Related to receptor tyrosine kinase

RYK
Identifiers
Aliases	RYK, D3S3195, JTK5, JTK5A, RYK1, receptor-like tyrosine kinase, receptor like tyrosine kinase
External IDs	OMIM: 600524 MGI: 101766 HomoloGene: 68287 GeneCards: RYK
Gene location (Human)
Chr.	Chromosome 3 (human)[1]
End	134,250,744 bp[1]
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)[2]
End	102,908,305 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • protein tyrosine kinase activity; • transferase activity; • transmembrane signaling receptor activity; • kinase activity; • Wnt-activated receptor activity; • ATP binding; • GO:0001948 protein binding; • GO:0005110 frizzled binding; • Wnt-protein binding; • coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway; • receptor tyrosine kinase; • transmembrane receptor protein tyrosine kinase activity; • protein kinase activity;
Cellular component	• cytoplasm; • integral component of membrane; • integral component of plasma membrane; • membrane; • cell membrane; • cell nucleus; • receptor complex;
Biological process	• positive regulation of MAPK cascade; • corpus callosum development; • signal transduction; • canonical Wnt signaling pathway; • non-canonical Wnt signaling pathway; • neurogenesis; • commissural neuron axon guidance; • neuron projection development; • protein phosphorylation; • synapse assembly; • chemorepulsion of dopaminergic neuron axon; • neuron differentiation; • cell proliferation in midbrain; • phosphorylation; • axonogenesis; • axon guidance; • Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; • midbrain dopaminergic neuron differentiation; • planar cell polarity pathway involved in axon guidance; • Wnt signaling pathway; • peptidyl-tyrosine phosphorylation; • skeletal system morphogenesis; • negative regulation of axon extension involved in axon guidance; • negative chemotaxis; • negative regulation of signal transduction; • cell differentiation; • negative regulation of apoptotic process; • positive regulation of ERK1 and ERK2 cascade; • transmembrane receptor protein tyrosine kinase signaling pathway; • nervous system development;
	Sources:Amigo / QuickGO
Orthologs
	6259
	20187
	ENSG00000163785
	ENSMUSG00000032547
	P34925
	Q01887
	NM_001005861; NM_002958
	NM_001042607; NM_013649; NM_001284258
	NP_001005861; NP_002949
	NP_001036072; NP_001271187; NP_038677
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

GRCh38: Ensembl release 89: ENSG00000163785 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000032547 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"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.
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.
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.
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: 697–705. doi:10.1038/nn.4282. PMC 4847956.

Partanen J, Mäkelä TP, Alitalo R, et al. (1991). "Putative tyrosine kinases expressed in K-562 human leukemia cells". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 8913–8917. doi:10.1073/pnas.87.22.8913. PMC 55070. PMID 2247464.
Gough NM, Rakar S, Hovens CM, Wilks A (1995). "Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK". Mamm. Genome. 6 (4): 255–6. doi:10.1007/BF00352411. PMID 7613029.
Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene. 8 (12): 3403–3410. PMID 8247543.
Stacker SA, Hovens CM, Vitali A, et al. (1993). "Molecular cloning and chromosomal localisation of the human homologue of a receptor related to tyrosine kinases (RYK)". Oncogene. 8 (5): 1347–1356. PMID 8386829.
Tamagnone L, Partanen J, Armstrong E, et al. (1993). "The human ryk cDNA sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain". Oncogene. 8 (7): 2009–2014. PMID 8390040.
Wang XC, Katso R, Butler R, et al. (1996). "H-RYK, an unusual receptor kinase: isolation and analysis of expression in ovarian cancer". Mol. Med. 2 (2): 189–203. PMC 2230112. PMID 8726462.
Katso RM, Russell RB, Ganesan TS (1999). "Functional analysis of H-Ryk, an atypical member of the receptor tyrosine kinase family". Mol. Cell. Biol. 19 (9): 6427–6440. PMC 84612. PMID 10454588.
Trivier E, Ganesan TS (2002). "RYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6". J. Biol. Chem. 277 (25): 23037–43. doi:10.1074/jbc.M202486200. PMID 11956217.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
Lu W, Yamamoto V, Ortega B, Baltimore D (2004). "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth". Cell. 119 (1): 97–108. doi:10.1016/j.cell.2004.09.019. PMID 15454084.
Watanabe A, Akita S, Tin NT, et al. (2006). "A mutation in RYK is a genetic factor for nonsyndromic cleft lip and palate". Cleft Palate Craniofac. J. 43 (3): 310–6. doi:10.1597/04-145.1. PMID 16681403.
Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biology. 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000163785 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-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.

[hovens-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.

[halford-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: 697–705. doi:10.1038/nn.4282. PMC 4847956.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Related to receptor tyrosine kinase

History

Structure

Function

References

Further reading