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P46662

- MERL_MOUSE

UniProt

P46662 - MERL_MOUSE

Protein

Merlin

Gene

Nf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (27 Jun 2003)
      Previous versions | rss
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    Functioni

    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 By similarity. Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.By similarity1 Publication

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. brain development Source: MGI
    3. cell-cell junction organization Source: MGI
    4. ectoderm development Source: MGI
    5. hippocampus development Source: MGI
    6. lens fiber cell differentiation Source: UniProtKB
    7. mesoderm formation Source: MGI
    8. negative regulation of cell-cell adhesion Source: Ensembl
    9. negative regulation of cell proliferation Source: MGI
    10. negative regulation of DNA replication Source: Ensembl
    11. negative regulation of MAPK cascade Source: MGI
    12. negative regulation of protein kinase activity Source: MGI
    13. negative regulation of tyrosine phosphorylation of Stat3 protein Source: Ensembl
    14. negative regulation of tyrosine phosphorylation of Stat5 protein Source: Ensembl
    15. odontogenesis of dentin-containing tooth Source: MGI
    16. positive regulation of cell differentiation Source: MGI
    17. positive regulation of stress fiber assembly Source: Ensembl
    18. regulation of cell proliferation Source: MGI
    19. regulation of hippo signaling Source: Ensembl
    20. regulation of neural precursor cell proliferation Source: MGI
    21. regulation of protein localization to nucleus Source: MGI
    22. regulation of protein stability Source: MGI
    23. Schwann cell proliferation Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Merlin
    Alternative name(s):
    Moesin-ezrin-radixin-like protein
    Neurofibromin-2
    Schwannomin
    Gene namesi
    Name:Nf2
    Synonyms:Nf-2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97307. Nf2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cytoplasmcytoskeleton By similarity. Nucleus By similarity
    Note: Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with VPRBP 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 By similarity.By similarity

    GO - Cellular componenti

    1. adherens junction Source: MGI
    2. apical part of cell Source: MGI
    3. cleavage furrow Source: MGI
    4. cortical actin cytoskeleton Source: MGI
    5. cytoplasm Source: MGI
    6. cytoskeleton Source: MGI
    7. early endosome Source: Ensembl
    8. extrinsic component of membrane Source: InterPro
    9. filopodium Source: MGI
    10. lamellipodium Source: MGI
    11. nucleolus Source: Ensembl
    12. nucleus Source: MGI
    13. perinuclear region of cytoplasm Source: Ensembl
    14. plasma membrane Source: UniProtKB-SubCell
    15. ruffle Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are born with abnormally small lenses with serious structural defects. Failure of lens vesicle separation and the resulting changes in cell organization causes lenses to herniate, leading to expulsion of lens fiber cells through a perforation in the cornea. Developing lenses show loss of cell apical-basal polarity, failure of the lens vesicle to separate from the surface ectoderm, failure to properly exit the cell cycle during fiber cell differentiation and incomplete terminal differentiation of fiber cells.1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 596596MerlinPRO_0000219413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei518 – 5181Phosphoserine; by PAKBy similarity

    Post-translational modificationi

    Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail.By similarity
    Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP46662.
    PaxDbiP46662.
    PRIDEiP46662.

    PTM databases

    PhosphoSiteiP46662.

    Expressioni

    Gene expression databases

    ArrayExpressiP46662.
    BgeeiP46662.
    CleanExiMM_NF2.
    GenevestigatoriP46662.

    Interactioni

    Subunit structurei

    Interacts with SLC9A3R1, HGS and AGAP2. Interacts with SGSM3. Interacts (via FERM domain) with MPP1 By similarity. Interacts with LAYN and WWC1. Interacts with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201737. 4 interactions.
    IntActiP46662. 5 interactions.
    MINTiMINT-242068.

    Structurei

    Secondary structure

    1
    596
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 277
    Beta strandi32 – 387
    Helixi43 – 5412
    Helixi59 – 613
    Beta strandi62 – 687
    Beta strandi71 – 744
    Beta strandi77 – 804
    Helixi81 – 833
    Beta strandi89 – 10012
    Helixi105 – 1084
    Helixi112 – 12716
    Helixi135 – 15016
    Turni155 – 1573
    Turni160 – 1656
    Helixi171 – 1766
    Helixi181 – 19212
    Helixi193 – 1953
    Helixi200 – 21112
    Turni215 – 2184
    Beta strandi220 – 2267
    Beta strandi231 – 2366
    Beta strandi238 – 2458
    Beta strandi248 – 2514
    Beta strandi253 – 2575
    Helixi258 – 2603
    Beta strandi261 – 2677
    Beta strandi270 – 2778
    Turni278 – 2803
    Beta strandi283 – 2864
    Helixi290 – 30920
    Helixi316 – 33722

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ISNX-ray2.90A18-340[»]
    3WA0X-ray2.31A/B/C/D/E/F19-314[»]
    4P7IX-ray2.60A/B1-313[»]
    ProteinModelPortaliP46662.
    SMRiP46662. Positions 18-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46662.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 311290FERMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi327 – 465139Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG328202.
    GeneTreeiENSGT00650000092953.
    HOGENOMiHOG000007113.
    HOVERGENiHBG002185.
    InParanoidiP46662.
    KOiK16684.
    OMAiITNEMER.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP46662.
    TreeFamiTF313935.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR011174. ERM.
    IPR011259. ERM_C_dom.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR008954. Moesin_tail.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002305. ERM. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P46662-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV    50
    CRTLGLRETW FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF 100
    YPENAEEELV QEITQHLFFL QVKKQILDEK VYCPPEASVL LASYAVQAKY 150
    GDYDPSVHKR GFLAQEELLP KRVINLYQMT PEMWEERITA WYAEHRGRAR 200
    DEAEMEYLKI AQDLEMYGVN YFTIRNKKGT ELLLGVDALG LHIYDPENRL 250
    TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC 300
    IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE 350
    RTRDELERRL LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ 400
    KAAEAEQEMQ RIKATAIRTE EEKRLMEQKV LEAEVLALKM AEESERRAKE 450
    ADQLKQDLQE AREAERRAKQ KLLEIATKPT YPPMNPIPPP LPPDIPSFDI 500
    IADSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN ELKTEIEALK 550
    LKERETALDV LHSESSDRGG PSSKHNTIKK LTLQSAKSRV AFFEEL 596
    Length:596
    Mass (Da):69,776
    Last modified:June 27, 2003 - v2
    Checksum:i8D06F557E3435851
    GO
    Isoform 2 (identifier: P46662-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         581-596: LTLQSAKSRVAFFEEL → PQAQGRRPICI

    Show »
    Length:591
    Mass (Da):69,176
    Checksum:i20B97F99EBF87184
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti475 – 4751I → T in AAA39808. (PubMed:7981675)Curated
    Sequence conflicti554 – 5541R → A in AAA39807. (PubMed:8012352)Curated
    Sequence conflicti554 – 5541R → A in AAA63648. (PubMed:8012352)Curated
    Sequence conflicti570 – 5701G → A in AAA39808. (PubMed:7981675)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei581 – 59616LTLQS…FFEEL → PQAQGRRPICI in isoform 2. 1 PublicationVSP_000493Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74671 mRNA. Translation: CAA52737.1.
    L27105 mRNA. Translation: AAA39807.1.
    L27090 mRNA. Translation: AAA63648.1.
    L28176 mRNA. Translation: AAA39808.1.
    AK045998 mRNA. Translation: BAC32567.1.
    X75759 mRNA. Translation: CAA53386.1.
    CCDSiCCDS24391.1. [P46662-1]
    CCDS56757.1. [P46662-2]
    PIRiI48683.
    I54368.
    I68664.
    RefSeqiNP_001239179.1. NM_001252250.1. [P46662-2]
    NP_001239180.1. NM_001252251.1. [P46662-2]
    NP_001239181.1. NM_001252252.1.
    NP_001239182.1. NM_001252253.1.
    NP_035028.2. NM_010898.4. [P46662-1]
    XP_006514633.1. XM_006514570.1. [P46662-2]
    UniGeneiMm.297109.

    Genome annotation databases

    EnsembliENSMUST00000053079; ENSMUSP00000055033; ENSMUSG00000009073. [P46662-2]
    ENSMUST00000056290; ENSMUSP00000055061; ENSMUSG00000009073. [P46662-2]
    ENSMUST00000109910; ENSMUSP00000105536; ENSMUSG00000009073. [P46662-1]
    GeneIDi18016.
    KEGGimmu:18016.
    UCSCiuc007hvf.2. mouse. [P46662-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74671 mRNA. Translation: CAA52737.1 .
    L27105 mRNA. Translation: AAA39807.1 .
    L27090 mRNA. Translation: AAA63648.1 .
    L28176 mRNA. Translation: AAA39808.1 .
    AK045998 mRNA. Translation: BAC32567.1 .
    X75759 mRNA. Translation: CAA53386.1 .
    CCDSi CCDS24391.1. [P46662-1 ]
    CCDS56757.1. [P46662-2 ]
    PIRi I48683.
    I54368.
    I68664.
    RefSeqi NP_001239179.1. NM_001252250.1. [P46662-2 ]
    NP_001239180.1. NM_001252251.1. [P46662-2 ]
    NP_001239181.1. NM_001252252.1.
    NP_001239182.1. NM_001252253.1.
    NP_035028.2. NM_010898.4. [P46662-1 ]
    XP_006514633.1. XM_006514570.1. [P46662-2 ]
    UniGenei Mm.297109.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ISN X-ray 2.90 A 18-340 [» ]
    3WA0 X-ray 2.31 A/B/C/D/E/F 19-314 [» ]
    4P7I X-ray 2.60 A/B 1-313 [» ]
    ProteinModelPortali P46662.
    SMRi P46662. Positions 18-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201737. 4 interactions.
    IntActi P46662. 5 interactions.
    MINTi MINT-242068.

    PTM databases

    PhosphoSitei P46662.

    Proteomic databases

    MaxQBi P46662.
    PaxDbi P46662.
    PRIDEi P46662.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000053079 ; ENSMUSP00000055033 ; ENSMUSG00000009073 . [P46662-2 ]
    ENSMUST00000056290 ; ENSMUSP00000055061 ; ENSMUSG00000009073 . [P46662-2 ]
    ENSMUST00000109910 ; ENSMUSP00000105536 ; ENSMUSG00000009073 . [P46662-1 ]
    GeneIDi 18016.
    KEGGi mmu:18016.
    UCSCi uc007hvf.2. mouse. [P46662-1 ]

    Organism-specific databases

    CTDi 4771.
    MGIi MGI:97307. Nf2.

    Phylogenomic databases

    eggNOGi NOG328202.
    GeneTreei ENSGT00650000092953.
    HOGENOMi HOG000007113.
    HOVERGENi HBG002185.
    InParanoidi P46662.
    KOi K16684.
    OMAi ITNEMER.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P46662.
    TreeFami TF313935.

    Miscellaneous databases

    ChiTaRSi NF2. mouse.
    EvolutionaryTracei P46662.
    NextBioi 293053.
    PROi P46662.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46662.
    Bgeei P46662.
    CleanExi MM_NF2.
    Genevestigatori P46662.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019750. Band_41_fam.
    IPR011174. ERM.
    IPR011259. ERM_C_dom.
    IPR000798. Ez/rad/moesin_like.
    IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
    IPR019748. FERM_central.
    IPR019747. FERM_CS.
    IPR000299. FERM_domain.
    IPR018979. FERM_N.
    IPR018980. FERM_PH-like_C.
    IPR008954. Moesin_tail.
    IPR011993. PH_like_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00769. ERM. 1 hit.
    PF09380. FERM_C. 1 hit.
    PF00373. FERM_M. 1 hit.
    PF09379. FERM_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002305. ERM. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF48678. SSF48678. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The murine NF2 homologue encodes a highly conserved merlin protein with alternative forms."
      Haase V.H., Trofatter J.A., Maccollin M., Tarttelin E., Gusella J.F., Ramesh V.
      Hum. Mol. Genet. 3:407-411(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Alternative transcripts in the mouse neurofibromatosis type 2 (NF2) gene are conserved and code for schwannomins with distinct C-terminal domains."
      Huynh D.P., Nechiporuk T., Pulst S.M.
      Hum. Mol. Genet. 3:1075-1079(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Brain.
    4. "The mouse neurofibromatosis type 2 gene maps to chromosome 11."
      Claudio J.O., Marineau C., Rouleau G.A.
      Genomics 21:437-439(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 400-596.
      Tissue: Brain.
    5. "Layilin, a cell surface hyaluronan receptor, interacts with merlin and radixin."
      Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T., Hynes R.O.
      Exp. Cell Res. 308:177-187(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LAYN.
    6. "The tumor suppressor merlin is required for cell cycle exit, terminal differentiation, and cell polarity in the developing murine lens."
      Wiley L.A., Dattilo L.K., Kang K.B., Giovannini M., Beebe D.C.
      Invest. Ophthalmol. Vis. Sci. 51:3611-3618(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiMERL_MOUSE
    AccessioniPrimary (citable) accession number: P46662
    Secondary accession number(s): Q8BR03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 27, 2003
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3