• ATP binding • protein tyrosine kinase activity • protein kinase activity • GO:0001948 protein binding • transmembrane receptor protein tyrosine kinase activity • kinase activity • nucleotide binding • transferase activity • receptor tyrosine kinase • transmembrane signaling receptor activity • Wnt-protein binding
Cellular component
• integral component of membrane • photoreceptor outer segment • rhabdomere • membrane • integral component of plasma membrane • plasma membrane • cytoplasm • extracellular space • receptor complex
Biological process
• spermatogenesis • vagina development • protein kinase B signaling • natural killer cell differentiation • cell surface receptor signaling pathway • protein phosphorylation • platelet activation • cell-cell signaling • positive regulation of phagocytosis • apoptotic cell clearance • substrate adhesion-dependent cell spreading • leukocyte migration • negative regulation of lymphocyte activation • phosphorylation • retina development in camera-type eye • negative regulation of leukocyte apoptotic process • phagocytosis • secretion by cell • peptidyl-tyrosine phosphorylation • negative regulation of cytokine production • neutrophil clearance • negative regulation of signal transduction • Wnt signaling pathway • cell differentiation • negative regulation of apoptotic process • positive regulation of ERK1 and ERK2 cascade • transmembrane receptor protein tyrosine kinase signaling pathway • nervous system development • cell migration
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
10461
17289
Ensembl
ENSG00000153208
ENSMUSG00000014361
UniProt
Q12866
Q60805
RefSeq (mRNA)
NM_006343
NM_008587
RefSeq (protein)
NP_006334
NP_032613
Location (UCSC)
Chr 2: 111.9 – 112.03 Mb
Chr 2: 128.7 – 128.8 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Proto-oncogene tyrosine-protein kinase MER is an enzyme that in humans is encoded by the MERTK gene.[5][6][7]
Contents
1 Function
2 References
3 Further reading
4 External links
Function[edit]
This gene is a member of the TYRO3/AXL/MER (TAM) receptor kinase family and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) domains, and one tyrosine kinase domain. Mutations in this gene have been associated with disruption of the retinal pigment epithelium (RPE) phagocytosis pathway and onset of autosomal recessive retinitis pigmentosa (RP).[7]
References[edit]
^ a b cGRCh38: Ensembl release 89: ENSG00000153208 - Ensembl, May 2017
^ a b cGRCm38: Ensembl release 89: ENSMUSG00000014361 - 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.
^Graham DK, Dawson TL, Mullaney DL, Snodgrass HR, Earp HS (June 1994). "Cloning and mRNA expression analysis of a novel human protooncogene, c-mer". Cell Growth & Differentiation. 5 (6): 647–57. PMID 8086340.
^Weier HU, Fung J, Lersch RA (Jun 1999). "Assignment of protooncogene MERTK (a.k.a. c-mer) to human chromosome 2q14.1 by in situ hybridization". Cytogenetics and Cell Genetics. 84 (1–2): 91–2. doi:10.1159/000015223. PMID 10343112. S2CID 43714175.
^ a b"Entrez Gene: MERTK c-mer proto-oncogene tyrosine kinase".
Further reading[edit]
Iwase T, Tanaka M, Suzuki M, Naito Y, Sugimura H, Kino I (July 1993). "Identification of protein-tyrosine kinase genes preferentially expressed in embryo stomach and gastric cancer". Biochemical and Biophysical Research Communications. 194 (2): 698–705. doi:10.1006/bbrc.1993.1878. hdl:10271/1029. PMID 7688222.
Mark MR, Chen J, Hammonds RG, Sadick M, Godowsk PJ (April 1996). "Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl". The Journal of Biological Chemistry. 271 (16): 9785–9. doi:10.1074/jbc.271.16.9785. PMID 8621659.
Ling L, Templeton D, Kung HJ (August 1996). "Identification of the major autophosphorylation sites of Nyk/Mer, an NCAM-related receptor tyrosine kinase". The Journal of Biological Chemistry. 271 (31): 18355–62. doi:10.1074/jbc.271.31.18355. PMID 8702477.
Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Nagata K, Ohashi K, Nakano T, Arita H, Zong C, Hanafusa H, Mizuno K (November 1996). "Identification of the product of growth arrest-specific gene 6 as a common ligand for Axl, Sky, and Mer receptor tyrosine kinases". The Journal of Biological Chemistry. 271 (47): 30022–7. doi:10.1074/jbc.271.47.30022. PMID 8939948.
Georgescu MM, Kirsch KH, Shishido T, Zong C, Hanafusa H (February 1999). "Biological effects of c-Mer receptor tyrosine kinase in hematopoietic cells depend on the Grb2 binding site in the receptor and activation of NF-kappaB". Molecular and Cellular Biology. 19 (2): 1171–81. doi:10.1128/mcb.19.2.1171. PMC 116046. PMID 9891051.
Gal A, Li Y, Thompson DA, Weir J, Orth U, Jacobson SG, Apfelstedt-Sylla E, Vollrath D (November 2000). "Mutations in MERTK, the human orthologue of the RCS rat retinal dystrophy gene, cause retinitis pigmentosa". Nature Genetics. 26 (3): 270–1. doi:10.1038/81555. PMID 11062461. S2CID 2812292.
Thompson DA, McHenry CL, Li Y, Richards JE, Othman MI, Schwinger E, Vollrath D, Jacobson SG, Gal A (January 2002). "Retinal dystrophy due to paternal isodisomy for chromosome 1 or chromosome 2, with homoallelism for mutations in RPE65 or MERTK, respectively". American Journal of Human Genetics. 70 (1): 224–9. doi:10.1086/338455. PMC 384890. PMID 11727200.
Yin JL, Hambly BD, Bao SS, Painter D, Bishop GA, Eris JM (September 2003). "Expression of growth arrest-specific gene 6 and its receptors in dysfunctional human renal allografts". Transplant International. 16 (9): 681–8. doi:10.1007/s00147-003-0593-3. PMID 12768229. S2CID 13419387.
McHenry CL, Liu Y, Feng W, Nair AR, Feathers KL, Ding X, Gal A, Vollrath D, Sieving PA, Thompson DA (May 2004). "MERTK arginine-844-cysteine in a patient with severe rod-cone dystrophy: loss of mutant protein function in transfected cells". Investigative Ophthalmology & Visual Science. 45 (5): 1456–63. doi:10.1167/iovs.03-0909. PMID 15111602.
Chen C, Li Q, Darrow AL, Wang Y, Derian CK, Yang J, de Garavilla L, Andrade-Gordon P, Damiano BP (June 2004). "Mer receptor tyrosine kinase signaling participates in platelet function". Arteriosclerosis, Thrombosis, and Vascular Biology. 24 (6): 1118–23. doi:10.1161/01.ATV.0000130662.30537.08. PMID 15130911.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (June 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
Li Y, Mahajan NP, Webster-Cyriaque J, Bhende P, Hong GK, Earp HS, Kenney S (November 2004). "The C-mer gene is induced by Epstein-Barr virus immediate-early protein BRLF1". Journal of Virology. 78 (21): 11778–85. doi:10.1128/JVI.78.21.11778-11785.2004. PMC 523243. PMID 15479819.
Gould WR, Baxi SM, Schroeder R, Peng YW, Leadley RJ, Peterson JT, Perrin LA (April 2005). "Gas6 receptors Axl, Sky and Mer enhance platelet activation and regulate thrombotic responses". Journal of Thrombosis and Haemostasis. 3 (4): 733–41. doi:10.1111/j.1538-7836.2005.01186.x. PMID 15733062. S2CID 20373626.
Liu T, Qian WJ, Gritsenko MA, Camp DG, Monroe ME, Moore RJ, Smith RD (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
Graham DK, Salzberg DB, Kurtzberg J, Sather S, Matsushima GK, Keating AK, Liang X, Lovell MA, Williams SA, Dawson TL, Schell MJ, Anwar AA, Snodgrass HR, Earp HS (May 2006). "Ectopic expression of the proto-oncogene Mer in pediatric T-cell acute lymphoblastic leukemia". Clinical Cancer Research. 12 (9): 2662–9. doi:10.1158/1078-0432.CCR-05-2208. PMID 16675557.
Tada A, Wada Y, Sato H, Itabashi T, Kawamura M, Tamai M, Nishida K (May 2006). "Screening of the MERTK gene for mutations in Japanese patients with autosomal recessive retinitis pigmentosa". Molecular Vision. 12: 441–4. PMID 16710167.
External links[edit]
GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview
Overview of all the structural information available in the PDB for UniProt: Q12866 (Tyrosine-protein kinase Mer) at the PDBe-KB.
vtePDB gallery
2dbj: Solution structures of the fn3 domain of human Proto-oncogene tyrosine-protein kinase MER precursor
2p0c: Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER
vteProtein kinases: tyrosine kinases (EC 2.7.10)
Receptor tyrosine kinases (EC 2.7.10.1)
Growth factor receptors
EGF receptor family
EGFR
ERBB2
ERBB3
ERBB4
Insulin receptor family
IGF1R
INSR
INSRR
PDGF receptor family
CSF1R
FLT3
KIT
PDGFR (PDGFRA
PDGFRB)
FGF receptor family
FGFR1
FGFR2
FGFR3
FGFR4
VEGF receptors family
VEGFR1
VEGFR2
VEGFR3
HGF receptor family
MET
RON
Trk receptor family
NTRK1
NTRK2
NTRK3
EPH receptor family
EPHA1
EPHA2
EPHA3
EPHA4
EPHA5
EPHA6
EPHA7
EPHA8
EPHB1
EPHB2
EPHB3
EPHB4
EPHB5
EPHB6
EPHX
LTK receptor family
LTK
ALK
TIE receptor family
TIE
TEK
ROR receptor family
ROR1
ROR2
DDR receptor family
DDR1
DDR2
PTK7 receptor family
PTK7
RYK receptor family
RYK
MuSK receptor family
MUSK
ROS receptor family
ROS1
AATYK receptor family
AATYK
AATYK2
AXL receptor family
AXL
MER
TYRO3
RET receptor family
RET
uncategorised
STYK1
Non-receptor tyrosine kinases (EC 2.7.10.2)
ABL family
ABL1
ARG
ACK family
ACK1
TNK1
CSK family
CSK
MATK
FAK family
FAK
PYK2
FES family
FES
FER
FRK family
FRK
BRK
SRMS
JAK family
JAK1
JAK2
JAK3
TYK2
SRC-A family
SRC
FGR
FYN
YES1
SRC-B family
BLK
HCK
LCK
LYN
TEC family
TEC
BMX
BTK
ITK
TXK
SYK family
SYK
ZAP70
vteEnzymes
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)
Biology portal
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