NF2
entrez
4771
canonical
uniprot
P35240
canonical
ensembl
ENSG00000186575
resolver
ensp
ENSP00000335652
resolver
ensp
ENSP00000340626
resolver
ensp
ENSP00000344666
resolver
ensp
ENSP00000354529
resolver
ensp
ENSP00000354897
resolver
ensp
ENSP00000355183
resolver
ensp
ENSP00000380891
resolver
ensp
ENSP00000384797
resolver
ensp
ENSP00000409921
resolver
ensp
ENSP00000500117
resolver
ensp
ENSP00000576759
resolver
ensp
ENSP00000576761
resolver
ensp
ENSP00000650259
resolver
ensp
ENSP00000650261
resolver
ensp
ENSP00000722407
resolver
ensp
ENSP00000753185
resolver
enst
ENST00000361166
resolver
genesymbol
NF2
resolver
genesymbol_syn
SCH
resolver
hgnc
HGNC:7773
resolver
uniprot
A0A5K1VW66
resolver
uniprot
O95683
resolver
uniprot
Q8WUJ2
resolver
uniprot
Q969N0
resolver
uniprot
Q969Q3
resolver
uniprot
Q96T30
resolver
uniprot
Q96T31
resolver
uniprot
Q96T32
resolver
uniprot
Q96T33
resolver
uniprot
Q9BTW3
resolver
uniprot
Q9UNG9
resolver
uniprot
Q9UNH3
resolver
uniprot
Q9UNH4
resolver
uniprot_entry
A0A5K1VW66_HUMAN
resolver
uniprot_entry
MERL_HUMAN
resolver
uniprot_sec
O95683
resolver
uniprot_sec
Q8WUJ2
resolver
uniprot_sec
Q969N0
resolver
uniprot_sec
Q969Q3
resolver
uniprot_sec
Q96T30
resolver
uniprot_sec
Q96T31
resolver
uniprot_sec
Q96T32
resolver
uniprot_sec
Q96T33
resolver
uniprot_sec
Q9BTW3
resolver
uniprot_sec
Q9UNG9
resolver
uniprot_sec
Q9UNH3
resolver
uniprot_sec
Q9UNH4
resolver
amino_acid_sequence
MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL
uniprot
proteins
disease_involvement
DISEASE: Schwannomatosis, vestibular (SWNV) [MIM:101000]: An autosomal dominant neoplasia syndrome characterized by the development of multiple benign nerve sheath tumors called schwannomas, particularly affecting the vestibular nerve. Affected individuals usually present with bilateral vestibular schwannomas but can have schwannomas on other cranial, spinal, and peripheral/cutaneous nerves. Meningiomas are common, whereas 20 to 35% of affected individuals develop intramedullary spinal cord tumors called ependymomas. The condition is also characterized by several ophthalmic features such as lenticular opacities, retinal hamartoma, epiretinal membranes. {ECO:0000269|PubMed:10090912, ECO:0000269|PubMed:10669747, ECO:0000269|PubMed:10790209, ECO:0000269|PubMed:12709270, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:20445339, ECO:0000269|PubMed:7666400, ECO:0000269|PubMed:7759081, ECO:0000269|PubMed:7913580, ECO:0000269|PubMed:8081368, ECO:0000269|PubMed:8230593, ECO:0000269|PubMed:8379998, ECO:0000269|PubMed:8566958, ECO:0000269|PubMed:8698340, ECO:0000269|PubMed:9643284}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive neoplasm of the serosal lining of the chest. It appears as broad sheets of cells, with some regions containing spindle-shaped, sarcoma-like cells and other regions showing adenomatous patterns. Pleural mesotheliomas have been linked to exposure to asbestos. {ECO:0000269|PubMed:12136076}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. {ECO:0000269|PubMed:20159598, ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}.
uniprot
proteins
mass_dalton
69690
uniprot
proteins
mutagenesis
MUTAGEN 64; /note="L->P: Abolishes binding to AGAP2 and interaction with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex."; /evidence="ECO:0000269|PubMed:15598747, ECO:0000269|PubMed:20178741"; MUTAGEN 518; /note="S->A: Loss of phosphorylation. Significant accumulation in the nucleus and no effect on binding to DCAF1."; /evidence="ECO:0000269|PubMed:20178741"; MUTAGEN 518; /note="S->D: No effect on phosphorylation. Defective nuclear accumulation. Significant decrease in binding to DCAF1 and in ability to inhibit cell proliferation."; /evidence="ECO:0000269|PubMed:20178741
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail (PubMed:20178741). The dephosphorylation of Ser-518 favors the interaction with NOP53 (PubMed:21167305). {ECO:0000269|PubMed:20178741, ECO:0000269|PubMed:21167305}.; PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation. {ECO:0000269|PubMed:18332868}.
uniprot
proteins
pubmed
10090912
uniprot
proteins
pubmed
10401006
uniprot
proteins
pubmed
10669747
uniprot
proteins
pubmed
10790209
uniprot
proteins
pubmed
10861283
uniprot
proteins
pubmed
11827459
uniprot
proteins
pubmed
11856822
uniprot
proteins
pubmed
12136076
uniprot
proteins
pubmed
12709270
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15541357
uniprot
proteins
pubmed
15598747
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18332868
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19144871
uniprot
proteins
pubmed
20159598
uniprot
proteins
pubmed
20159599
uniprot
proteins
pubmed
20178741
uniprot
proteins
pubmed
20445339
uniprot
proteins
pubmed
21167305
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7666400
uniprot
proteins
pubmed
7759081
uniprot
proteins
pubmed
7913580
uniprot
proteins
pubmed
7951231
uniprot
proteins
pubmed
8004107
uniprot
proteins
pubmed
8012353
uniprot
proteins
pubmed
8081368
uniprot
proteins
pubmed
8162073
uniprot
proteins
pubmed
8230593
uniprot
proteins
pubmed
8379998
uniprot
proteins
pubmed
8453669
uniprot
proteins
pubmed
8566958
uniprot
proteins
pubmed
8655144
uniprot
proteins
pubmed
8698340
uniprot
proteins
pubmed
9430655
uniprot
proteins
pubmed
9643284
uniprot
proteins
pubmed
9817927
uniprot
proteins
sequence_length
595
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=In a fibroblastic cell line, isoform 1 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia. Colocalizes with MPP1 in non-myelin-forming Schwann cells. Binds with DCAF1 in the nucleus. The intramolecular association of the FERM domain with the C-terminal tail promotes nuclear accumulation. The unphosphorylated form accumulates predominantly in the nucleus while the phosphorylated form is largely confined to the non-nuclear fractions.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 7 is absent from ruffling membranes and filopodia.; SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm, perinuclear region. Cytoplasmic granule. Note=Observed in cytoplasmic granules concentrated in a perinuclear location. Isoform 9 is absent from ruffling membranes and filopodia.; SUBCELLULAR LOCATION: [Isoform 10]: Nucleus. Cell projection, filopodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Cytoplasmic granule. Cytoplasm, cytoskeleton. Note=In a fibroblastic cell line, isoform 10 is found homogeneously distributed over the entire cell, with a particularly strong staining in ruffling membranes and filopodia.
uniprot
proteins