G1PQN2 · G1PQN2_MYOLU

Function

Catalytic activity

Features

Showing features for binding site, active site.

1984100200300400500600700800900
Type
IDPosition(s)Description
Binding site625-633ATP (UniProtKB | ChEBI)
Binding site651ATP (UniProtKB | ChEBI)
Active site744Proton acceptor

GO annotations

AspectTerm
Cellular Componentdendrite
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionaxon guidance receptor activity
Molecular Functiontransmembrane-ephrin receptor activity
Biological Processangiogenesis
Biological Processaxonal fasciculation
Biological Processcell migration
Biological Processcentral nervous system projection neuron axonogenesis
Biological Processcorpus callosum development
Biological Processdendritic spine morphogenesis
Biological Processdigestive tract morphogenesis
Biological Processpositive regulation of synapse assembly
Biological Processprotein autophosphorylation
Biological Processregulation of axonogenesis
Biological Processregulation of cell-cell adhesion
Biological Processretinal ganglion cell axon guidance
Biological Processroof of mouth development
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processthymus development
Biological Processurogenital system development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ephrin type-B receptor 3
  • EC number

Gene names

    • Name
      EPHB3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Vespertilionidae > Myotis

Accessions

  • Primary accession
    G1PQN2

Proteomes

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Cell projection, dendrite

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond61↔179
Disulfide bond96↔106

Keywords

Interaction

Subunit

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain19-197Eph LBD
Domain319-434Fibronectin type-III
Domain435-528Fibronectin type-III
Domain619-882Protein kinase
Domain911-975SAM

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    984
  • Mass (Da)
    108,718
  • Last updated
    2011-10-19 v1
  • MD5 Checksum
    3BC6DA8E6D6DE5BB64C861EE1980056D
LFLPILSLAPDLFSSVAPPETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIANAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKDTQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGVPGPGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLHLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQKNSVQLDGLRPEARYVVQVRARTVAGYGQYSRPAEFETTSERAVPSCLQAPVPCSSRAGLVFVVAVVVIAVVLPQKQRHGSDSEYTEKLQQYSNGKGSQVAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAPE02008594
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAPE02008595
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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