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Cited by 528Cytokine Signaling Pathways and InteractionsProtein Kinase Regulation and GTPase SignalingProtein Tyrosine Phosphatases

Two Novel Protein-Tyrosine Kinases, Each with a Second Phosphotransferase-Related Catalytic Domain, Define a New Class of Protein Kinase

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Wilks, A F, Harpur, A G, Kurban, R R, Ralph, S J, Zürcher, G, Ziemiecki, A·1991·Molecular and Cellular Biology
DOI 10.1128/mcb.11.4.2057PMC PMC359893
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Abstract

The protein-tyrosine kinases (PTKs) are a burgeoning family of proteins, each of which bears a conserved domain of 250 to 300 amino acids capable of phosphorylating substrate proteins on tyrosine residues. We recently exploited the existence of two highly conserved sequence elements within the catalytic domain to generate PTK-specific degenerate oligonucleotide primers (A. F. Wilks, Proc. Natl. Acad. Sci. USA 86:1603-1607, 1989). By application of the polymerase chain reaction, portions of the catalytic domains of several novel PTKs were amplified. We describe here the primary sequence of one of these new PTKs, JAK1 (from Janus kinase), a member of a new class of PTK characterized by the presence of a second phosphotransferase-related domain immediately N terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. A second member of this family (JAK2) has been partially characterized and exhibits a similar array of kinase-related domains. JAK1 is a large, widely expressed membrane-associated phosphoprotein of approximately 130,000 Da. The PTK activity of JAK1 has been located in the C-terminal PTK-like domain. The role of the second kinaselike domain is unknown.

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  • The human genome encodes four JAKs: JAK1, JAK2, JAK3, and TYK2.

    “The human genome encodes four JAKs—JAK1, JAK2, JAK3, and tyrosine kinase 2 (TYK2)—that associate selectively (Fig. 1) with different receptors (Wilks, 1989; Firmbach-Kraft et al., 1990; Wilks et al., 1991; Harpur et al., 1992).”

    From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as Wilks et al., 1991

    The abstract (p. 2057) identifies JAK1 and says JAK2 is a second member of the family. The indexed passages do not identify JAK3 or TYK2 or state that the human genome encodes exactly four JAKs, so this paper supports only part of the attributed list. (LLM, conf=0.87)

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Cited by

Sorted by citations

Authors
Wilks, A. F., Harpur, A. G., Kurban, R. R., Ralph, S. J., Zürcher, G., & Ziemiecki, A.
Affiliations
The Royal Melbourne Hospital (AU)
ORCID
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
1991-04
Volume
11
Issue
4
Pages
2057-2065
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
DOI
10.1128/mcb.11.4.2057
PMC
PMC359893
OpenAlex
W2047851489
Cited by
528
References
0
Citations by year
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FWCI
15.42
Type
journal article
Language
en
Open access
Locations
  • Molecular and Cellular Biology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
tyrosine kinase, JAK1, JAK2, Janus kinase, kinase domain structure, degenerate oligonucleotide primers
MeSH terms
Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, DNA, Humans, Molecular Sequence Data, Phosphorylation, Phosphotransferases, Phylogeny, Protein Kinases, Protein-Tyrosine Kinases, Sequence Homology, Nucleic Acid, Gene Expression, Polymerase Chain Reaction

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