Merlin (protein)

Mammalian protein found in Homo sapiens

NF2

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

4ZRJ, 1H4R, 3U8Z, 4ZRI

Identifiers
Aliases| NF2, ACN, BANF, SCH, neurofibromin 2 (merlin), neurofibromin 2, merlin-1, moesin-ezrin-radixin like (MERLIN) tumor suppressor
External IDs| OMIM: 607379; MGI: 97307; HomoloGene: 2180; GeneCards: NF2; OMA:NF2 - orthologs
| Gene location (Human)

Chr.| Chromosome 22 (human)[1]

Band| 22q12.2| Start| 29,603,556 bp[1]
End| 29,698,598 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 11 (mouse)[2]

Band| 11 A1|11 3.0 cM| Start| 4,715,845 bp[2]
End| 4,799,536 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* stromal cell of endometrium

* dorsal motor nucleus of vagus nerve

* tendon of biceps brachii

* Region I of hippocampus proper

* glutes

* postcentral gyrus

* vastus lateralis muscle

* triceps brachii muscle

* entorhinal cortex

* inferior olivary nucleus

| Top expressed in

* gastrula

* saccule

* otic vesicle

* neural layer of retina

* otic placode

* submandibular gland

* muscle of thigh

* secondary oocyte

* molar

* myocardium of ventricle

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* cytoskeletal protein binding
* protein binding
* actin binding

Cellular component|

* cytoplasm
* cell body
* cell projection
* membrane
* filopodium
* ruffle
* adherens junction
* plasma membrane
* apical part of cell
* ruffle membrane
* early endosome
* nucleolus
* cortical actin cytoskeleton
* perinuclear region of cytoplasm
* neuron projection
* cleavage furrow
* cytoskeleton
* nucleus
* lamellipodium
* filopodium membrane
* cytosol

Biological process|

* negative regulation of receptor signaling pathway via JAK-STAT
* regulation of gliogenesis
* cell-cell junction organization
* regulation of protein stability
* negative regulation of cell-cell adhesion
* negative regulation of protein kinase activity
* mesoderm formation
* ectoderm development
* negative regulation of DNA replication
* Schwann cell proliferation
* regulation of neural precursor cell proliferation
* regulation of protein localization to nucleus
* negative regulation of cell-matrix adhesion
* odontogenesis of dentin-containing tooth
* brain development
* negative regulation of cell migration
* lens fiber cell differentiation
* regulation of cell population proliferation
* positive regulation of cell differentiation
* negative regulation of MAPK cascade
* regulation of hippo signaling
* hippocampus development
* regulation of stem cell proliferation
* regulation of neurogenesis
* actin cytoskeleton organization
* positive regulation of stress fiber assembly
* negative regulation of cell population proliferation
* negative regulation of tyrosine phosphorylation of STAT protein
* regulation of apoptotic process
* regulation of cell cycle

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

4771

18016

Ensembl| |

ENSG00000186575

ENSMUSG00000009073

UniProt| |

P35240

P46662

RefSeq (mRNA)| | NM_181835
NM_000268
NM_016418
NM_181825
NM_181826

NM_181827
NM_181828
NM_181829
NM_181830
NM_181831
NM_181832
NM_181833
NM_181834

| NM_001252250
NM_001252251
NM_001252252
NM_001252253
NM_010898

NM_001361675
NM_001361676
NM_001361677

RefSeq (protein)| | NP_000259
NP_057502
NP_861546
NP_861966
NP_861967

NP_861968
NP_861969
NP_861970
NP_861971

| NP_001239179
NP_001239180
NP_001239181
NP_001239182
NP_035028

NP_001348604
NP_001348605
NP_001348606

Location (UCSC)| Chr 22: 29.6 – 29.7 Mb| Chr 11: 4.72 – 4.8 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Merlin (also called neurofibromin 2 or schwannomin) is a cytoskeletal protein. In humans, it is a tumor suppressor protein involved in neurofibromatosis type II.[5][6] Sequence data reveal its similarity to the ERM protein family.

Merlin is an acronym for "Moesin-Ezrin-Radixin-like protein".

## Gene

[edit]

Human merlin is coded by the gene NF2 in chromosome 22. Mouse merlin gene is located on chromosome 11[7] and rat merlin gene on chromosome 17. Fruit fly merlin gene (symbol Mer) is located on chromosome 1 and shares 58% similarity to its human homologue. Other merlin-like genes are known from a wide range of animals, and the derivation of merlin is thought to be in early metazoa. Merlin is a member of the ERM family of proteins including ezrin, moesin, and radixin, which are in the protein 4.1 superfamily of proteins. Merlin is also known as schwannomin, a name derived from the most common type of tumor in the NF2 patient phenotype, the schwannoma.

## Structure

[edit]

Vertebrate merlin is a 70 kDa protein. There are 10 known isoforms of human merlin molecule (the full molecule being 595 amino acids in length). The two most common of these are also found in the mouse and are called type 1 and type 2, differing by the absence or presence of exon 16 or 17, respectively). All the known varieties have a conserved N-terminal part, which contains a FERM domain (a domain found in most cytoskeletal-membrane organizing proteins). The FERM domain is followed by an alpha-helical domain and a hydrophilic tail.[8][9] Merlin can dimerize with itself and heterodimerize with other ERM family proteins.

## Function

[edit]

Merlin is a membrane-cytoskeleton scaffolding protein, i.e. linking actin filaments to cell membrane or membrane glycoproteins.[10] Human merlin is predominantly found in nervous tissue, but also in several other fetal tissues, and is mainly located in adherens junctions.[11] Its tumor suppressor properties are probably associated with contact-mediated growth inhibition. Drosophila merlin is expressed in embryonic hindgut, salivary glands, and imaginal discs, and has apparently a slightly different role than in vertebrates.[12]

The phosphorylation of serine 518 is known to alter the functional state of merlin.[13] The signaling pathway of merlin is proposed to include several salient cell growth controlling molecules, including eIF3c, CD44, protein kinase A, and p21 activated kinases.

Work in Drosophila identified Merlin as an upstream regulator of the Hippo tumor suppressor pathway,[14] a function that is conserved in mammals.[15] The Hippo pathway is a well conserved signalling pathway that coordinately regulates cell proliferation and apoptosis.[16]

Mutations of the NF2 gene cause a human autosomal dominant disease called neurofibromatosis type 2. It is characterized by the development of tumors of the nervous system, most commonly of bilateral vestibular schwannomas (also called acoustic neuromas). NF2 belongs to the tumor suppressor group of genes.[17]

## Interactions

[edit]

Merlin (protein) has been shown to interact with:

* CUL4A,[18]
* DDB1,[18]
* EZR,[19]
* HGS,[20][21]
* MED28,[22]
* RIT1,[18]
* SDCBP,[23]
* SPTBN1,[24] and
* VPRBP.[18]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000186575 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009073 - 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. ^ Rouleau GA, Merel P, Lutchman M, Sanson M, Zucman J, Marineau C, Hoang-Xuan K, Demczuk S, Desmaze C, Plougastel B (1993). "Alteration in a new gene encoding a putative membrane-organizing protein causes neuro-fibromatosis type 2". Nature. 363 (6429): 515–21\. Bibcode:1993Natur.363..515R. doi:10.1038/363515a0. PMID 8379998. S2CID 24532924.515-21&rft.date=1993&rft_id=info:doi/10.1038/363515a0&rft_id=https://api.semanticscholar.org/CorpusID:24532924#id-name=S2CID&rft_id=info:pmid/8379998&rft_id=info:bibcode/1993Natur.363..515R&rft.aulast=Rouleau&rft.aufirst=GA&rft.au=Merel,+P&rft.au=Lutchman,+M&rft.au=Sanson,+M&rft.au=Zucman,+J&rft.au=Marineau,+C&rft.au=Hoang-Xuan,+K&rft.au=Demczuk,+S&rft.au=Desmaze,+C&rft.au=Plougastel,+B&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
6. ^ Golovnina K, Blinov A, Akhmametyeva EM, Omelyanchuk LV, Chang LS (2005). "Evolution and origin of merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor gene". BMC Evol. Biol. 5 (1): 69. Bibcode:2005BMCEE...5...69G. doi:10.1186/1471-2148-5-69. PMC 1315344. PMID 16324214.
7. ^ Haase VH, Trofatter JA, MacCollin M, Tarttelin E, Gusella JF, Ramesh V (1994). "The murine NF2 homologue encodes a highly conserved merlin protein with alternative forms". Hum. Mol. Genet. 3 (3): 407–11\. doi:10.1093/hmg/3.3.407. PMID 8012352.407-11&rft.date=1994&rft_id=info:doi/10.1093/hmg/3.3.407&rft_id=info:pmid/8012352&rft.aulast=Haase&rft.aufirst=VH&rft.au=Trofatter,+JA&rft.au=MacCollin,+M&rft.au=Tarttelin,+E&rft.au=Gusella,+JF&rft.au=Ramesh,+V&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
8. ^ Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Tsukita S, Hakoshima T (2002). "Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain". J. Biol. Chem. 277 (12): 10332–6\. doi:10.1074/jbc.M109979200. PMID 11756419.10332-6&rft.date=2002&rft_id=info:doi/10.1074/jbc.M109979200&rft_id=info:pmid/11756419&rft.aulast=Shimizu&rft.aufirst=T&rft.au=Seto,+A&rft.au=Maita,+N&rft.au=Hamada,+K&rft.au=Tsukita,+S&rft.au=Tsukita,+S&rft.au=Hakoshima,+T&rft_id=https://doi.org/10.1074%2Fjbc.M109979200&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
9. ^ Ali Khajeh J, Ju JH, Atchiba M (2014). "Molecular conformation of the full-length tumor suppressor NF2/Merlin--a small-angle neutron scattering study". Journal of Molecular Biology. 426 (15): 2755–68\. doi:10.1016/j.jmb.2014.05.011. PMC 4407695. PMID 24882693.2755-68&rft.date=2014&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4407695#id-name=PMC&rft_id=info:pmid/24882693&rft_id=info:doi/10.1016/j.jmb.2014.05.011&rft.aulast=Ali+Khajeh&rft.aufirst=J&rft.au=Ju,+JH&rft.au=Atchiba,+M&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4407695&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
10. ^ McClatchey AI, Giovannini M (2005). "Membrane organization and tumorigenesis--the NF2 tumor suppressor, Merlin". Genes Dev. 19 (19): 2265–77\. doi:10.1101/gad.1335605. PMID 16204178.2265-77&rft.date=2005&rft_id=info:doi/10.1101/gad.1335605&rft_id=info:pmid/16204178&rft.aulast=McClatchey&rft.aufirst=AI&rft.au=Giovannini,+M&rft_id=https://doi.org/10.1101%2Fgad.1335605&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
11. ^ den Bakker MA, Vissers KJ, Molijn AC, Kros JM, Zwarthoff EC, van der Kwast TH (1999). "Expression of the neurofibromatosis type 2 gene in human tissues". J. Histochem. Cytochem. 47 (11): 1471–80\. doi:10.1177/002215549904701113. PMID 10544220.1471-80&rft.date=1999&rft_id=info:doi/10.1177/002215549904701113&rft_id=info:pmid/10544220&rft.aulast=den+Bakker&rft.aufirst=MA&rft.au=Vissers,+KJ&rft.au=Molijn,+AC&rft.au=Kros,+JM&rft.au=Zwarthoff,+EC&rft.au=van+der+Kwast,+TH&rft_id=https://doi.org/10.1177%2F002215549904701113&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
12. ^ LaJeunesse DR, McCartney BM, Fehon RG (1998). "Structural Analysis of Drosophila Merlin Reveals Functional Domains Important for Growth Control and Subcellular Localization". J. Cell Biol. 141 (7): 1589–99\. doi:10.1083/jcb.141.7.1589. PMC 2133006. PMID 9647651.1589-99&rft.date=1998&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133006#id-name=PMC&rft_id=info:pmid/9647651&rft_id=info:doi/10.1083/jcb.141.7.1589&rft.aulast=LaJeunesse&rft.aufirst=DR&rft.au=McCartney,+BM&rft.au=Fehon,+RG&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133006&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
13. ^ Alfthan K, Heiska L, Grönholm M, Renkema GH, Carpén O (2004). "Cyclic AMP-dependent protein kinase phosphorylates merlin at serine 518 independently of p21-activated kinase and promotes merlin-ezrin heterodimerization". J. Biol. Chem. 279 (18): 18559–66\. doi:10.1074/jbc.M313916200. PMID 14981079.18559-66&rft.date=2004&rft_id=info:doi/10.1074/jbc.M313916200&rft_id=info:pmid/14981079&rft.aulast=Alfthan&rft.aufirst=K&rft.au=Heiska,+L&rft.au=Grönholm,+M&rft.au=Renkema,+GH&rft.au=Carpén,+O&rft_id=https://doi.org/10.1074%2Fjbc.M313916200&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
14. ^ Hamaratoglu F, Willecke M, Kango-Singh M, et al. (2006). "The tumour-suppressor genes NF2/Merlin and Expanded act through Hippo signalling to regulate cell proliferation and apoptosis". Nature Cell Biology. 8 (1): 27–36\. doi:10.1038/ncb1339. PMID 16341207. S2CID 15468669.27-36&rft.date=2006&rft_id=https://api.semanticscholar.org/CorpusID:15468669#id-name=S2CID&rft_id=info:pmid/16341207&rft_id=info:doi/10.1038/ncb1339&rft.aulast=Hamaratoglu&rft.aufirst=F&rft.au=Willecke,+M&rft.au=Kango-Singh,+M&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
15. ^ Zhang N, Bai H, David KK, Dong J, Zheng Y, Cai J, Giovannini M, Liu P, Anders RA, Pan D (2010). "The Merlin/NF2 tumor suppressor functions through the YAP oncoprotein to regulate tissue homeostasis in mammals". Developmental Cell. 19 (1): 27–38\. doi:10.1016/j.devcel.2010.06.015. PMC 2925178. PMID 20643348.27-38&rft.date=2010&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2925178#id-name=PMC&rft_id=info:pmid/20643348&rft_id=info:doi/10.1016/j.devcel.2010.06.015&rft.aulast=Zhang&rft.aufirst=N&rft.au=Bai,+H&rft.au=David,+KK&rft.au=Dong,+J&rft.au=Zheng,+Y&rft.au=Cai,+J&rft.au=Giovannini,+M&rft.au=Liu,+P&rft.au=Anders,+RA&rft.au=Pan,+D&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2925178&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
16. ^ Pan D (October 2010). "The hippo signaling pathway in development and cancer". Developmental Cell. 19 (4): 491–505\. doi:10.1016/j.devcel.2010.09.011. PMC 3124840. PMID 20951342.491-505&rft.date=2010-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3124840#id-name=PMC&rft_id=info:pmid/20951342&rft_id=info:doi/10.1016/j.devcel.2010.09.011&rft.aulast=Pan&rft.aufirst=D&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3124840&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
17. ^ Scoles DR, Yong WH, Qin Y, Wawrowsky K, Pulst SM (2006). "Schwannomin inhibits tumorigenesis through direct interaction with the eukaryotic initiation factor subunit c (eIF3c)". Hum. Mol. Genet. 15 (7): 1059–70\. doi:10.1093/hmg/ddl021. PMID 16497727.1059-70&rft.date=2006&rft_id=info:doi/10.1093/hmg/ddl021&rft_id=info:pmid/16497727&rft.aulast=Scoles&rft.aufirst=DR&rft.au=Yong,+WH&rft.au=Qin,+Y&rft.au=Wawrowsky,+K&rft.au=Pulst,+SM&rft_id=https://doi.org/10.1093%2Fhmg%2Fddl021&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
18. ^ a b c d Huang J, Chen J (July 2008). "VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation". Oncogene. 27 (29): 4056–64\. doi:10.1038/onc.2008.44. PMID 18332868. S2CID 23628888.4056-64&rft.date=2008-07&rft_id=https://api.semanticscholar.org/CorpusID:23628888#id-name=S2CID&rft_id=info:pmid/18332868&rft_id=info:doi/10.1038/onc.2008.44&rft.aulast=Huang&rft.aufirst=J&rft.au=Chen,+J&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
19. ^ Grönholm M, Sainio M, Zhao F, Heiska L, Vaheri A, Carpén O (March 1999). "Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin". J. Cell Sci. 112 (6): 895–904\. doi:10.1242/jcs.112.6.895. PMID 10036239.895-904&rft.date=1999-03&rft_id=info:doi/10.1242/jcs.112.6.895&rft_id=info:pmid/10036239&rft.aulast=Grönholm&rft.aufirst=M&rft.au=Sainio,+M&rft.au=Zhao,+F&rft.au=Heiska,+L&rft.au=Vaheri,+A&rft.au=Carpén,+O&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
20. ^ Gutmann DH, Haipek CA, Burke SP, Sun CX, Scoles DR, Pulst SM (April 2001). "The NF2 interactor, hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), associates with merlin in the "open" conformation and suppresses cell growth and motility". Hum. Mol. Genet. 10 (8): 825–34\. doi:10.1093/hmg/10.8.825. PMID 11285248.825-34&rft.date=2001-04&rft_id=info:doi/10.1093/hmg/10.8.825&rft_id=info:pmid/11285248&rft.aulast=Gutmann&rft.aufirst=DH&rft.au=Haipek,+CA&rft.au=Burke,+SP&rft.au=Sun,+CX&rft.au=Scoles,+DR&rft.au=Pulst,+SM&rft_id=https://doi.org/10.1093%2Fhmg%2F10.8.825&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
21. ^ Scoles DR, Huynh DP, Chen MS, Burke SP, Gutmann DH, Pulst SM (July 2000). "The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate". Hum. Mol. Genet. 9 (11): 1567–74\. doi:10.1093/hmg/9.11.1567. PMID 10861283.1567-74&rft.date=2000-07&rft_id=info:doi/10.1093/hmg/9.11.1567&rft_id=info:pmid/10861283&rft.aulast=Scoles&rft.aufirst=DR&rft.au=Huynh,+DP&rft.au=Chen,+MS&rft.au=Burke,+SP&rft.au=Gutmann,+DH&rft.au=Pulst,+SM&rft_id=https://doi.org/10.1093%2Fhmg%2F9.11.1567&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
22. ^ Wiederhold T, Lee MF, James M, Neujahr R, Smith N, Murthy A, Hartwig J, Gusella JF, Ramesh V (November 2004). "Magicin, a novel cytoskeletal protein associates with the NF2 tumor suppressor merlin and Grb2". Oncogene. 23 (54): 8815–25\. doi:10.1038/sj.onc.1208110. PMID 15467741.8815-25&rft.date=2004-11&rft_id=info:doi/10.1038/sj.onc.1208110&rft_id=info:pmid/15467741&rft.aulast=Wiederhold&rft.aufirst=T&rft.au=Lee,+MF&rft.au=James,+M&rft.au=Neujahr,+R&rft.au=Smith,+N&rft.au=Murthy,+A&rft.au=Hartwig,+J&rft.au=Gusella,+JF&rft.au=Ramesh,+V&rft_id=https://doi.org/10.1038%2Fsj.onc.1208110&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
23. ^ Jannatipour M, Dion P, Khan S, Jindal H, Fan X, Laganière J, Chishti AH, Rouleau GA (August 2001). "Schwannomin isoform-1 interacts with syntenin via PDZ domains". J. Biol. Chem. 276 (35): 33093–100\. doi:10.1074/jbc.M105792200. PMID 11432873.33093-100&rft.date=2001-08&rft_id=info:doi/10.1074/jbc.M105792200&rft_id=info:pmid/11432873&rft.aulast=Jannatipour&rft.aufirst=M&rft.au=Dion,+P&rft.au=Khan,+S&rft.au=Jindal,+H&rft.au=Fan,+X&rft.au=Laganière,+J&rft.au=Chishti,+AH&rft.au=Rouleau,+GA&rft_id=https://doi.org/10.1074%2Fjbc.M105792200&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">
24. ^ Neill GW, Crompton MR (September 2001). "Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains". Biochem. J. 358 (Pt 3): 727–35\. doi:10.1042/0264-6021:3580727. PMC 1222106. PMID 11535133.727-35&rft.date=2001-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222106#id-name=PMC&rft_id=info:pmid/11535133&rft_id=info:doi/10.1042/0264-6021:3580727&rft.aulast=Neill&rft.aufirst=GW&rft.au=Crompton,+MR&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222106&rfr_id=info:sid/en.wikipedia.org:Merlin+(protein)" class="Z3988">

## External links

[edit]

* GeneReviews/NCBI/NIH/UW entry on Neurofibromatosis 2
* FlyBase synopsis of gene Mer

* v
* t
* e

Tumor suppressor genes and Oncogenes

Ligand|

| Growth factors|

| ONCO|

* c-Sis/PDGF
* HGF

|

Receptor|

| Wnt signaling pathway|

| TSP|

* CDH1

|

Hedgehog signaling pathway|

| TSP|

* PTCH1

|

TGF beta signaling pathway|

| TSP|

* TGF beta receptor 2

|

Receptor tyrosine kinase|

| ONCO|

* ErbB/c-ErbB
* HER2/neu
* Her 3
* c-Met
* c-Ret

|

JAK-STAT signaling pathway|

| ONCO|

* c-Kit
* Flt3

|

Intracellular signaling P+Ps|

| Wnt signaling pathway|

| ONCO|

* Beta-catenin

|

TSP|

* APC

TGF beta signaling pathway|

| TSP|

* SMAD2
* SMAD4

|

Akt/PKB signaling pathway|

| ONCO|

* c-Akt

|

TSP|

* PTEN

Hippo signaling pathway|

| TSP|

* Neurofibromin 2/Merlin

|

MAPK/ERK pathway|

| ONCO|

* c-Ras
* HRAS
* c-Raf

|

TSP|

* Neurofibromin 1

Other/unknown|

| ONCO|

* c-Src

|

TSP|

* Maspin

Nucleus|

| Cell cycle|

| ONCO|

* CDK4
* Cyclin D
* Cyclin E

|

TSP|

* p53
* pRb
* WT1
* p16/p14arf

DNA repair/Fanconi|

| TSP|

* BRCA1
* BRCA2

|

Ubiquitin ligase|

| ONCO|

* CBL
* MDM2

|

TSP|

* VHL

Transcription factor|

| ONCO|

* AP-1
* c-Fos
* c-Jun
* c-Myc

|

TSP|

* KLF6

Mitochondrion|

| Apoptosis inhibitor|

* SDHB
* SDHD

|

Other/ungrouped|

* c-Bcl-2
* Notch
* Stathmin

* v
* t
* e

Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin|

* SAG
* ARRB1
* ARRB2
* ARR3

Membrane-spanning 4A|

* MS4A1
* MS4A2
* MS4A3
* MS4A4A
* MS4A4E
* MS4A5
* MS4A6A
* MS4A6E
* MS4A7
* MS4A8B
* MS4A9
* MS4A10
* MS4A12
* MS4A13
* MS4A14
* MS4A15
* MS4A18

Myelin|

* Myelin basic protein
* PMP2
* Myelin proteolipid protein
* PLP1
* Myelin oligodendrocyte glycoprotein
* Myelin-associated glycoprotein
* Myelin protein zero

Pulmonary surfactant|

* Pulmonary surfactant-associated protein B
* Pulmonary surfactant-associated protein C

Tetraspanin|

* TSPAN1
* TSPAN2
* TSPAN3
* TSPAN4
* TSPAN5
* TSPAN6
* TSPAN7
* TSPAN8
* TSPAN9
* TSPAN10
* TSPAN11
* TSPAN12
* TSPAN13
* TSPAN14
* TSPAN15
* TSPAN16
* TSPAN17
* TSPAN18
* TSPAN19
* TSPAN20
* TSPAN21
* TSPAN22
* TSPAN23
* TSPAN24
* TSPAN25
* TSPAN26
* TSPAN27
* TSPAN28
* TSPAN29
* TSPAN30
* TSPAN31
* TSPAN32
* TSPAN33
* TSPAN34

Other/ungrouped|

* Calnexin
* LDL-receptor-related protein-associated protein
* Neurofibromin 2
* Presenilin
* PSEN1
* PSEN2
* HFE
* Phospholipid transfer proteins
* Dysferlin
* STRC
* OTOF

see also other cell membrane protein disorders

* v
* t
* e

Signaling pathway: Hippo signaling pathway

Receptor|

* FAT4

Adaptor protein|

* NF2
* FRMD6
* SAV1
* MOBKL1A
* MOBKL1B

Kinase|

* MST1
* LATS1
* LATS2
* STK3

Transcription factor|

* YAP1
* TAZ

Other/unknown|

* RASSF1

* v
* t
* e

PDB gallery

* 1h4r: CRYSTAL STRUCTURE OF THE FERM DOMAIN OF MERLIN, THE NEUROFIBROMATOSIS 2 TUMOR SUPPRESSOR PROTEIN.

* 1isn: Crystal structure of merlin FERM domain

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