Related to receptor tyrosine kinase

The related to receptor tyrosine kinase (RYK) gene encodes the protein Ryk.

RYK
Identifiers
AliasesRYK, D3S3195, JTK5, JTK5A, RYK1, receptor-like tyrosine kinase, receptor like tyrosine kinase
External IDsOMIM: 600524 MGI: 101766 HomoloGene: 68287 GeneCards: RYK
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3q22.2Start134,065,303 bp[1]
End134,250,744 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

6259

20187

Ensembl

ENSG00000163785

ENSMUSG00000032547

UniProt

P34925

Q01887

RefSeq (mRNA)

NM_001005861
NM_002958

NM_001042607
NM_013649
NM_001284258

RefSeq (protein)

NP_001005861
NP_002949

NP_001036072
NP_001271187
NP_038677

Location (UCSC)Chr 3: 134.07 – 134.25 MbChr 9: 102.83 – 102.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The protein encoded by this gene is an atypical member of the family of growth factor receptor protein tyrosine kinases, differing from other members at a number of conserved residues in the activation and nucleotide binding domains. This gene product belongs to a subfamily whose members do not appear to be regulated by phosphorylation in the activation segment. It has been suggested that mediation of biological activity by recruitment of a signaling-competent auxiliary protein may occur through an as yet uncharacterized mechanism. Two alternative splice variants have been identified, encoding distinct isoforms.[5]

History

The gene encoding mouse RYK was first identified in 1992.[6] Subsequently, cDNA encoding the RYK protein have been isolated from the following species.[7]

Structure

In common with other receptor tyrosine kinase family members, RYK is composed of three domains, an N-terminal, extracellular ligand-binding domain, a transmembrane spanning domain and a C-terminal intracellular domain. However, in contrast to other receptor tyrosine kinases the C-terminal domain of RYK is devoid of detectable kinase activity.[7]

Function

RYK is involved in regulation of axon growth during development of the nervous system.[8]

References

  1. GRCh38: Ensembl release 89: ENSG00000163785 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000032547 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "RYK receptor like tyrosine kinase [ Homo sapiens (human) ]". National Center for Biotechnology Information, U.S. National Library of Medicine. 13 March 2020. Retrieved 2 April 2020.
  6. Hovens CM, Stacker SA (1992). "RYK, a receptor tyrosine kinase-related molecule with unusual kinase domain motifs". Proc. Natl. Acad. Sci. USA. 89 (24): 11818–11822. doi:10.1073/pnas.89.24.11818. PMC 50648. PMID 1334548.
  7. Halford MM, Stacker SA (2001). "Revelations of the RYK receptor". BioEssays. 23 (1): 34–45. doi:10.1002/1521-1878(200101)23:1<34::AID-BIES1005>3.0.CO;2-D. PMID 11135307.
  8. Hollis ER, Ishiko N, Yu T, Lu CC, Haimovich A, Tolentino K, Richman A, Tury A, Wang SH, Pessian M, Jo E, Kolodkin A, Zou Y (2016). "Ryk controls remapping of motor cortex during functional recovery after spinal cord injury". Nature Neuroscience. 19 (5): 697–705. doi:10.1038/nn.4282. PMC 4847956. PMID 27065364.

Further reading

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