Biological Processpost-embryonic development
Biological Processprotein localization to cell junction
Biological Processregulation of body fluid levels
Biological Processvasculogenesis
Biological Processvenous blood vessel morphogenesis
Biological Processventricular septum development
Biological Processventricular trabecula myocardium morphogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein HEG homolog 1

Gene names

    • Name
      HEG1
    • Synonyms
      KIAA1237

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9ULI3
  • Secondary accessions
    • Q6NX66
    • Q8NC40
    • Q9BSV0

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Cell membrane
; Single-pass type I membrane protein
Cell junction

Isoform 2

Secreted

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain30-1248Extracellular
Transmembrane1249-1269Helical
Topological domain1270-1381Cytoplasmic

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_048984145in dbSNP:rs4404487
Natural variantVAR_059269305in dbSNP:rs2981546
Natural variantVAR_032253602in dbSNP:rs6790837
Natural variantVAR_032254980in dbSNP:rs10804567
Natural variantVAR_0322551039in dbSNP:rs6438869

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,480 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
Signal1-29UniProt
ChainPRO_000028698130-1381UniProtProtein HEG homolog 1
Glycosylation67UniProtO-linked (GalNAc...) threonine
Glycosylation123UniProtN-linked (GlcNAc...) asparagine
Glycosylation159UniProtN-linked (GlcNAc...) asparagine
Glycosylation180UniProtN-linked (GlcNAc...) asparagine
Glycosylation314UniProtN-linked (GlcNAc...) asparagine
Glycosylation462UniProtN-linked (GlcNAc...) asparagine
Glycosylation520UniProtN-linked (GlcNAc...) asparagine
Glycosylation610UniProtN-linked (GlcNAc...) asparagine
Disulfide bond989↔1000UniProt
Disulfide bond994↔1011UniProt
Disulfide bond1013↔1022UniProt
Disulfide bond1029↔1040UniProt
Disulfide bond1034↔1049UniProt
Disulfide bond1051↔1062UniProt
Glycosylation1137UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)1293PRIDEPhosphoserine
Modified residue (large scale data)1319PRIDEPhosphoserine
Modified residue (large scale data)1330PRIDEPhosphotyrosine
Modified residue (large scale data)1332PRIDEPhosphoserine
Modified residue (large scale data)1347PRIDEPhosphotyrosine
Modified residue1359UniProtPhosphoserine
Modified residue (large scale data)1359PRIDEPhosphoserine
Modified residue (large scale data)1366PRIDEPhosphotyrosine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates interaction with CCM2.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9ULI3KRIT1 O005226EBI-12734419, EBI-1573121

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region24-108Disordered
Compositional bias55-69Basic and acidic residues
Region301-325Disordered
Region376-447Disordered
Compositional bias402-445Polar residues
Compositional bias491-527Polar residues
Region491-529Disordered
Region612-680Disordered
Region706-757Disordered
Region774-830Disordered
Domain985-1023EGF-like 1
Domain1025-1063EGF-like 2; calcium-binding

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q9ULI3-1

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.

  • Length
    1,381
  • Mass (Da)
    147,461
  • Last updated
    2007-05-15 v3
  • Checksum
    2E8402AC5227F95C
MASPRASRWPPPLLLLLLPLLLLPPAAPGTRDPPPSPARRALSLAPLAGAGLELQLERRPEREPPPTPPRERRGPATPGPSYRAPEPGAATQRGPSGRAPRGGSADAAWKHWPESNTEAHVENITFYQNQEDFSTVSSKEGVMVQTSGKSHAASDAPENLTLLAETADARGRSGSSSRTNFTILPVGYSLEIATALTSQSGNLASESLHLPSSSSEFDERIAAFQTKSGTASEMGTERAMGLSEEWTVHSQEATTSAWSPSFLPALEMGELTTPSRKRNSSGPDLSWLHFYRTAASSPLLDLSSSSESTEKLNNSTGLQSSSVSQTKTMHVATVFTDGGPRTLRSLTVSLGPVSKTEGFPKDSRIATTSSSVLLSPSAVESRRNSRVTGNPGDEEFIEPSTENEFGLTSLRWQNDSPTFGEHQLASSSEVQNGSPMSQTETVSRSVAPMRGGEITAHWLLTNSTTSADVTGSSASYPEGVNASVLTQFSDSTVQSGGSHTALGDRSYSESSSTSSSESLNSSAPRGERSIAGISYGQVRGTAIEQRTSSDHTDHTYLSSTFTKGERALLSITDNSSSSDIVESSTSYIKISNSSHSEYSSFFHAQTERSNISSYDGEYAQPSTESPVLHTSNLPSYTPTINMPNTSVVLDTDAEFVSDSSSSSSSSSSSSSSGPPLPLPSVSQSHHLFSSILPSTRASVHLLKSTSDASTPWSSSPSPLPVSLTTSTSAPLSVSQTTLPQSSSTPVLPRARETPVTSFQTSTMTSFMTMLHSSQTADLKSQSTPHQEKVITESKSPSLVSLPTESTKAVTTNSPLPPSLTESSTEQTLPATSTNLAQMSPTFTTTILKTSQPLMTTPGTLSSTASLVTGPIAVQTTAGKQLSLTHPEILVPQISTEGGISTERNRVIVDATTGLIPLTSVPTSAKEMTTKLGVTAEYSPASRSLGTSPSPQTTVVSTAEDLAPKSATFAVQSSTQSPTTVSSSASVNSCAVNPCLHNGECVADNTSRGYHCRCPPSWQGDDCSVDVNECLSNPCPSTAMCNNTQGSFICKCPVGYQLEKGICNLVRTFVTEFKLKRTFLNTTVEKHSDLQEVENEITKTLNMCFSALPSYIRSTVHASRESNAVVISLQTTFSLASNVTLFDLADRMQKCVNSCKSSAEVCQLLGSQRRIFRAGSLCKRKSPECDKDTSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGIALIVTCCRKNKNDISKLIFKSGDFQMSPYAEYPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTSVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF

Q9ULI3-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 986-1012: VNSCAVNPCLHNGECVADNTSRGYHCR → GKTQSHKHMLTARPSPALRATWGSGFM
    • 1013-1381: Missing

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H7C4K2H7C4K2_HUMANHEG163
A0A994J6K3A0A994J6K3_HUMANHEG11481

Sequence caution

The sequence AAH67235.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAC11336.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias55-69Basic and acidic residues
Compositional bias402-445Polar residues
Compositional bias491-527Polar residues
Alternative sequenceVSP_025275986-1012in isoform 2
Alternative sequenceVSP_0252761013-1381in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC026342
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC092983
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC117488
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AB033063
EMBL· GenBank· DDBJ
BAA86551.2
EMBL· GenBank· DDBJ
mRNA
AK074987
EMBL· GenBank· DDBJ
BAC11336.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC004539
EMBL· GenBank· DDBJ
AAH04539.2
EMBL· GenBank· DDBJ
mRNA
BC067235
EMBL· GenBank· DDBJ
AAH67235.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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