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P35240

- MERL_HUMAN

UniProt

P35240 - MERL_HUMAN

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Protein

Merlin

Gene

NF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 - Biological processi

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

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. apical part of cell Source: Ensembl
  3. cleavage furrow Source: Ensembl
  4. cortical actin cytoskeleton Source: Ensembl
  5. cytoplasm Source: HGNC
  6. cytoskeleton Source: ProtInc
  7. early endosome Source: HGNC
  8. extrinsic component of membrane Source: InterPro
  9. filopodium Source: Ensembl
  10. lamellipodium Source: Ensembl
  11. membrane Source: UniProtKB
  12. nucleolus Source: HGNC
  13. nucleus Source: UniProtKB
  14. perinuclear region of cytoplasm Source: HGNC
  15. plasma membrane Source: UniProtKB
  16. ruffle Source: Ensembl
Complete GO annotation...

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 PAK1 Publication

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

BgeeiP35240.
ExpressionAtlasiP35240. baseline and differential.
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. 34 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.
GeneTreeiENSGT00760000119078.
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

        10         20         30         40         50
MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV
60 70 80 90 100
CRTLGLRETW FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF
110 120 130 140 150
YPENAEEELV QEITQHLFFL QVKKQILDEK IYCPPEASVL LASYAVQAKY
160 170 180 190 200
GDYDPSVHKR GFLAQEELLP KRVINLYQMT PEMWEERITA WYAEHRGRAR
210 220 230 240 250
DEAEMEYLKI AQDLEMYGVN YFAIRNKKGT ELLLGVDALG LHIYDPENRL
260 270 280 290 300
TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC
310 320 330 340 350
IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE
360 370 380 390 400
RTRDELERRL LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ
410 420 430 440 450
KAAEAEQEMQ RIKATAIRTE EEKRLMEQKV LEAEVLALKM AEESERRAKE
460 470 480 490 500
ADQLKQDLQE AREAERRAKQ KLLEIATKPT YPPMNPIPAP LPPDIPSFNL
510 520 530 540 550
IGDSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN ELKTEIEALK
560 570 580 590
LKERETALDI LHNENSDRGG SSKHNTIKKL TLQSAKSRVA FFEEL
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. 1 Publication
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. 34 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.
GeneTreei ENSGT00760000119078.
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

Bgeei P35240.
ExpressionAtlasi P35240. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 174 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