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Merlin (Moesin-ezrin-radixin-like protein) (Neurofibromin-2) (Schwannomerlin) (Schwannomin)

 MERL_HUMAN              Reviewed;         595 AA.
P35240; O95683; Q8WUJ2; Q969N0; Q969Q3; Q96T30; Q96T31; Q96T32;
Q96T33; Q9BTW3; Q9UNG9; Q9UNH3; Q9UNH4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
18-JUL-2018, entry version 213.
RecName: Full=Merlin;
AltName: Full=Moesin-ezrin-radixin-like protein;
AltName: Full=Neurofibromin-2;
AltName: Full=Schwannomerlin;
AltName: Full=Schwannomin;
Name=NF2; Synonyms=SCH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8453669; DOI=10.1016/0092-8674(93)90406-G;
Trofatter J.A., Maccollin M.M., Rutter J.L., Murrell J.R., Duyao M.P.,
Parry D.N., Eldridge R., Kley N., Menon A.G., Pulaski K., Haase V.H.,
Ambrose C.M., Munroe D., Bove C., Haines J.L., Martuza R.L.,
Macdonald M.E., Seizinger B.R., Short M.P., Buckler A.J.,
Gusella J.F.;
"A novel moesin-, ezrin-, radixin-like gene is a candidate for the
neurofibromatosis 2 tumor suppressor.";
Cell 72:791-800(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8379998; DOI=10.1038/363515a0;
Rouleau G.A., Merel P., Lutchman M., Sanson M., Zucman J.,
Marineau C., Hoang-Xuan K., Demczuk S., Desmaze C., Plougastel B.,
Pulst S., Lenoir G., Bijlsma E., Fashold R., Dumanski J.P.,
de Jong P., Parry D., Eldrige R., Aurias A., Delattre O., Thomas G.;
"Alteration in a new gene encoding a putative membrane-organizing
protein causes neuro-fibromatosis type 2.";
Nature 363:515-521(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=9817927; DOI=10.1093/hmg/7.13.2095;
Zucman-Rossi J., Legoix P., Der Sarjussian H., Cheret G., Sor F.,
Bernardi A., Cazes L., Giraud S., Lenoir G., Thomas G.;
"NF2 gene in neurofibromatosis type 2 patients.";
Hum. Mol. Genet. 7:2095-2101(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9 AND 10), AND SUBCELLULAR
LOCATION.
PubMed=10401006; DOI=10.1093/hmg/8.8.1561;
Schmucker B., Tang Y., Kressel M.;
"Novel alternatively spliced isoforms of the neurofibromatosis type 2
tumor suppressor are targeted to the nucleus and cytoplasmic
granules.";
Hum. Mol. Genet. 8:1561-1570(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 8).
PubMed=11827459; DOI=10.1006/geno.2001.6672;
Chang L.-S., Akhmametyeva E.M., Wu Y., Zhu L., Welling D.B.;
"Multiple transcription initiation sites, alternative splicing, and
differential polyadenylation contribute to the complexity of human
neurofibromatosis 2 transcripts.";
Genomics 79:63-76(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
REVIEW.
Marineau C., Merel P., Rouleau G.A., Thomas G.;
"The gene of neurofibromatosis type 2.";
Medecine/Sciences 11:35-42(1995).
[9]
INTERACTION WITH SLC9A3R1.
PubMed=9430655; DOI=10.1074/jbc.273.3.1273;
Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C.,
Solomon F., Gusella J., Ramesh V.;
"NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common
interactor for merlin and ERM (MERM) proteins.";
J. Biol. Chem. 273:1273-1276(1998).
[10]
INTERACTION WITH HGS.
PubMed=10861283; DOI=10.1093/hmg/9.11.1567;
Scoles D.R., Huynh D.P., Chen M.S., Burke S.P., Gutmann D.H.,
Pulst S.-M.;
"The neurofibromatosis 2 tumor suppressor protein interacts with
hepatocyte growth factor-regulated tyrosine kinase substrate.";
Hum. Mol. Genet. 9:1567-1574(2000).
[11]
INTERACTION WITH SCHIP1, CHARACTERIZATION OF VARIANTS NF2 PHE-119 DEL,
AND CHARACTERIZATION OF VARIANT MET-219.
TISSUE=Brain;
PubMed=10669747; DOI=10.1128/MCB.20.5.1699-1712.2000;
Goutebroze L., Brault E., Muchardt C., Camonis J., Thomas G.;
"Cloning and characterization of SCHIP-1, a novel protein interacting
specifically with spliced isoforms and naturally occurring mutant NF2
proteins.";
Mol. Cell. Biol. 20:1699-1712(2000).
[12]
INVOLVEMENT IN MESOM.
PubMed=12136076; DOI=10.1212/WNL.59.2.290;
Baser M.E., De Rienzo A., Altomare D., Balsara B.R., Hedrick N.M.,
Gutmann D.H., Pitts L.H., Jackler R.K., Testa J.R.;
"Neurofibromatosis 2 and malignant mesothelioma.";
Neurology 59:290-291(2002).
[13]
INTERACTION WITH SGSM3.
PubMed=15541357; DOI=10.1016/j.bbrc.2004.10.095;
Lee I.K., Kim K.-S., Kim H., Lee J.Y., Ryu C.H., Chun H.J., Lee K.-U.,
Lim Y., Kim Y.H., Huh P.-W., Lee K.-H., Han S.-I., Jun T.-Y.,
Rha H.K.;
"MAP, a protein interacting with a tumor suppressor, merlin, through
the run domain.";
Biochem. Biophys. Res. Commun. 325:774-783(2004).
[14]
INTERACTION WITH AGAP2, AND MUTAGENESIS OF LEU-64.
PubMed=15598747; DOI=10.1073/pnas.0405971102;
Rong R., Tang X., Gutmann D.H., Ye K.;
"Neurofibromatosis 2 (NF2) tumor suppressor merlin inhibits
phosphatidylinositol 3-kinase through binding to PIKE-L.";
Proc. Natl. Acad. Sci. U.S.A. 101:18200-18205(2004).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
INTERACTION WITH DCAF1, AND UBIQUITINATION.
PubMed=18332868; DOI=10.1038/onc.2008.44;
Huang J., Chen J.;
"VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for
degradation.";
Oncogene 27:4056-4064(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
INTERACTION WITH MPP1, AND SUBCELLULAR LOCATION.
PubMed=19144871; DOI=10.3181/0809-RM-275;
Seo P.-S., Quinn B.J., Khan A.A., Zeng L., Takoudis C.G., Hanada T.,
Bolis A., Bolino A., Chishti A.H.;
"Identification of erythrocyte p55/MPP1 as a binding partner of NF2
tumor suppressor protein/Merlin.";
Exp. Biol. Med. 234:255-262(2009).
[19]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DCAF1 AND THE
CUL4A-RBX1-DDB1-VPRBP/DCAF1 E3 UBIQUITIN-PROTEIN LIGASE COMPLEX,
PHOSPHORYLATION, MUTAGENESIS OF LEU-64 AND SER-518, CHARACTERIZATION
OF VARIANT ARG-46, AND CHARACTERIZATION OF VARIANTS NF2 SER-62 AND
PRO-141.
PubMed=20178741; DOI=10.1016/j.cell.2010.01.029;
Li W., You L., Cooper J., Schiavon G., Pepe-Caprio A., Zhou L.,
Ishii R., Giovannini M., Hanemann C.O., Long S.B.,
Erdjument-Bromage H., Zhou P., Tempst P., Giancotti F.G.;
"Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin
ligase CRL4(DCAF1) in the nucleus.";
Cell 140:477-490(2010).
[20]
FUNCTION.
PubMed=20159598; DOI=10.1016/j.devcel.2009.12.012;
Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.;
"Kibra functions as a tumor suppressor protein that regulates Hippo
signaling in conjunction with Merlin and Expanded.";
Dev. Cell 18:288-299(2010).
[21]
INTERACTION WITH WWC1.
PubMed=20159599; DOI=10.1016/j.devcel.2009.12.011;
Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N.;
"Kibra Is a regulator of the Salvador/Warts/Hippo signaling network.";
Dev. Cell 18:300-308(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
FUNCTION, INTERACTION WITH NOP53, AND PHOSPHORYLATION.
PubMed=21167305; DOI=10.1016/j.biocel.2010.12.011;
Chen H., Mei L., Zhou L., Zhang X., Guo C., Li J., Wang H., Zhu Y.,
Zheng Y., Huang L.;
"Moesin-ezrin-radixin-like protein (merlin) mediates protein
interacting with the carboxyl terminus-1 (PICT-1)-induced growth
inhibition of glioblastoma cells in the nucleus.";
Int. J. Biochem. Cell Biol. 43:545-555(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-313.
PubMed=11856822; DOI=10.1107/S0907444901021175;
Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.;
"The structure of the FERM domain of merlin, the neurofibromatosis
type 2 gene product.";
Acta Crystallogr. D 58:381-391(2002).
[26]
VARIANT NF2 TYR-220.
PubMed=8230593; DOI=10.1001/jama.1993.03510190072029;
Maccollin M.M., Mohney T., Trofatter J.A., Wertelecki W., Ramesh V.,
Gusella J.F.;
"DNA diagnosis of neurofibromatosis 2. Altered coding sequence of the
merlin tumor suppressor in an extended pedigree.";
JAMA 270:2316-2320(1993).
[27]
VARIANT NF2 PHE-96 DEL.
PubMed=7913580;
Maccollin M.M., Ramesh V., Jacoby L.B., Louis D.N., Rubio M.-P.,
Pulaski K., Trofatter J.A., Short M.P., Bove C., Eldridge R.,
Parry D.M., Gusella J.F.;
"Mutational analysis of patients with neurofibromatosis 2.";
Am. J. Hum. Genet. 55:314-320(1994).
[28]
VARIANT ARG-46.
PubMed=8004107; DOI=10.1093/hmg/3.2.347;
Irving R.M., Moffat D.A., Hardy D.G., Barton D.E., Xuereb J.H.,
Maher E.R.;
"Somatic NF2 gene mutations in familial and non-familial vestibular
schwannoma.";
Hum. Mol. Genet. 3:347-350(1994).
[29]
VARIANTS MET-219 AND CYS-418.
PubMed=8012353; DOI=10.1093/hmg/3.3.413;
Jacoby L.B., Maccollin M.M., Louis D.N., Mohney T., Rubio M.-P.,
Pulaski K., Trofatter J.A., Kley N., Seizinger B.R., Ramesh V.,
Gusella J.F.;
"Exon scanning for mutation of the NF2 gene in schwannomas.";
Hum. Mol. Genet. 3:413-419(1994).
[30]
VARIANTS NF2 SER-62; GLY-106 AND MET-352.
PubMed=8081368; DOI=10.1093/hmg/3.5.813;
Bourn D., Carter S.A., Mason S., Gareth D., Evans R., Strachan T.;
"Germline mutations in the neurofibromatosis type 2 tumour suppressor
gene.";
Hum. Mol. Genet. 3:813-816(1994).
[31]
VARIANTS GLU-79 AND HIS-351.
PubMed=7951231; DOI=10.1093/hmg/3.6.885;
Sainz J., Huynh D.P., Figueroa K., Ragge N.K., Baser M.E., Pulst S.M.;
"Mutations of the neurofibromatosis type 2 gene and lack of the gene
product in vestibular schwannomas.";
Hum. Mol. Genet. 3:885-891(1994).
[32]
VARIANTS PHE-273 AND ILE-364.
PubMed=8162073; DOI=10.1038/ng0294-185;
Bianchi A.B., Hara T., Ramesh V., Gao J., Klein Szanto A.J., Morin F.,
Menon A.G., Trofatter J.A., Gusella J.F., Seizinger B.R., Kley N.;
"Mutations in transcript isoforms of the neurofibromatosis 2 gene in
multiple human tumour types.";
Nat. Genet. 6:185-192(1994).
[33]
VARIANTS NF2 PHE-119 DEL; GLU-413 AND PRO-535.
PubMed=7759081; DOI=10.1007/BF00223872;
Bourn D., Evans G., Mason S., Tekes S., Trueman L., Strachan T.;
"Eleven novel mutations in the NF2 tumour suppressor gene.";
Hum. Genet. 95:572-574(1995).
[34]
VARIANT NF2 PRO-535.
PubMed=7666400; DOI=10.1136/jmg.32.6.470;
Evans D.G.R., Bourn D., Wallace A., Ramsden R.T., Mitchell J.D.,
Strachan T.;
"Diagnostic issues in a family with late onset type 2
neurofibromatosis.";
J. Med. Genet. 32:470-474(1995).
[35]
VARIANT NF2 PRO-538.
PubMed=8566958; DOI=10.1007/BF02265270;
Kluwe L., Mautner V.-F.;
"A missense mutation in the NF2 gene results in moderate and mild
clinical phenotypes of neurofibromatosis type 2.";
Hum. Genet. 97:224-227(1996).
[36]
VARIANTS PHE-96 DEL; ILE-117; PHE-119 DEL; 122-VAL--GLU-129 DEL AND
PHE-339.
PubMed=8655144; DOI=10.1007/BF02281874;
de Vitis L.R., Tedde A., Vitelli F., Ammannati F., Mennonna P.,
Bigozzi U., Montali E., Papi L.;
"Screening for mutations in the neurofibromatosis type 2 (NF2) gene in
sporadic meningiomas.";
Hum. Genet. 97:632-637(1996).
[37]
VARIANTS NF2 CYS-197 AND HIS-539.
PubMed=8698340; DOI=10.1007/s004390050188;
Welling D.B., Guida M., Goll F., Pearl D.K., Glasscock M.E.,
Pappas D.G., Linthicum F.H., Rogers D., Prior T.W.;
"Mutational spectrum in the neurofibromatosis type 2 gene in sporadic
and familial schwannomas.";
Hum. Genet. 98:189-193(1996).
[38]
VARIANTS NF2 SER-62; VAL-77; GLY-106; MET-352; GLU-413 AND PRO-535.
PubMed=9643284; DOI=10.1136/jmg.35.6.450;
Evans D.G.R., Trueman L., Wallace A., Collins S., Strachan T.;
"Genotype/phenotype correlations in type 2 neurofibromatosis (NF2):
evidence for more severe disease associated with truncating
mutations.";
J. Med. Genet. 35:450-455(1998).
[39]
ERRATUM.
Evans D.G., Trueman L., Wallace A., Collins S., Strachan T.;
J. Med. Genet. 36:87-87(1999).
[40]
VARIANT NF2 ARG-234.
PubMed=10090912; DOI=10.1086/302338;
Baser M.E., Kluwe L., Mautner V.-F.;
"Germ-line NF2 mutations and disease severity in neurofibromatosis
type 2 patients with retinal abnormalities.";
Am. J. Hum. Genet. 64:1230-1233(1999).
[41]
VARIANTS NF2 SER-62; THR-533 AND MET-579.
PubMed=10790209;
DOI=10.1002/(SICI)1098-1004(200005)15:5<474::AID-HUMU9>3.0.CO;2-7;
Faudoa R., Xue Z., Lee F., Baser M.E., Hung G.;
"Detection of novel NF2 mutations by an RNA mismatch cleavage
method.";
Hum. Mutat. 15:474-478(2000).
[42]
VARIANT NF2 PRO-141.
PubMed=12709270; DOI=10.1016/S1472-6483(10)61809-3;
Verlinsky Y., Rechitsky S., Verlinsky O., Chistokhina A.,
Sharapova T., Masciangelo C., Levy M., Kaplan B., Lederer K.,
Kuliev A.;
"Preimplantation diagnosis for neurofibromatosis.";
Reprod. BioMed. Online 4:218-222(2002).
[43]
VARIANT [LARGE SCALE ANALYSIS] LYS-463.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[44]
INVOLVEMENT IN SWNTS1.
PubMed=18072270; DOI=10.1002/humu.20679;
Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L.;
"Evidence of a four-hit mechanism involving SMARCB1 and NF2 in
schwannomatosis-associated schwannomas.";
Hum. Mutat. 29:227-231(2008).
[45]
VARIANT NF2 ARG-133.
PubMed=20445339; DOI=10.3343/kjlm.2010.30.2.190;
Seong M.W., Yeo I.K., Cho S.I., Park C.K., Kim S.K., Paek S.H.,
Kim D.G., Jung H.W., Park H., Kim S.Y., Kim J.Y., Park S.S.;
"Molecular characterization of the NF2 gene in Korean patients with
neurofibromatosis type 2: a report of four novel mutations.";
Korean J. Lab. Med. 30:190-194(2010).
-!- FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo)
signaling pathway, a signaling pathway that plays a pivotal role
in tumor suppression by restricting proliferation and promoting
apoptosis. Along with WWC1 can synergistically induce the
phosphorylation of LATS1 and LATS2 and can probably function in
the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway.
May act as a membrane stabilizing protein. May inhibit PI3 kinase
by binding to AGAP2 and impairing its stimulating activity.
Suppresses cell proliferation and tumorigenesis by inhibiting the
CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.
{ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741,
ECO:0000269|PubMed:21167305}.
-!- SUBUNIT: Interacts with SLC9A3R1, HGS and AGAP2. Interacts with
LAYN (By similarity). Interacts with SGSM3. Interacts (via FERM
domain) with MPP1. Interacts with WWC1. Interacts with the CUL4A-
RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The
unphosphorylated form interacts (via FERM domain) with
VPRBP/DCAF1. Interacts (via FERM domain) with NOP53; the
interaction is direct (PubMed:21167305). Interacts with SCHIP1;
the interaction is direct (PubMed:10669747). {ECO:0000250,
ECO:0000269|PubMed:10669747, ECO:0000269|PubMed:10861283,
ECO:0000269|PubMed:15541357, ECO:0000269|PubMed:15598747,
ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:19144871,
ECO:0000269|PubMed:20159599, ECO:0000269|PubMed:20178741,
ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:9430655}.
-!- INTERACTION:
E2RJV1:AMOT (xeno); NbExp=2; IntAct=EBI-1014500, EBI-16145865;
Q4VCS5:AMOT; NbExp=8; IntAct=EBI-1014472, EBI-2511319;
Q4VCS5-1:AMOT; NbExp=2; IntAct=EBI-1014472, EBI-3903812;
Q4VCS5-2:AMOT; NbExp=6; IntAct=EBI-1014472, EBI-3891843;
Q9BZE4:GTPBP4; NbExp=9; IntAct=EBI-1014472, EBI-1056249;
O95835:LATS1; NbExp=4; IntAct=EBI-1014472, EBI-444209;
Q16584:MAP3K11; NbExp=4; IntAct=EBI-1014472, EBI-49961;
Q9H204:MED28; NbExp=4; IntAct=EBI-1014472, EBI-514199;
F1PFK4:PARD3 (xeno); NbExp=2; IntAct=EBI-1014500, EBI-16145946;
Q8NI35:PATJ; NbExp=2; IntAct=EBI-1014472, EBI-724390;
Q10728:Ppp1r12a (xeno); NbExp=2; IntAct=EBI-1014472, EBI-918263;
P0DPB4:Schip1 (xeno); NbExp=2; IntAct=EBI-1014472, EBI-1397475;
O14745:SLC9A3R1; NbExp=4; IntAct=EBI-1014500, EBI-349787;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell projection, filopodium
membrane; Peripheral membrane protein; Cytoplasmic side. Cell
projection, ruffle membrane; Peripheral membrane protein;
Cytoplasmic side. Nucleus. Note=In a fibroblastic cell line,
isoform 1 is found homogeneously distributed over the entire cell,
with a particularly strong staining in ruffling membranes and
filopodia. Colocalizes with MPP1 in non-myelin-forming Schwann
cells. Binds with DCAF1 in the nucleus. The intramolecular
association of the FERM domain with the C-terminal tail promotes
nuclear accumulation. The unphosphorylated form accumulates
predominantly in the nucleus while the phosphorylated form is
largely confined to the non-nuclear fractions.
-!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, perinuclear region.
Cytoplasmic granule. Note=Observed in cytoplasmic granules
concentrated in a perinuclear location. Isoform 7 is absent from
ruffling membranes and filopodia.
-!- SUBCELLULAR LOCATION: Isoform 9: Cytoplasm, perinuclear region.
Cytoplasmic granule. Note=Observed in cytoplasmic granules
concentrated in a perinuclear location. Isoform 9 is absent from
ruffling membranes and filopodia.
-!- SUBCELLULAR LOCATION: Isoform 10: Nucleus. Cell projection,
filopodium membrane; Peripheral membrane protein; Cytoplasmic
side. Cell projection, ruffle membrane; Peripheral membrane
protein; Cytoplasmic side. Cytoplasm, perinuclear region.
Cytoplasmic granule. Cytoplasm, cytoskeleton. Note=In a
fibroblastic cell line, isoform 10 is found homogeneously
distributed over the entire cell, with a particularly strong
staining in ruffling membranes and filopodia.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1; Synonyms=I;
IsoId=P35240-1; Sequence=Displayed;
Name=2;
IsoId=P35240-2; Sequence=VSP_000492;
Name=3; Synonyms=II;
IsoId=P35240-3; Sequence=VSP_007050, VSP_007051;
Name=4; Synonyms=delE2/3;
IsoId=P35240-4; Sequence=VSP_007041, VSP_007050, VSP_007051;
Name=5; Synonyms=delE3;
IsoId=P35240-5; Sequence=VSP_007042, VSP_007050, VSP_007051;
Name=6; Synonyms=delE2;
IsoId=P35240-6; Sequence=VSP_007040, VSP_007050, VSP_007051;
Name=7; Synonyms=MER150;
IsoId=P35240-7; Sequence=VSP_007045, VSP_007046;
Name=8;
IsoId=P35240-8; Sequence=VSP_007048, VSP_007050, VSP_007051;
Name=9; Synonyms=MER162;
IsoId=P35240-9; Sequence=VSP_007044;
Name=10; Synonyms=MER151;
IsoId=P35240-10; Sequence=VSP_007041, VSP_007043, VSP_007047,
VSP_007049;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 3 are
predominant. Isoform 4, isoform 5 and isoform 6 are expressed
moderately. Isoform 8 is found at low frequency. Isoform 7,
isoform 9 and isoform 10 are not expressed in adult tissues, with
the exception of adult retina expressing isoform 10. Isoform 9 is
faintly expressed in fetal brain, heart, lung, skeletal muscle and
spleen. Fetal thymus expresses isoforms 1, 7, 9 and 10 at similar
levels.
-!- PTM: Phosphorylation of Ser-518 inhibits nuclear localization by
disrupting the intramolecular association of the FERM domain with
the C-terminal tail (PubMed:20178741). The dephosphorylation of
Ser-518 favors the interaction with NOP53 (PubMed:21167305).
{ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}.
-!- PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3
ubiquitin-protein ligase complex for ubiquitination and subsequent
proteasome-dependent degradation. {ECO:0000269|PubMed:18332868}.
-!- DISEASE: Neurofibromatosis 2 (NF2) [MIM:101000]: Genetic disorder
characterized by bilateral vestibular schwannomas (formerly called
acoustic neuromas), schwannomas of other cranial and peripheral
nerves, meningiomas, and ependymomas. It is inherited in an
autosomal dominant fashion with full penetrance. Affected
individuals generally develop symptoms of eighth-nerve dysfunction
in early adulthood, including deafness and balance disorder.
Although the tumors of NF2 are histologically benign, their
anatomic location makes management difficult, and patients suffer
great morbidity and mortality. {ECO:0000269|PubMed:10090912,
ECO:0000269|PubMed:10669747, ECO:0000269|PubMed:10790209,
ECO:0000269|PubMed:12709270, ECO:0000269|PubMed:20178741,
ECO:0000269|PubMed:20445339, ECO:0000269|PubMed:7666400,
ECO:0000269|PubMed:7759081, ECO:0000269|PubMed:7913580,
ECO:0000269|PubMed:8081368, ECO:0000269|PubMed:8230593,
ECO:0000269|PubMed:8566958, ECO:0000269|PubMed:8698340,
ECO:0000269|PubMed:9643284}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer
syndrome in which patients develop multiple non-vestibular
schwannomas, benign neoplasms that arise from Schwann cells of the
cranial, peripheral, and autonomic nerves.
{ECO:0000269|PubMed:18072270}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An
aggressive neoplasm of the serosal lining of the chest. It appears
as broad sheets of cells, with some regions containing spindle-
shaped, sarcoma-like cells and other regions showing adenomatous
patterns. Pleural mesotheliomas have been linked to exposure to
asbestos. {ECO:0000269|PubMed:12136076}. Note=The disease may be
caused by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NF2ID117.html";
-----------------------------------------------------------------------
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EMBL; L11353; AAA36212.1; -; mRNA.
EMBL; X72655; CAA51220.1; -; Genomic_DNA.
EMBL; X72656; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72657; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72658; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72659; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72660; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72661; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72662; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72663; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72664; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72665; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72666; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72667; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72668; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72669; CAA51220.1; JOINED; Genomic_DNA.
EMBL; X72670; CAA51220.1; JOINED; Genomic_DNA.
EMBL; Z22664; CAA80377.1; -; mRNA.
EMBL; Y18000; CAA76992.1; -; Genomic_DNA.
EMBL; Y18000; CAA76993.1; -; Genomic_DNA.
EMBL; AF122827; AAD48752.1; -; mRNA.
EMBL; AF122828; AAD48753.1; -; mRNA.
EMBL; AF123570; AAD48754.1; -; mRNA.
EMBL; AF369657; AAK54160.1; -; mRNA.
EMBL; AF369658; AAK54161.1; -; mRNA.
EMBL; AF369661; AAK54162.1; -; mRNA.
EMBL; AF369662; AAK54163.1; -; mRNA.
EMBL; AF369663; AAK54164.1; -; mRNA.
EMBL; AF369664; AAK54165.1; -; mRNA.
EMBL; AF369665; AAK54166.1; -; mRNA.
EMBL; AF369700; AAK54195.1; -; mRNA.
EMBL; AF369701; AAK54196.1; -; mRNA.
EMBL; CR456530; CAG30416.1; -; mRNA.
EMBL; BC003112; AAH03112.2; -; mRNA.
EMBL; BC020257; AAH20257.1; -; mRNA.
CCDS; CCDS13861.1; -. [P35240-1]
CCDS; CCDS13862.1; -. [P35240-3]
CCDS; CCDS13863.1; -. [P35240-6]
CCDS; CCDS13864.1; -. [P35240-5]
CCDS; CCDS13865.1; -. [P35240-4]
CCDS; CCDS54516.1; -. [P35240-9]
PIR; S33809; S33809.
RefSeq; NP_000259.1; NM_000268.3. [P35240-1]
RefSeq; NP_057502.2; NM_016418.5. [P35240-3]
RefSeq; NP_861546.1; NM_181825.2. [P35240-3]
RefSeq; NP_861966.1; NM_181828.2. [P35240-6]
RefSeq; NP_861967.1; NM_181829.2. [P35240-5]
RefSeq; NP_861968.1; NM_181830.2. [P35240-4]
RefSeq; NP_861969.1; NM_181831.2. [P35240-4]
RefSeq; NP_861970.1; NM_181832.2. [P35240-3]
RefSeq; NP_861971.1; NM_181833.2. [P35240-9]
UniGene; Hs.187898; -.
PDB; 1H4R; X-ray; 1.80 A; A/B=1-313.
PDB; 3U8Z; X-ray; 2.64 A; A/B/C/D=18-312.
PDB; 4ZRI; X-ray; 2.70 A; A/B=1-320.
PDB; 4ZRJ; X-ray; 2.30 A; A=1-320, B=506-595.
PDBsum; 1H4R; -.
PDBsum; 3U8Z; -.
PDBsum; 4ZRI; -.
PDBsum; 4ZRJ; -.
ProteinModelPortal; P35240; -.
SMR; P35240; -.
BioGrid; 110844; 214.
CORUM; P35240; -.
DIP; DIP-35389N; -.
ELM; P35240; -.
IntAct; P35240; 40.
MINT; P35240; -.
STRING; 9606.ENSP00000344666; -.
CarbonylDB; P35240; -.
iPTMnet; P35240; -.
PhosphoSitePlus; P35240; -.
BioMuta; NF2; -.
DMDM; 462594; -.
EPD; P35240; -.
MaxQB; P35240; -.
PaxDb; P35240; -.
PeptideAtlas; P35240; -.
PRIDE; P35240; -.
ProteomicsDB; 54999; -.
ProteomicsDB; 55000; -. [P35240-10]
ProteomicsDB; 55001; -. [P35240-2]
ProteomicsDB; 55002; -. [P35240-3]
ProteomicsDB; 55003; -. [P35240-4]
ProteomicsDB; 55004; -. [P35240-5]
ProteomicsDB; 55005; -. [P35240-6]
ProteomicsDB; 55006; -. [P35240-7]
ProteomicsDB; 55007; -. [P35240-8]
ProteomicsDB; 55008; -. [P35240-9]
DNASU; 4771; -.
Ensembl; ENST00000334961; ENSP00000335652; ENSG00000186575. [P35240-4]
Ensembl; ENST00000338641; ENSP00000344666; ENSG00000186575. [P35240-1]
Ensembl; ENST00000353887; ENSP00000340626; ENSG00000186575. [P35240-4]
Ensembl; ENST00000361166; ENSP00000354529; ENSG00000186575. [P35240-3]
Ensembl; ENST00000361452; ENSP00000354897; ENSG00000186575. [P35240-5]
Ensembl; ENST00000361676; ENSP00000355183; ENSG00000186575. [P35240-6]
Ensembl; ENST00000397789; ENSP00000380891; ENSG00000186575. [P35240-3]
Ensembl; ENST00000403435; ENSP00000384029; ENSG00000186575. [P35240-8]
Ensembl; ENST00000403999; ENSP00000384797; ENSG00000186575. [P35240-3]
Ensembl; ENST00000413209; ENSP00000409921; ENSG00000186575. [P35240-9]
Ensembl; ENST00000432151; ENSP00000395885; ENSG00000186575. [P35240-10]
GeneID; 4771; -.
KEGG; hsa:4771; -.
UCSC; uc003afy.5; human. [P35240-1]
CTD; 4771; -.
DisGeNET; 4771; -.
EuPathDB; HostDB:ENSG00000186575.17; -.
GeneCards; NF2; -.
GeneReviews; NF2; -.
HGNC; HGNC:7773; NF2.
HPA; CAB005385; -.
HPA; HPA003097; -.
MalaCards; NF2; -.
MIM; 101000; phenotype.
MIM; 156240; phenotype.
MIM; 162091; phenotype.
MIM; 607379; gene.
neXtProt; NX_P35240; -.
OpenTargets; ENSG00000186575; -.
Orphanet; 637; Neurofibromatosis type 2.
Orphanet; 93921; Neurofibromatosis type 3.
PharmGKB; PA31580; -.
eggNOG; KOG3529; Eukaryota.
eggNOG; ENOG410XQFP; LUCA.
GeneTree; ENSGT00920000148976; -.
HOVERGEN; HBG002185; -.
InParanoid; P35240; -.
KO; K16684; -.
OMA; MQRIKVT; -.
OrthoDB; EOG091G06UO; -.
PhylomeDB; P35240; -.
TreeFam; TF313935; -.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
SignaLink; P35240; -.
SIGNOR; P35240; -.
ChiTaRS; NF2; human.
EvolutionaryTrace; P35240; -.
GeneWiki; Merlin_(protein); -.
GenomeRNAi; 4771; -.
PMAP-CutDB; P35240; -.
PRO; PR:P35240; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000186575; -.
ExpressionAtlas; P35240; baseline and differential.
Genevisible; P35240; HS.
GO; GO:0005912; C:adherens junction; IEA:Ensembl.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IDA:HGNC.
GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HGNC.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:HGNC.
GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl.
GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; TAS:HGNC.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:HGNC.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; TAS:HGNC.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IDA:HGNC.
GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:HGNC.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:HGNC.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
GO; GO:0014013; P:regulation of gliogenesis; IEA:Ensembl.
GO; GO:0035330; P:regulation of hippo signaling; IMP:UniProtKB.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
GO; GO:0072091; P:regulation of stem cell proliferation; IEA:Ensembl.
GO; GO:0014010; P:Schwann cell proliferation; IMP:HGNC.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 1.25.40.1020; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR011174; ERM.
InterPro; IPR011259; ERM_C_dom.
InterPro; IPR000798; Ez/rad/moesin-like.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR019747; FERM_CS.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR008954; Moesin_tail_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF00769; ERM; 1.
Pfam; PF09380; FERM_C; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
PIRSF; PIRSF002305; ERM; 1.
PRINTS; PR00935; BAND41.
PRINTS; PR00661; ERMFAMILY.
SMART; SM00295; B41; 1.
SMART; SM01196; FERM_C; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF48678; SSF48678; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00660; FERM_1; 1.
PROSITE; PS00661; FERM_2; 1.
PROSITE; PS50057; FERM_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Deafness;
Disease mutation; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Tumor suppressor; Ubl conjugation.
CHAIN 1 595 Merlin.
/FTId=PRO_0000219412.
DOMAIN 22 311 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
COMPBIAS 327 465 Glu-rich.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 518 518 Phosphoserine; by PAK.
{ECO:0000244|PubMed:17081983}.
VAR_SEQ 39 121 Missing (in isoform 4 and isoform 10).
{ECO:0000303|PubMed:10401006,
ECO:0000303|PubMed:11827459,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007041.
VAR_SEQ 39 80 Missing (in isoform 6).
{ECO:0000303|PubMed:11827459}.
/FTId=VSP_007040.
VAR_SEQ 81 121 Missing (in isoform 5).
{ECO:0000303|PubMed:11827459}.
/FTId=VSP_007042.
VAR_SEQ 150 579 Missing (in isoform 9).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007044.
VAR_SEQ 150 225 Missing (in isoform 10).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007043.
VAR_SEQ 259 259 N -> R (in isoform 7).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007045.
VAR_SEQ 260 595 Missing (in isoform 7).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007046.
VAR_SEQ 334 379 MERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL
MRSEE -> GQRGRSAEAGPAGSTRGGAKSQAEAPGDCHQA
HVPAHEPNSSTVAS (in isoform 10).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007047.
VAR_SEQ 335 363 Missing (in isoform 8).
{ECO:0000303|PubMed:11827459}.
/FTId=VSP_007048.
VAR_SEQ 380 595 Missing (in isoform 10).
{ECO:0000303|PubMed:10401006}.
/FTId=VSP_007049.
VAR_SEQ 580 595 LTLQSAKSRVAFFEEL -> SSPRQKTYLHLSPQSRLFPGT
LYVVMLYVVMVLPSVILTRA (in isoform 2).
{ECO:0000305}.
/FTId=VSP_000492.
VAR_SEQ 580 590 LTLQSAKSRVA -> PQAQGRRPICI (in isoform 3,
isoform 4, isoform 5, isoform 6 and
isoform 8). {ECO:0000303|PubMed:11827459,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007050.
VAR_SEQ 591 595 Missing (in isoform 3, isoform 4, isoform
5, isoform 6 and isoform 8).
{ECO:0000303|PubMed:11827459,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007051.
VARIANT 46 46 L -> R (in vestibular schwannoma; loss of
ability to interact with the CUL4A-RBX1-
DDB1-VprBP/DCAF1 E3 ubiquitin-protein
ligase complex).
{ECO:0000269|PubMed:20178741,
ECO:0000269|PubMed:8004107}.
/FTId=VAR_000809.
VARIANT 62 62 F -> S (in NF2; loss of ability to
interact with the CUL4A-RBX1-DDB1-VprBP/
DCAF1 E3 ubiquitin-protein ligase
complex; dbSNP:rs121434261).
{ECO:0000269|PubMed:10790209,
ECO:0000269|PubMed:20178741,
ECO:0000269|PubMed:8081368,
ECO:0000269|PubMed:9643284}.
/FTId=VAR_000810.
VARIANT 77 77 M -> V (in NF2).
{ECO:0000269|PubMed:9643284}.
/FTId=VAR_043011.
VARIANT 79 79 K -> E (in vestibular schwannoma).
{ECO:0000269|PubMed:7951231}.
/FTId=VAR_000811.
VARIANT 96 96 Missing (in NF2; also found in sporadic
meningioma). {ECO:0000269|PubMed:7913580,
ECO:0000269|PubMed:8655144}.
/FTId=VAR_000812.
VARIANT 106 106 E -> G (in NF2).
{ECO:0000269|PubMed:8081368,
ECO:0000269|PubMed:9643284}.
/FTId=VAR_000813.
VARIANT 117 117 L -> I (in sporadic meningioma).
{ECO:0000269|PubMed:8655144}.
/FTId=VAR_000814.
VARIANT 119 119 Missing (in sporadic meningioma; no
effect on interaction with SCHIP1).
{ECO:0000269|PubMed:10669747,
ECO:0000269|PubMed:7759081,
ECO:0000269|PubMed:8655144}.
/FTId=VAR_000815.
VARIANT 122 129 Missing (in sporadic meningioma).
{ECO:0000269|PubMed:8655144}.
/FTId=VAR_000816.
VARIANT 133 133 C -> R (in NF2).
{ECO:0000269|PubMed:20445339}.
/FTId=VAR_065227.
VARIANT 141 141 L -> P (in NF2; loss of ability to
interact with the CUL4A-RBX1-DDB1-VprBP/
DCAF1 E3 ubiquitin-protein ligase
complex). {ECO:0000269|PubMed:12709270,
ECO:0000269|PubMed:20178741}.
/FTId=VAR_043012.
VARIANT 197 197 G -> C (in NF2).
{ECO:0000269|PubMed:8698340}.
/FTId=VAR_043013.
VARIANT 219 219 V -> M (in vestibular schwannoma; changed
interaction with SCHIP1).
{ECO:0000269|PubMed:10669747,
ECO:0000269|PubMed:8012353}.
/FTId=VAR_000817.
VARIANT 220 220 N -> Y (in NF2).
{ECO:0000269|PubMed:8230593}.
/FTId=VAR_000818.
VARIANT 234 234 L -> R (in NF2; also found in retinal
hamartoma; severe).
{ECO:0000269|PubMed:10090912}.
/FTId=VAR_009123.
VARIANT 273 273 I -> F (in breast ductal carcinoma).
{ECO:0000269|PubMed:8162073}.
/FTId=VAR_000819.
VARIANT 339 339 L -> F (in sporadic meningioma).
{ECO:0000269|PubMed:8655144}.
/FTId=VAR_000820.
VARIANT 351 351 R -> H (in dbSNP:rs771675702).
{ECO:0000269|PubMed:7951231}.
/FTId=VAR_029041.
VARIANT 352 352 T -> M (in NF2; dbSNP:rs764441073).
{ECO:0000269|PubMed:8081368,
ECO:0000269|PubMed:9643284}.
/FTId=VAR_000821.
VARIANT 360 360 L -> P (in NF2; dbSNP:rs74315492).
/FTId=VAR_000822.
VARIANT 364 364 K -> I (in melanoma).
{ECO:0000269|PubMed:8162073}.
/FTId=VAR_000823.
VARIANT 413 413 K -> E (in NF2; dbSNP:rs766974263).
{ECO:0000269|PubMed:7759081,
ECO:0000269|PubMed:9643284}.
/FTId=VAR_043014.
VARIANT 418 418 R -> C (in vestibular schwannoma;
dbSNP:rs765540111).
{ECO:0000269|PubMed:8012353}.
/FTId=VAR_000824.
VARIANT 463 463 E -> K (in a breast cancer sample;
somatic mutation; dbSNP:rs74315503).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035848.
VARIANT 533 533 K -> T (in NF2).
{ECO:0000269|PubMed:10790209}.
/FTId=VAR_043015.
VARIANT 535 535 L -> P (in NF2; late onset;
dbSNP:rs74315493).
{ECO:0000269|PubMed:7666400,
ECO:0000269|PubMed:7759081,
ECO:0000269|PubMed:9643284}.
/FTId=VAR_000825.
VARIANT 538 538 Q -> P (in NF2; mild; dbSNP:rs74315494).
{ECO:0000269|PubMed:8566958}.
/FTId=VAR_000826.
VARIANT 539 539 L -> H (in NF2).
{ECO:0000269|PubMed:8698340}.
/FTId=VAR_043016.
VARIANT 579 579 K -> M (in NF2).
{ECO:0000269|PubMed:10790209}.
/FTId=VAR_043017.
MUTAGEN 64 64 L->P: Abolishes binding to AGAP2 and
interaction with the CUL4A-RBX1-DDB1-
VprBP/DCAF1 E3 ubiquitin-protein ligase
complex. {ECO:0000269|PubMed:15598747,
ECO:0000269|PubMed:20178741}.
MUTAGEN 518 518 S->A: Loss of phosphorylation.
Significant accumulation in the nucleus
and no effect on binding to DCAF1.
{ECO:0000269|PubMed:20178741}.
MUTAGEN 518 518 S->D: No effect on phosphorylation.
Defective nuclear accumulation.
Significant decrease in binding to DCAF1
and in ability to inhibit cell
proliferation.
{ECO:0000269|PubMed:20178741}.
CONFLICT 77 77 M -> I (in Ref. 7; AAH20257).
{ECO:0000305}.
CONFLICT 581 581 T -> P (in Ref. 5; AAK54160/AAK54162).
{ECO:0000305}.
STRAND 21 27 {ECO:0000244|PDB:1H4R}.
STRAND 32 38 {ECO:0000244|PDB:1H4R}.
HELIX 43 54 {ECO:0000244|PDB:1H4R}.
HELIX 59 61 {ECO:0000244|PDB:1H4R}.
STRAND 62 68 {ECO:0000244|PDB:1H4R}.
STRAND 71 74 {ECO:0000244|PDB:1H4R}.
STRAND 77 80 {ECO:0000244|PDB:4ZRJ}.
HELIX 81 83 {ECO:0000244|PDB:1H4R}.
STRAND 84 86 {ECO:0000244|PDB:4ZRJ}.
STRAND 89 100 {ECO:0000244|PDB:1H4R}.
HELIX 105 108 {ECO:0000244|PDB:1H4R}.
HELIX 112 127 {ECO:0000244|PDB:1H4R}.
HELIX 135 150 {ECO:0000244|PDB:1H4R}.
TURN 155 157 {ECO:0000244|PDB:1H4R}.
TURN 160 165 {ECO:0000244|PDB:1H4R}.
HELIX 171 174 {ECO:0000244|PDB:1H4R}.
HELIX 181 193 {ECO:0000244|PDB:1H4R}.
TURN 194 197 {ECO:0000244|PDB:1H4R}.
HELIX 200 211 {ECO:0000244|PDB:1H4R}.
TURN 215 218 {ECO:0000244|PDB:1H4R}.
STRAND 220 226 {ECO:0000244|PDB:1H4R}.
STRAND 231 236 {ECO:0000244|PDB:1H4R}.
STRAND 238 244 {ECO:0000244|PDB:1H4R}.
STRAND 249 251 {ECO:0000244|PDB:1H4R}.
STRAND 253 257 {ECO:0000244|PDB:1H4R}.
HELIX 258 260 {ECO:0000244|PDB:1H4R}.
STRAND 261 267 {ECO:0000244|PDB:1H4R}.
STRAND 270 277 {ECO:0000244|PDB:1H4R}.
STRAND 283 286 {ECO:0000244|PDB:1H4R}.
HELIX 290 310 {ECO:0000244|PDB:1H4R}.
HELIX 513 547 {ECO:0000244|PDB:4ZRJ}.
HELIX 552 554 {ECO:0000244|PDB:4ZRJ}.
HELIX 557 562 {ECO:0000244|PDB:4ZRJ}.
HELIX 573 581 {ECO:0000244|PDB:4ZRJ}.
HELIX 585 594 {ECO:0000244|PDB:4ZRJ}.
SEQUENCE 595 AA; 69690 MW; B1A1BF2BD5DA561C CRC64;
MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV CRTLGLRETW
FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF YPENAEEELV QEITQHLFFL
QVKKQILDEK IYCPPEASVL LASYAVQAKY GDYDPSVHKR GFLAQEELLP KRVINLYQMT
PEMWEERITA WYAEHRGRAR DEAEMEYLKI AQDLEMYGVN YFAIRNKKGT ELLLGVDALG
LHIYDPENRL TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC
IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE RTRDELERRL
LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ KAAEAEQEMQ RIKATAIRTE
EEKRLMEQKV LEAEVLALKM AEESERRAKE ADQLKQDLQE AREAERRAKQ KLLEIATKPT
YPPMNPIPAP LPPDIPSFNL IGDSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN
ELKTEIEALK LKERETALDI LHNENSDRGG SSKHNTIKKL TLQSAKSRVA FFEEL


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