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P35240

- MERL_HUMAN

UniProt

P35240 - MERL_HUMAN

Protein

Merlin

Gene

NF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      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.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: HGNC
    2. cell-cell junction organization Source: Ensembl
    3. ectoderm development Source: Ensembl
    4. lens fiber cell differentiation Source: Ensembl
    5. mesoderm formation Source: Ensembl
    6. negative regulation of cell-cell adhesion Source: HGNC
    7. negative regulation of cell-matrix adhesion Source: HGNC
    8. negative regulation of cell migration Source: HGNC
    9. negative regulation of cell proliferation Source: UniProtKB
    10. negative regulation of DNA replication Source: HGNC
    11. negative regulation of JAK-STAT cascade Source: HGNC
    12. negative regulation of MAPK cascade Source: Ensembl
    13. negative regulation of protein kinase activity Source: Ensembl
    14. negative regulation of tyrosine phosphorylation of Stat3 protein Source: HGNC
    15. negative regulation of tyrosine phosphorylation of Stat5 protein Source: HGNC
    16. odontogenesis of dentin-containing tooth Source: Ensembl
    17. positive regulation of stress fiber assembly Source: HGNC
    18. regulation of hippo signaling Source: UniProtKB
    19. Schwann cell proliferation Source: HGNC

    Enzyme and pathway databases

    SignaLinkiP35240.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Merlin
    Alternative name(s):
    Moesin-ezrin-radixin-like protein
    Neurofibromin-2
    Schwannomerlin
    Schwannomin
    Gene namesi
    Name:NF2
    Synonyms:SCH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7773. NF2.

    Subcellular locationi

    Isoform 1 : Cell projectionfilopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle 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 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.
    Isoform 7 : Cytoplasmperinuclear region. Cytoplasmic granule
    Note: Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 7 is absent from ruffling membranes and filopodia.
    Isoform 9 : Cytoplasmperinuclear region. Cytoplasmic granule
    Note: Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 9 is absent from ruffling membranes and filopodia.
    Isoform 10 : Nucleus. Cell projectionfilopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Cytoplasmic granule. Cytoplasmcytoskeleton
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    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.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621F → S in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 3 Publications
    VAR_000810
    Natural varianti77 – 771M → V in NF2. 1 Publication
    VAR_043011
    Natural varianti96 – 961Missing in NF2 and in sporadic meningioma. 2 Publications
    VAR_000812
    Natural varianti106 – 1061E → G in NF2. 2 Publications
    VAR_000813
    Natural varianti133 – 1331C → R in NF2. 1 Publication
    VAR_065227
    Natural varianti141 – 1411L → P in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 1 Publication
    VAR_043012
    Natural varianti197 – 1971G → C in NF2. 1 Publication
    VAR_043013
    Natural varianti220 – 2201N → Y in NF2. 1 Publication
    VAR_000818
    Natural varianti234 – 2341L → R in NF2 and in retinal hamartoma; severe. 1 Publication
    VAR_009123
    Natural varianti352 – 3521T → M in NF2. 2 Publications
    VAR_000821
    Natural varianti360 – 3601L → P in NF2.
    VAR_000822
    Natural varianti413 – 4131K → E in NF2. 2 Publications
    VAR_043014
    Natural varianti533 – 5331K → T in NF2. 1 Publication
    VAR_043015
    Natural varianti535 – 5351L → P in NF2; late onset. 3 Publications
    VAR_000825
    Natural varianti538 – 5381Q → P in NF2; mild. 1 Publication
    VAR_000826
    Natural varianti539 – 5391L → H in NF2. 1 Publication
    VAR_043016
    Natural varianti579 – 5791K → M in NF2. 1 Publication
    VAR_043017
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641L → P: Abolishes binding to AGAP2 and interaction with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 2 Publications
    Mutagenesisi518 – 5181S → A: Loss of phosphorylation. Significant accumulation in the nucleus and no effect on binding to VPRBP. 1 Publication
    Mutagenesisi518 – 5181S → D: No effect on phosphorylation. Defective nuclear accumulation. Significant decrease in binding to VPRBP and in ability to inhibit cell proliferation. 1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi101000. phenotype.
    156240. phenotype.
    162091. phenotype.
    Orphaneti637. Neurofibromatosis type 2.
    93921. Neurofibromatosis type 3.
    PharmGKBiPA31580.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 595595MerlinPRO_0000219412Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei518 – 5181Phosphoserine; by PAK2 Publications

    Post-translational modificationi

    Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail.2 Publications
    Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP35240.
    PaxDbiP35240.
    PRIDEiP35240.

    PTM databases

    PhosphoSiteiP35240.

    Miscellaneous databases

    PMAP-CutDBP35240.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP35240.
    BgeeiP35240.
    GenevestigatoriP35240.

    Organism-specific databases

    HPAiCAB005385.
    HPA003097.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMOTQ4VCS58EBI-1014472,EBI-2511319
    AMOTQ4VCS5-12EBI-1014472,EBI-3903812
    AMOTQ4VCS5-26EBI-1014472,EBI-3891843
    GTPBP4Q9BZE49EBI-1014472,EBI-1056249
    INADLQ8NI352EBI-1014472,EBI-724390
    LATS1O958354EBI-1014472,EBI-444209
    MAP3K11Q165844EBI-1014472,EBI-49961
    MED28Q9H2044EBI-1014472,EBI-514199
    Ppp1r12aQ107282EBI-1014472,EBI-918263From a different organism.
    Schip1Q3TI532EBI-1014472,EBI-1397475From a different organism.
    SLC9A3R1O147454EBI-1014500,EBI-349787

    Protein-protein interaction databases

    BioGridi110844. 32 interactions.
    IntActiP35240. 25 interactions.

    Structurei

    Secondary structure

    1
    595
    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 – 1744
    Helixi181 – 19313
    Turni194 – 1974
    Helixi200 – 21112
    Turni215 – 2184
    Beta strandi220 – 2267
    Beta strandi231 – 2366
    Beta strandi238 – 2447
    Beta strandi249 – 2513
    Beta strandi253 – 2575
    Helixi258 – 2603
    Beta strandi261 – 2677
    Beta strandi270 – 2778
    Beta strandi283 – 2864
    Helixi290 – 31021

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H4RX-ray1.80A/B1-313[»]
    3U8ZX-ray2.64A/B/C/D18-312[»]
    ProteinModelPortaliP35240.
    SMRiP35240. Positions 18-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35240.

    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.
    HOVERGENiHBG002185.
    InParanoidiP35240.
    KOiK16684.
    OMAiITNEMER.
    OrthoDBiEOG7BGHK6.
    PhylomeDBiP35240.
    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 (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35240-1) [UniParc]FASTAAdd to Basket

    Also known as: I

    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 IYCPPEASVL LASYAVQAKY 150
    GDYDPSVHKR GFLAQEELLP KRVINLYQMT PEMWEERITA WYAEHRGRAR 200
    DEAEMEYLKI AQDLEMYGVN YFAIRNKKGT 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 YPPMNPIPAP LPPDIPSFNL 500
    IGDSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN ELKTEIEALK 550
    LKERETALDI LHNENSDRGG SSKHNTIKKL TLQSAKSRVA FFEEL 595
    Length:595
    Mass (Da):69,690
    Last modified:February 1, 1994 - v1
    Checksum:iB1A1BF2BD5DA561C
    GO
    Isoform 2 (identifier: P35240-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-595: LTLQSAKSRVAFFEEL → SSPRQKTYLHLSPQSRLFPGTLYVVMLYVVMVLPSVILTRA

    Show »
    Length:620
    Mass (Da):72,514
    Checksum:i6A462A3A113A6C28
    GO
    Isoform 3 (identifier: P35240-3) [UniParc]FASTAAdd to Basket

    Also known as: II

    The sequence of this isoform differs from the canonical sequence as follows:
         580-590: LTLQSAKSRVA → PQAQGRRPICI
         591-595: Missing.

    Show »
    Length:590
    Mass (Da):69,090
    Checksum:i99B732B48367D22A
    GO
    Isoform 4 (identifier: P35240-4) [UniParc]FASTAAdd to Basket

    Also known as: delE2/3

    The sequence of this isoform differs from the canonical sequence as follows:
         39-121: Missing.
         580-590: LTLQSAKSRVA → PQAQGRRPICI
         591-595: Missing.

    Show »
    Length:507
    Mass (Da):59,096
    Checksum:iDD8162ABBC9EA4CA
    GO
    Isoform 5 (identifier: P35240-5) [UniParc]FASTAAdd to Basket

    Also known as: delE3

    The sequence of this isoform differs from the canonical sequence as follows:
         81-121: Missing.
         580-590: LTLQSAKSRVA → PQAQGRRPICI
         591-595: Missing.

    Show »
    Length:549
    Mass (Da):64,189
    Checksum:i905559E6F72D3F4C
    GO
    Isoform 6 (identifier: P35240-6) [UniParc]FASTAAdd to Basket

    Also known as: delE2

    The sequence of this isoform differs from the canonical sequence as follows:
         39-80: Missing.
         580-590: LTLQSAKSRVA → PQAQGRRPICI
         591-595: Missing.

    Show »
    Length:548
    Mass (Da):63,996
    Checksum:i58E15B35515C10EE
    GO
    Isoform 7 (identifier: P35240-7) [UniParc]FASTAAdd to Basket

    Also known as: MER150

    The sequence of this isoform differs from the canonical sequence as follows:
         259-259: N → R
         260-595: Missing.

    Show »
    Length:259
    Mass (Da):30,454
    Checksum:i3C7B9CDBC884CDF6
    GO
    Isoform 8 (identifier: P35240-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         335-363: Missing.
         580-590: LTLQSAKSRVA → PQAQGRRPICI
         591-595: Missing.

    Show »
    Length:561
    Mass (Da):65,350
    Checksum:i371C417ABDB68D02
    GO
    Isoform 9 (identifier: P35240-9) [UniParc]FASTAAdd to Basket

    Also known as: MER162

    The sequence of this isoform differs from the canonical sequence as follows:
         150-579: Missing.

    Show »
    Length:165
    Mass (Da):19,215
    Checksum:i01B92CD1AFEEB202
    GO
    Isoform 10 (identifier: P35240-10) [UniParc]FASTAAdd to Basket

    Also known as: MER151

    The sequence of this isoform differs from the canonical sequence as follows:
         39-121: Missing.
         150-225: Missing.
         334-379: MERQRLAREK...ANEALMRSEE → GQRGRSAEAG...HEPNSSTVAS
         380-595: Missing.

    Show »
    Length:220
    Mass (Da):24,515
    Checksum:i05961D105F94276E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771M → I in AAH20257. (PubMed:15489334)Curated
    Sequence conflicti581 – 5811T → P in AAK54160. (PubMed:11827459)Curated
    Sequence conflicti581 – 5811T → P in AAK54162. (PubMed:11827459)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461L → R in vestibular schwannoma; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 1 Publication
    VAR_000809
    Natural varianti62 – 621F → S in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 3 Publications
    VAR_000810
    Natural varianti77 – 771M → V in NF2. 1 Publication
    VAR_043011
    Natural varianti79 – 791K → E in vestibular schwannoma. 1 Publication
    VAR_000811
    Natural varianti96 – 961Missing in NF2 and in sporadic meningioma. 2 Publications
    VAR_000812
    Natural varianti106 – 1061E → G in NF2. 2 Publications
    VAR_000813
    Natural varianti117 – 1171L → I in sporadic meningioma. 1 Publication
    VAR_000814
    Natural varianti119 – 1191Missing in sporadic meningioma. 2 Publications
    VAR_000815
    Natural varianti122 – 1298Missing in sporadic meningioma.
    VAR_000816
    Natural varianti133 – 1331C → R in NF2. 1 Publication
    VAR_065227
    Natural varianti141 – 1411L → P in NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. 1 Publication
    VAR_043012
    Natural varianti197 – 1971G → C in NF2. 1 Publication
    VAR_043013
    Natural varianti219 – 2191V → M in vestibular schwannoma. 1 Publication
    VAR_000817
    Natural varianti220 – 2201N → Y in NF2. 1 Publication
    VAR_000818
    Natural varianti234 – 2341L → R in NF2 and in retinal hamartoma; severe. 1 Publication
    VAR_009123
    Natural varianti273 – 2731I → F in breast ductal carcinoma. 1 Publication
    VAR_000819
    Natural varianti339 – 3391L → F in sporadic meningioma. 1 Publication
    VAR_000820
    Natural varianti344 – 3441Q → H.
    Corresponds to variant rs2229064 [ dbSNP | Ensembl ].
    VAR_048358
    Natural varianti351 – 3511R → H.1 Publication
    VAR_029041
    Natural varianti352 – 3521T → M in NF2. 2 Publications
    VAR_000821
    Natural varianti360 – 3601L → P in NF2.
    VAR_000822
    Natural varianti364 – 3641K → I in melanoma. 1 Publication
    VAR_000823
    Natural varianti413 – 4131K → E in NF2. 2 Publications
    VAR_043014
    Natural varianti418 – 4181R → C in vestibular schwannoma. 1 Publication
    VAR_000824
    Natural varianti463 – 4631E → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035848
    Natural varianti533 – 5331K → T in NF2. 1 Publication
    VAR_043015
    Natural varianti535 – 5351L → P in NF2; late onset. 3 Publications
    VAR_000825
    Natural varianti538 – 5381Q → P in NF2; mild. 1 Publication
    VAR_000826
    Natural varianti539 – 5391L → H in NF2. 1 Publication
    VAR_043016
    Natural varianti579 – 5791K → M in NF2. 1 Publication
    VAR_043017

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 12183Missing in isoform 4 and isoform 10. 3 PublicationsVSP_007041Add
    BLAST
    Alternative sequencei39 – 8042Missing in isoform 6. 1 PublicationVSP_007040Add
    BLAST
    Alternative sequencei81 – 12141Missing in isoform 5. 1 PublicationVSP_007042Add
    BLAST
    Alternative sequencei150 – 579430Missing in isoform 9. 1 PublicationVSP_007044Add
    BLAST
    Alternative sequencei150 – 22576Missing in isoform 10. 1 PublicationVSP_007043Add
    BLAST
    Alternative sequencei259 – 2591N → R in isoform 7. 1 PublicationVSP_007045
    Alternative sequencei260 – 595336Missing in isoform 7. 1 PublicationVSP_007046Add
    BLAST
    Alternative sequencei334 – 37946MERQR…MRSEE → GQRGRSAEAGPAGSTRGGAK SQAEAPGDCHQAHVPAHEPN SSTVAS in isoform 10. 1 PublicationVSP_007047Add
    BLAST
    Alternative sequencei335 – 36329Missing in isoform 8. 1 PublicationVSP_007048Add
    BLAST
    Alternative sequencei380 – 595216Missing in isoform 10. 1 PublicationVSP_007049Add
    BLAST
    Alternative sequencei580 – 59516LTLQS…FFEEL → SSPRQKTYLHLSPQSRLFPG TLYVVMLYVVMVLPSVILTR A in isoform 2. CuratedVSP_000492Add
    BLAST
    Alternative sequencei580 – 59011LTLQSAKSRVA → PQAQGRRPICI in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8. 2 PublicationsVSP_007050Add
    BLAST
    Alternative sequencei591 – 5955Missing in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8. 2 PublicationsVSP_007051

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11353 mRNA. Translation: AAA36212.1.
    X72655
    , X72656, X72657, X72658, X72659, X72660, X72661, X72662, X72663, X72664, X72665, X72666, X72667, X72668, X72669, X72670 Genomic DNA. Translation: CAA51220.1.
    Z22664 mRNA. Translation: CAA80377.1.
    Y18000 Genomic DNA. Translation: CAA76992.1.
    Y18000 Genomic DNA. Translation: CAA76993.1.
    AF122827 mRNA. Translation: AAD48752.1.
    AF122828 mRNA. Translation: AAD48753.1.
    AF123570 mRNA. Translation: AAD48754.1.
    AF369657 mRNA. Translation: AAK54160.1.
    AF369658 mRNA. Translation: AAK54161.1.
    AF369661 mRNA. Translation: AAK54162.1.
    AF369662 mRNA. Translation: AAK54163.1.
    AF369663 mRNA. Translation: AAK54164.1.
    AF369664 mRNA. Translation: AAK54165.1.
    AF369665 mRNA. Translation: AAK54166.1.
    AF369700 mRNA. Translation: AAK54195.1.
    AF369701 mRNA. Translation: AAK54196.1.
    CR456530 mRNA. Translation: CAG30416.1.
    BC003112 mRNA. Translation: AAH03112.2.
    BC020257 mRNA. Translation: AAH20257.1.
    CCDSiCCDS13861.1. [P35240-1]
    CCDS13862.1. [P35240-3]
    CCDS13863.1. [P35240-6]
    CCDS13864.1. [P35240-5]
    CCDS13865.1. [P35240-4]
    CCDS54516.1. [P35240-9]
    PIRiS33809.
    RefSeqiNP_000259.1. NM_000268.3. [P35240-1]
    NP_057502.2. NM_016418.5. [P35240-3]
    NP_861546.1. NM_181825.2. [P35240-3]
    NP_861966.1. NM_181828.2. [P35240-6]
    NP_861967.1. NM_181829.2. [P35240-5]
    NP_861968.1. NM_181830.2. [P35240-4]
    NP_861969.1. NM_181831.2. [P35240-4]
    NP_861970.1. NM_181832.2. [P35240-3]
    NP_861971.1. NM_181833.2. [P35240-9]
    UniGeneiHs.187898.

    Genome annotation databases

    EnsembliENST00000334961; ENSP00000335652; ENSG00000186575. [P35240-4]
    ENST00000338641; ENSP00000344666; ENSG00000186575. [P35240-1]
    ENST00000353887; ENSP00000340626; ENSG00000186575. [P35240-4]
    ENST00000361166; ENSP00000354529; ENSG00000186575. [P35240-3]
    ENST00000361452; ENSP00000354897; ENSG00000186575. [P35240-5]
    ENST00000361676; ENSP00000355183; ENSG00000186575. [P35240-6]
    ENST00000397789; ENSP00000380891; ENSG00000186575. [P35240-3]
    ENST00000403435; ENSP00000384029; ENSG00000186575. [P35240-8]
    ENST00000403999; ENSP00000384797; ENSG00000186575. [P35240-3]
    ENST00000413209; ENSP00000409921; ENSG00000186575. [P35240-9]
    ENST00000432151; ENSP00000395885; ENSG00000186575. [P35240-10]
    GeneIDi4771.
    KEGGihsa:4771.
    UCSCiuc003afy.4. human. [P35240-3]
    uc003afz.4. human. [P35240-4]
    uc003aga.4. human. [P35240-6]
    uc003age.4. human. [P35240-1]
    uc003agh.4. human. [P35240-5]
    uc003agj.4. human. [P35240-9]

    Polymorphism databases

    DMDMi462594.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11353 mRNA. Translation: AAA36212.1 .
    X72655
    , X72656 , X72657 , X72658 , X72659 , X72660 , X72661 , X72662 , X72663 , X72664 , X72665 , X72666 , X72667 , X72668 , X72669 , X72670 Genomic DNA. Translation: CAA51220.1 .
    Z22664 mRNA. Translation: CAA80377.1 .
    Y18000 Genomic DNA. Translation: CAA76992.1 .
    Y18000 Genomic DNA. Translation: CAA76993.1 .
    AF122827 mRNA. Translation: AAD48752.1 .
    AF122828 mRNA. Translation: AAD48753.1 .
    AF123570 mRNA. Translation: AAD48754.1 .
    AF369657 mRNA. Translation: AAK54160.1 .
    AF369658 mRNA. Translation: AAK54161.1 .
    AF369661 mRNA. Translation: AAK54162.1 .
    AF369662 mRNA. Translation: AAK54163.1 .
    AF369663 mRNA. Translation: AAK54164.1 .
    AF369664 mRNA. Translation: AAK54165.1 .
    AF369665 mRNA. Translation: AAK54166.1 .
    AF369700 mRNA. Translation: AAK54195.1 .
    AF369701 mRNA. Translation: AAK54196.1 .
    CR456530 mRNA. Translation: CAG30416.1 .
    BC003112 mRNA. Translation: AAH03112.2 .
    BC020257 mRNA. Translation: AAH20257.1 .
    CCDSi CCDS13861.1. [P35240-1 ]
    CCDS13862.1. [P35240-3 ]
    CCDS13863.1. [P35240-6 ]
    CCDS13864.1. [P35240-5 ]
    CCDS13865.1. [P35240-4 ]
    CCDS54516.1. [P35240-9 ]
    PIRi S33809.
    RefSeqi NP_000259.1. NM_000268.3. [P35240-1 ]
    NP_057502.2. NM_016418.5. [P35240-3 ]
    NP_861546.1. NM_181825.2. [P35240-3 ]
    NP_861966.1. NM_181828.2. [P35240-6 ]
    NP_861967.1. NM_181829.2. [P35240-5 ]
    NP_861968.1. NM_181830.2. [P35240-4 ]
    NP_861969.1. NM_181831.2. [P35240-4 ]
    NP_861970.1. NM_181832.2. [P35240-3 ]
    NP_861971.1. NM_181833.2. [P35240-9 ]
    UniGenei Hs.187898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H4R X-ray 1.80 A/B 1-313 [» ]
    3U8Z X-ray 2.64 A/B/C/D 18-312 [» ]
    ProteinModelPortali P35240.
    SMRi P35240. Positions 18-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110844. 32 interactions.
    IntActi P35240. 25 interactions.

    PTM databases

    PhosphoSitei P35240.

    Polymorphism databases

    DMDMi 462594.

    Proteomic databases

    MaxQBi P35240.
    PaxDbi P35240.
    PRIDEi P35240.

    Protocols and materials databases

    DNASUi 4771.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334961 ; ENSP00000335652 ; ENSG00000186575 . [P35240-4 ]
    ENST00000338641 ; ENSP00000344666 ; ENSG00000186575 . [P35240-1 ]
    ENST00000353887 ; ENSP00000340626 ; ENSG00000186575 . [P35240-4 ]
    ENST00000361166 ; ENSP00000354529 ; ENSG00000186575 . [P35240-3 ]
    ENST00000361452 ; ENSP00000354897 ; ENSG00000186575 . [P35240-5 ]
    ENST00000361676 ; ENSP00000355183 ; ENSG00000186575 . [P35240-6 ]
    ENST00000397789 ; ENSP00000380891 ; ENSG00000186575 . [P35240-3 ]
    ENST00000403435 ; ENSP00000384029 ; ENSG00000186575 . [P35240-8 ]
    ENST00000403999 ; ENSP00000384797 ; ENSG00000186575 . [P35240-3 ]
    ENST00000413209 ; ENSP00000409921 ; ENSG00000186575 . [P35240-9 ]
    ENST00000432151 ; ENSP00000395885 ; ENSG00000186575 . [P35240-10 ]
    GeneIDi 4771.
    KEGGi hsa:4771.
    UCSCi uc003afy.4. human. [P35240-3 ]
    uc003afz.4. human. [P35240-4 ]
    uc003aga.4. human. [P35240-6 ]
    uc003age.4. human. [P35240-1 ]
    uc003agh.4. human. [P35240-5 ]
    uc003agj.4. human. [P35240-9 ]

    Organism-specific databases

    CTDi 4771.
    GeneCardsi GC22P029999.
    GeneReviewsi NF2.
    HGNCi HGNC:7773. NF2.
    HPAi CAB005385.
    HPA003097.
    MIMi 101000. phenotype.
    156240. phenotype.
    162091. phenotype.
    607379. gene.
    neXtProti NX_P35240.
    Orphaneti 637. Neurofibromatosis type 2.
    93921. Neurofibromatosis type 3.
    PharmGKBi PA31580.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG328202.
    HOVERGENi HBG002185.
    InParanoidi P35240.
    KOi K16684.
    OMAi ITNEMER.
    OrthoDBi EOG7BGHK6.
    PhylomeDBi P35240.
    TreeFami TF313935.

    Enzyme and pathway databases

    SignaLinki P35240.

    Miscellaneous databases

    EvolutionaryTracei P35240.
    GeneWikii Merlin_(protein).
    GenomeRNAii 4771.
    NextBioi 18368.
    PMAP-CutDB P35240.
    PROi P35240.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35240.
    Bgeei P35240.
    Genevestigatori P35240.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
    4. "Novel alternatively spliced isoforms of the neurofibromatosis type 2 tumor suppressor are targeted to the nucleus and cytoplasmic granules."
      Schmucker B., Tang Y., Kressel M.
      Hum. Mol. Genet. 8:1561-1570(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9 AND 10), SUBCELLULAR LOCATION.
    5. "Multiple transcription initiation sites, alternative splicing, and differential polyadenylation contribute to the complexity of human neurofibromatosis 2 transcripts."
      Chang L.-S., Akhmametyeva E.M., Wu Y., Zhu L., Welling D.B.
      Genomics 79:63-76(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6 AND 8).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Lung and Skin.
    8. "The gene of neurofibromatosis type 2."
      Marineau C., Merel P., Rouleau G.A., Thomas G.
      Medecine/Sciences 11:35-42(1995)
      Cited for: REVIEW.
    9. "NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins."
      Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C., Solomon F., Gusella J., Ramesh V.
      J. Biol. Chem. 273:1273-1276(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    10. "The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate."
      Scoles D.R., Huynh D.P., Chen M.S., Burke S.P., Gutmann D.H., Pulst S.-M.
      Hum. Mol. Genet. 9:1567-1574(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HGS.
    11. Cited for: INVOLVEMENT IN MESOM.
    12. Cited for: INTERACTION WITH SGSM3.
    13. "Neurofibromatosis 2 (NF2) tumor suppressor merlin inhibits phosphatidylinositol 3-kinase through binding to PIKE-L."
      Rong R., Tang X., Gutmann D.H., Ye K.
      Proc. Natl. Acad. Sci. U.S.A. 101:18200-18205(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGAP2, MUTAGENESIS OF LEU-64.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation."
      Huang J., Chen J.
      Oncogene 27:4056-4064(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCAF1, UBIQUITINATION.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Identification of erythrocyte p55/MPP1 as a binding partner of NF2 tumor suppressor protein/Merlin."
      Seo P.-S., Quinn B.J., Khan A.A., Zeng L., Takoudis C.G., Hanada T., Bolis A., Bolino A., Chishti A.H.
      Exp. Biol. Med. 234:255-262(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPP1, SUBCELLULAR LOCATION.
    18. "Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin ligase CRL4(DCAF1) in the nucleus."
      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.
      Cell 140:477-490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPRBP 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, CHARACTERIZATION OF VARIANTS NF2 SER-62 AND PRO-141.
    19. "Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded."
      Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.
      Dev. Cell 18:288-299(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Kibra Is a regulator of the Salvador/Warts/Hippo signaling network."
      Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N.
      Dev. Cell 18:300-308(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWC1.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "The structure of the FERM domain of merlin, the neurofibromatosis type 2 gene product."
      Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.
      Acta Crystallogr. D 58:381-391(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-313.
    23. "DNA diagnosis of neurofibromatosis 2. Altered coding sequence of the merlin tumor suppressor in an extended pedigree."
      Maccollin M.M., Mohney T., Trofatter J.A., Wertelecki W., Ramesh V., Gusella J.F.
      JAMA 270:2316-2320(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 TYR-220.
    24. "Mutational analysis of patients with neurofibromatosis 2."
      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.
      Am. J. Hum. Genet. 55:314-320(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 PHE-96 DEL.
    25. "Somatic NF2 gene mutations in familial and non-familial vestibular schwannoma."
      Irving R.M., Moffat D.A., Hardy D.G., Barton D.E., Xuereb J.H., Maher E.R.
      Hum. Mol. Genet. 3:347-350(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-46.
    26. Cited for: VARIANTS MET-219 AND CYS-418.
    27. "Germline mutations in the neurofibromatosis type 2 tumour suppressor gene."
      Bourn D., Carter S.A., Mason S., Gareth D., Evans R., Strachan T.
      Hum. Mol. Genet. 3:813-816(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NF2 SER-62; GLY-106 AND MET-352.
    28. "Mutations of the neurofibromatosis type 2 gene and lack of the gene product in vestibular schwannomas."
      Sainz J., Huynh D.P., Figueroa K., Ragge N.K., Baser M.E., Pulst S.M.
      Hum. Mol. Genet. 3:885-891(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLU-79 AND HIS-351.
    29. "Mutations in transcript isoforms of the neurofibromatosis 2 gene in multiple human tumour types."
      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.
      Nat. Genet. 6:185-192(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PHE-273 AND ILE-364.
    30. "Eleven novel mutations in the NF2 tumour suppressor gene."
      Bourn D., Evans G., Mason S., Tekes S., Trueman L., Strachan T.
      Hum. Genet. 95:572-574(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NF2 PHE-119 DEL; GLU-413 AND PRO-535.
    31. "Diagnostic issues in a family with late onset type 2 neurofibromatosis."
      Evans D.G.R., Bourn D., Wallace A., Ramsden R.T., Mitchell J.D., Strachan T.
      J. Med. Genet. 32:470-474(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 PRO-535.
    32. "A missense mutation in the NF2 gene results in moderate and mild clinical phenotypes of neurofibromatosis type 2."
      Kluwe L., Mautner V.-F.
      Hum. Genet. 97:224-227(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 PRO-538.
    33. "Screening for mutations in the neurofibromatosis type 2 (NF2) gene in sporadic meningiomas."
      de Vitis L.R., Tedde A., Vitelli F., Ammannati F., Mennonna P., Bigozzi U., Montali E., Papi L.
      Hum. Genet. 97:632-637(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PHE-96 DEL; ILE-117; PHE-119 DEL; 122-VAL--GLU-129 DEL AND PHE-339.
    34. "Mutational spectrum in the neurofibromatosis type 2 gene in sporadic and familial schwannomas."
      Welling D.B., Guida M., Goll F., Pearl D.K., Glasscock M.E., Pappas D.G., Linthicum F.H., Rogers D., Prior T.W.
      Hum. Genet. 98:189-193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NF2 CYS-197 AND HIS-539.
    35. "Genotype/phenotype correlations in type 2 neurofibromatosis (NF2): evidence for more severe disease associated with truncating mutations."
      Evans D.G.R., Trueman L., Wallace A., Collins S., Strachan T.
      J. Med. Genet. 35:450-455(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NF2 SER-62; VAL-77; GLY-106; MET-352; GLU-413 AND PRO-535.
    36. Erratum
      Evans D.G., Trueman L., Wallace A., Collins S., Strachan T.
      J. Med. Genet. 36:87-87(1999)
    37. "Germ-line NF2 mutations and disease severity in neurofibromatosis type 2 patients with retinal abnormalities."
      Baser M.E., Kluwe L., Mautner V.-F.
      Am. J. Hum. Genet. 64:1230-1233(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 ARG-234.
    38. "Detection of novel NF2 mutations by an RNA mismatch cleavage method."
      Faudoa R., Xue Z., Lee F., Baser M.E., Hung G.
      Hum. Mutat. 15:474-478(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS NF2 SER-62; THR-533 AND MET-579.
    39. Cited for: VARIANT NF2 PRO-141.
    40. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-463.
    41. "Evidence of a four-hit mechanism involving SMARCB1 and NF2 in schwannomatosis-associated schwannomas."
      Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L.
      Hum. Mutat. 29:227-231(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SWNTS1.
    42. "Molecular characterization of the NF2 gene in Korean patients with neurofibromatosis type 2: a report of four novel mutations."
      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.
      Korean J. Lab. Med. 30:190-194(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NF2 ARG-133.

    Entry informationi

    Entry nameiMERL_HUMAN
    AccessioniPrimary (citable) accession number: P35240
    Secondary accession number(s): O95683
    , Q8WUJ2, Q969N0, Q969Q3, Q96T30, Q96T31, Q96T32, Q96T33, Q9BTW3, Q9UNG9, Q9UNH3, Q9UNH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 173 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3