Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00629

Receptor tyrosine kinase class V signatures


A number of growth factors stimulate mitogenesis by interacting with a family of cell surface receptors which possess an intrinsic, ligand-sensitive, protein tyrosine kinase activity [1]. These receptor tyrosine kinases (RTK) all share the same topology: an extracellular ligand-binding domain, a single transmembrane region and a cytoplasmic kinase domain. However they can be classified into at least five groups on the basis of sequence similarities. The extracellular domain of class V RTK's consist of a region of about 300 amino acids, amongst which 16 conserved cysteines probably involved in disulfide bonds; this region is followed by two copies of a fibronectin type III domain. The ligands for these receptors are proteins of about 200 to 300 residues collectively known as Ephrins (see <PDOC01003>). The receptors currently known to belong to class V are [2,3,E1]:

  • EPHA1 (Eph-1; Esk).
  • EPHA2 (Eck; Mpk-5; Sek-2).
  • EPHA3 (Etk-1; Hek; Mek4; Tyro4; Rek4; Cek4).
  • EPHA4 (Sek; Hek8; Mpk-3; Cek8).
  • EPHA5 (Ehk-1; Hek7; Bsk; Cek7).
  • EPHA6 (Ehk-2).
  • EPHA7 (Ehk-3; Hek11; Mdk-1; Ebk).
  • EPHA8 (Eek).
  • EPHB1 (Eph-2; Elk; Net).
  • EPHB2 (Eph-3; Hek5; Drt; Erk; Nuk; Sek-3; Cek5; Qek5).
  • EPHB3 (Hek-2; Mdk-5).
  • EPHB4 (Htk; Mdk-2; Myk-1).
  • EPHB5 (Cek9).
  • EPHB6 (HEP).

The EPHA subtype receptors bind to GPI-anchored ephrins while the EPHB subtype receptors bind to type-I membrane ephrins.

We developed two signature patterns for this class of RTK's, which each include some of the conserved cysteine residues.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

RECEPTOR_TYR_KIN_V_1, PS00790; Receptor tyrosine kinase class V signature 1  (PATTERN)

RECEPTOR_TYR_KIN_V_2, PS00791; Receptor tyrosine kinase class V signature 2  (PATTERN)


1AuthorsYarden Y., Ullrich A.
TitleGrowth factor receptor tyrosine kinases.
SourceAnnu. Rev. Biochem. 57:443-478(1988).
PubMed ID3052279

2AuthorsSajjadi F.G., Pasquale E.B., Subramani S.
TitleIdentification of a new eph-related receptor tyrosine kinase gene from mouse and chicken that is developmentally regulated and encodes at least two forms of the receptor.
SourceNew Biol. 3:769-778(1991).
PubMed ID1657122

3AuthorsWicks I.P., Wilkinson D., Salvaris E., Boyd A.W.
TitleMolecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines.
SourceProc. Natl. Acad. Sci. U.S.A. 89:1611-1615(1992).
PubMed ID1311845


PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)